ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q9GZV4 | MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK | Function: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts . Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (By similarity).
PTM: Lys-50 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain and leads to the formation of a hypusine residue. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16793
Sequence Length: 153
Subcellular Location: Cytoplasm
|
Q6IS14 | MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGWPCKIVEMSASKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVPEDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK | Function: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome. Acts as ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity (By similarity).
PTM: Lys-50 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16773
Sequence Length: 154
Subcellular Location: Cytoplasm
|
Q64282 | MGENADGDQVMENLLQLRCHFTWKLLFENNDIPDLEVRISEQVQFLDIKNPLGMHNLLAYVRHLKGQQDEALQSLKEAEALIQSEQLSKRSLATWGNCAWLHYHRGSLAEAQIYLDKVEKVCKEFSSPFRYRLECAEMDCEEGWALLKCGGGNYKQAMACFAKALKVEPENPEYNTGYAVVAYRQDLDDNFISLEPLRKAVRLNPEDPYLKVLLALKLQDLGEHVEAEAHIEEALSSTSCQSYVIRYAAKYFRRKHRVDKALHLLNRALQASPSSGYLHYQKGLCYKQQISQLRTSRNRQPRRQDNVQELAQQAIHEFQETLKLRPTFEMAYVCMAEVQAEIHQYEEAERNFQKALNNKTLVAHIEQDIHLRYGRFLQFHKQSEDKAITLYLKGLKVEEKSFAWRKLLTALEKVAERRVCQNVHLVESTSLLGLVYKLKGQEKNALFYYEKALRLTGEMNPAF | Function: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism).
PTM: Phosphorylated.
Sequence Mass (Da): 53737
Sequence Length: 463
Domain: RNA recognition is mediated by a convoluted intramolecular fold of the TPR repeats (TPR eddy), which scaffolds unique additional helices that form an RNA binding cleft.
Subcellular Location: Cytoplasm
|
Q60462 | MSTTTKKSLESKLQQLKCHFTWNLMAGDESLDEFEDKVFNKDEFQKRECKATMCNILAFVKHRRGQNASALKELEKAEQFIQQQHPDHVEIRNIVTWGNYAWVYYHMGQLEKAQAYLDKVRQVCEKFSSPYRIESPELDCEEGWARLKCTRNQNERVKVCFEKALEKDPKNPEFTSGWAISNYRLDFWPAQQNAVDSLKQAIRMSPNSPYVKVLLALKLEMNQENQGKELVEEALREAPGETDVLRSAARFYYKTHDKDRAIQLLSQALELLPNNAYVYYYIGCFYRSKVLQIDSRRETSQNENREQLLKQAIYYLKKAEETKEMIKDSCSYLAHLYVLAEQYKEADYYFQKGFKKELTPGLKQLLHLRYGNFQFFQMKCEDKAIHQYLEGVKIRQKTKPKEKMTNKLRFIAERRRSQNGFDSKALHILAFLQELNKESQQAAKVSERGQDSERPVFSPSLHEGGNEQ | Function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis (By similarity).
Sequence Mass (Da): 55046
Sequence Length: 468
Domain: The C-terminal part folds into a super-helical structure and has an extensively positively-charged nucleotide-binding channel on its inner surface.
Subcellular Location: Cytoplasm
|
P09913 | MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGE | Function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis.
Sequence Mass (Da): 54632
Sequence Length: 472
Domain: The C-terminal part folds into a super-helical structure and has an extensively positively-charged nucleotide-binding channel on its inner surface.
Subcellular Location: Cytoplasm
|
Q64112 | MSTTSKESLVCNLRQLKCHFTWNLIAEDESLDEFEDRVFNKDEFQNSEFKATMCNILAYVKHCRGLNEAALQCLGEAEGFIQQQHPDQVEIRSLVTWGNYAWVYYHMGQFSKAQAYLDKVKQVCKKFSSPYRIENPALDCEEGWARLKCTKNQNERVKVCFQKALEKDPKNPEFTSGWAIAFYRLDDWPARNYCIDSLEQAIQLSPDNTYVKVLLALKLDAVHVHKNQAMALVEEALKKDPSAIDTLLRAARFYCKVYDTDRAIQLLRKALEKLPNNAYVHYYMGCCYRSKVHHMLNRREMVFSGDRKKLEELIQLAVNHLRKAEEIKEMLEYSCSFLADLYIIAKKYDEADYYFQKELSKDLPPGPKQLLHLRYGNFQFFQMKRQDKAIYHYMEGVKIKKKTIPQKKMREKLQRIALRRLHEDESDSEALHILAFLQENGGGQQADKDSERGVDSANQVPSASLDEDGAEY | Function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis.
Sequence Mass (Da): 55021
Sequence Length: 472
Domain: The C-terminal part folds into a super-helical structure and has an extensively positively-charged nucleotide-binding channel on its inner surface.
Subcellular Location: Cytoplasm
|
Q13325 | MSEIRKDTLKAILLELECHFTWNLLKEDIDLFEVEDTIGQQLEFLTTKSRLALYNLLAYVKHLKGQNKDALECLEQAEEIIQQEHSDKEEVRSLVTWGNYAWVYYHMDQLEEAQKYTGKIGNVCKKLSSPSNYKLECPETDCEKGWALLKFGGKYYQKAKAAFEKALEVEPDNPEFNIGYAITVYRLDDSDREGSVKSFSLGPLRKAVTLNPDNSYIKVFLALKLQDVHAEAEGEKYIEEILDQISSQPYVLRYAAKFYRRKNSWNKALELLKKALEVTPTSSFLHHQMGLCYRAQMIQIKKATHNRPKGKDKLKVDELISSAIFHFKAAMERDSMFAFAYTDLANMYAEGGQYSNAEDIFRKALRLENITDDHKHQIHYHYGRFQEFHRKSENTAIHHYLEALKVKDRSPLRTKLTSALKKLSTKRLCHNALDVQSLSALGFVYKLEGEKRQAAEYYEKAQKIDPENAEFLTALCELRLSI | Function: Interferon-induced RNA-binding protein involved in the human innate immune response. Has a broad and adaptable RNA structure recognition important for RNA recognition specificity in antiviral defense. Binds precursor and processed tRNAs as well as poly-U-tailed tRNA fragments . Specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner . Also recognizes and selectively binds AT-rich dsDNA . Additionally, as a mediator in innate immunity, regulates positively IKK-NFKB signaling by sinergizing the recruitment of IKK to MAP3K7 .
Sequence Mass (Da): 55847
Sequence Length: 482
Domain: RNA recognition is mediated by a convoluted intramolecular fold of the TPR repeats (TPR eddy), which scaffolds unique additional helices that form an RNA binding cleft . Undergoes a conformational change upon RNA-binding: unliganded exists in a more open conformation, facilitating RNA entry .
Subcellular Location: Cell projection
|
Q6K0P9 | MANNYKKIVLLKGLEVINDYHFRIVKSLLSNDLKLNPKMKEEYDKIQIADLMEEKFPGDAGLGKLIEFFKEIPTLGDLAETLKREKLKVANKIESIPVKGIIPSKKTKQKEVYPATPACTPSNRLTAKGAEETLGPQKRKKPSEEETGTKRSKMSKEQTRPSCSAGASTSTAMGRSPPPQTSSSAPPNTSSTESLKPLANRHATASKNIFREDPIIAMVLNATKVFKYESSENEQRRMFHATVATQTQFFHVKVLNINLKRKFIKKRIIIISNYSKRNSLLEVNEASSVSEAGPDQTFEVPKDIIRRAKKIPKINILHKQTSGYIVYGLFMLHTKIVNRKTTIYEIQDKTGSMAVVGKGECHNIPCEKGDKLRLFCFRLRKRENMSKLMSEMHSFIQIQKNTNQRSHDSRSMALPQEQSQHPKPSEASTTLPESHLKTPQMPPTTPSSSSFTKKDETHPGAQSSPANFRITSPTVAPPLSSDTSTNRHPAVP | Function: Major mediator of the tumor suppressor activity of IFN in breast cancer cells. Promotes ubiquitination and subsequent degradation of MDM2, which leads to p53/TP53 stabilization. Promotes ubiquitination and subsequent degradation of HDAC1, which in turn enhances maspin expression, and impairs invasive activity of cancer cells.
Sequence Mass (Da): 55065
Sequence Length: 492
Domain: The HIN-200 domain mediates interaction with MDM2.
Subcellular Location: Nucleus
|
P13164 | MHKEEHEVAVLGPPPSTILPRSTVINIHSETSVPDHVVWSLFNTLFLNWCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTIGFILLLVFGSVTVYHIMLQIIQEKRGY | Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV) . Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV and SARS-CoV-2 S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration . Inhibits SARS-CoV-2 S protein-mediated syncytia formation . Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53-dependent manner. Acts as a positive regulator of osteoblast differentiation. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation . IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome .
PTM: Palmitoylation on membrane-proximal cysteines controls clustering in membrane compartments and antiviral activity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13964
Sequence Length: 125
Subcellular Location: Cell membrane
|
Q9D103 | MPKEQQEVVVLGSPHISTSATATTINMPEISTPDHVVWSLFNTLFMNFCCLGFVAYAYSVKSRDRKMVGDTTGAQAFASTAKCLNISSLFFTILTAIVVIVVCAIR | Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53-dependent manner. Acts as a positive regulator of osteoblast differentiation.
PTM: Palmitoylation on membrane-proximal cysteines controls clustering in membrane compartments and antiviral activity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11524
Sequence Length: 106
Subcellular Location: Cell membrane
|
Q99J93 | MSHNSQAFLSTNAGLPPSYETIKEEYGVTELGEPSNSAVVRTTVINMPREVSVPDHVVWSLFNTLFFNACCLGFVAYAYSVKSRDRKMVGDVVGAQAYASTAKCLNISSLIFSILMVIICIIIFSTTSVVVFQSFAQRTPHSGF | Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner.
PTM: Palmitoylation on membrane-proximal cysteines controls clustering in membrane compartments and antiviral activity.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 15743
Sequence Length: 144
Subcellular Location: Cell membrane
|
Q05688 | NAIFVPRPERKRREVMQIANTTMSSRSRNTTVLDTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTTYENFIHLMIALPIAVLLIVGGLVIMLYVFHRKRNSSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSVKDEMEAGFREVSFYYSEENKPPEPEELDLEPENMESVPLDPSASSASLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALPLPQSSTC | Function: Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R (By similarity). When present in a hybrid receptor with INSR, binds IGF1 (By similarity).
PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner; Tyr-438 is predominantly phosphorylated first, followed by phosphorylation of Tyr-434 and Tyr-439. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-438, Tyr-434 and Tyr-439) have to be phosphorylated for optimal activity. Can be autophosphorylated at additional tyrosine residues (in vitro). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines. Phosphorylation of Tyr-253 is required for IRS1- and SHC1-binding (By similarity). Phosphorylation of Ser-551 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-555. Dephosphorylated by PTPN1 (By similarity).
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 72511
Sequence Length: 640
Subcellular Location: Cell membrane
EC: 2.7.10.1
|
Q29000 | ERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTEPVFFYVQAKTTYENFIHLIIALPVAVLLIVGGLVIMLYVFHRKRNNSRLGNGVMLFELMRMCWQYNPKMRPSFLEIISSIKDEMEPGFREVSFYYSEENKPPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNER | Function: Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R (By similarity). When present in a hybrid receptor with INSR, binds IGF1 (By similarity).
PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop have to be phosphorylated for optimal activity. Can be autophosphorylated at additional tyrosine residues (in vitro). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines (By similarity). Phosphorylation of Ser-225 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-229. Dephosphorylated by PTPN1 (By similarity).
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 34615
Sequence Length: 304
Subcellular Location: Cell membrane
EC: 2.7.10.1
|
Q61730 | MGLLWYLMSLSFYGILQSHASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSAMRFPVHKMYIEHGIHKITCPNVDGYFPSSVKPSVTWYKGCTEIVDFHNVLPEGMNLSFFIPLVSNNGNYTCVVTYPENGRLFHLTRTVTVKVVGSPKDALPPQIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEVWWTIDGKKPDDVTVDITINESVSYSSTEDETRTQILSIKKVTPEDLRRNYVCHARNTKGEAEQAAKVKQKVIPPRYTVELACGFGATVFLVVVLIVVYHVYWLEMVLFYRAHFGTDETILDGKEYDIYVSYARNVEEEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGIVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAVKDMKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRWSSNDKQGLSYSSLKNV | Function: Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Secreted forms (isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and increase the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD . May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (By similarity).
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65741
Sequence Length: 570
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Subcellular Location: Cell membrane
EC: 3.2.2.6
|
P08831 | MAKVPDLFEDLKNCYSENEDYSSEIDHLSLNQKSFYDASYEPLREDQMNKFMSLDTSETSKTSKLSFKENVVMVAASGKILKKRRLSLNQFITDDDLEAIANNTEEEIIKPRSAHYSFQSNVKYNFMRVIHQECILNDALNQSIIRDMSGPYLTATTLNNLEEAVKFDMVAYVSEEDSQLPVTLRISKTQLFVSAQNEDEPVLLKEMPETPKIIKDETNLLFFWEKHGSMDYFKSVAHPKLFIATKQEKLVHMASGPPSITDFQILEK | Function: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity.
PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization.
Sequence Mass (Da): 30833
Sequence Length: 268
Domain: The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function.
Subcellular Location: Nucleus
|
Q60480 | FEDLKNCYSENEEYASAIDHLSLNQKSFYDTNYDPLHENRVDEPVSPNPYENSEESNFTLEDSSDSSAVVLTSAHGEVLKKRRLSLNQTMSNEDLEAIANDSEEEIIEPWSVPYSFQSNLKFKYQRSIKKGAVITDAMHQSLIRESNGQHLKAMHVVDRKHEVKFDIDGYVSTATRIRPVTLKISKTQLYVCAQEEGQPVLLKE | Function: Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells (By similarity).
Sequence Mass (Da): 23333
Sequence Length: 204
Domain: The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function.
Subcellular Location: Cytoplasm
|
P01583 | MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA | Function: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems . After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex . Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4 . In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways . Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage . In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity .
PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization.
Sequence Mass (Da): 30607
Sequence Length: 271
Domain: The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function.
Subcellular Location: Nucleus
|
P18430 | MAKVPDLFEDLKNCYSENEEYSSDIDHLSLNQKSFYDASYEPLPGDGMDKFMPLSTSKTSKTSRLNFKDSVVMAAANGKILKKRRLSLNQFITDDDLEAIANDTEEEIIKPRSATYSFQSNMKYNFMRVINHQCILNDARNQSIIRDPSGQYLMAAVLNNLDEAVKFDMAAYTSNDDSQLPVTLRISETRLFVSAQNEDEPVLLKELPETPKTIKDETSLLFFWEKHGNMDYFKSAAHPKLFIATRQEKLVHMAPGLPSVTDFQILENQS | Function: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity.
PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization.
Sequence Mass (Da): 30789
Sequence Length: 270
Domain: The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function.
Subcellular Location: Nucleus
|
Q8R460 | MFSKHPFSTHISGRETPDFGEVFDLDQQVWIFRNQALVTVPRSHRVTPVSVTILPCKYPESLEQDKGIAIYLGIQNPDKCLFCKEVNGHPTLLLKEEKILDLYHHPEPMKPFLFYHTRTGGTSTFESVAFPGHYIASSKTGNPIFLTSKKGEYYNINFNLDIKS | Function: Functions as an agonist of NF-kappa B activation through the orphan IL-1-receptor-related protein 2/IL1RL2. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP (By similarity). Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. May play a role in pro-inflammatory responses during particular neutrophilic airway inflammation. May be involved in the innate immune response to fungal pathogens. Induces the production of pro-inflammatory cytokines in bone marrow-derived dendritic cells (BMDCs), including IL-12, Il-1 beta, IL-6, TNF-alpha and IL-23. Involved in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II. Induces the production of IFN-gamma, IL-4 and IL-17 by cultured CD4(+) T-cells and splenocytes.
PTM: N-terminal truncation leads to a dramatic enhancement of its activity (>1000-fold) . Proteolytically cleaved by cathepsin CTSG (By similarity).
Sequence Mass (Da): 18733
Sequence Length: 164
Subcellular Location: Cytoplasm
|
Q9NZH6 | MSFVGENSGVKMGSEDWEKDEPQCCLEDPAGSPLEPGPSLPTMNFVHTSPKVKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALASSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAAQKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFENRKHIEFSFQPVCKAEMSPSEVSD | Function: Immune regulatory cytokine that acts as a suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. Signaling can occur via two mechanisms, intracellularly through nuclear translocation with SMAD3 and extracellularly after secretion and binding to its receptor composed of IL18R1 and IL18RAP. Suppresses, or reduces, pro-inflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A and IL1RN, but spares anti-inflammatory cytokines. Inhibits dendritic cell activation.
PTM: Proteolytically converted to the mature form by CASP1.
Sequence Mass (Da): 24126
Sequence Length: 218
Subcellular Location: Cytoplasm
|
P26951 | MVLLWLTLLLIALPCLLQTKEDPNPPITNLRMKAKAQQLTWDLNRNVTDIECVKDADYSMPAVNNSYCQFGAISLCEVTNYTVRVANPPFSTWILFPENSGKPWAGAENLTCWIHDVDFLSCSWAVGPGAPADVQYDLYLNVANRRQQYECLHYKTDAQGTRIGCRFDDISRLSSGSQSSHILVRGRSAAFGIPCTDKFVVFSQIEILTPPNMTAKCNKTHSFMHWKMRSHFNRKFRYELQIQKRMQPVITEQVRDRTSFQLLNPGTYTVQIRARERVYEFLSAWSTPQRFECDQEEGANTRAWRTSLLIALGTLLALVCVFVICRRYLVMQRLFPRIPHMKDPIGDSFQNDKLVVWEAGKAGLEECLVTEVQVVQKT | Function: Cell surface receptor for IL3 expressed on hematopoietic progenitor cells, monocytes and B-lymphocytes that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells . Ligand stimulation rapidly induces hetrodimerization with IL3RB, phosphorylation and enzyme activity of effector proteins such as JAK2 and PI3K that play a role in signaling cell proliferation and differentiation. Activation of JAK2 leads to STAT5-mediated transcriptional program (By similarity).
PTM: Ubiquitinated by RNFT2 in response to IL3. Ubiquitination leads ligand-induced degradation by the proteasome.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43330
Sequence Length: 378
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Membrane
|
P26952 | MAANLWLILGLLASHSSDLAAVREAPPTAVTTPIQNLHIDPAHYTLSWDPAPGADITTGAFCRKGRDIFVWADPGLARCSFQSLSLCHVTNFTVFLGKDRAVAGSIQFPPDDDGDHEAAAQDLRCWVHEGQLSCQWERGPKATGDVHYRMFWRDVRLGPAHNRECPHYHSLDVNTAGPAPHGGHEGCTLDLDTVLGSTPNSPDLVPQVTITVNGSGRAGPVPCMDNTVDLQRAEVLAPPTLTVECNGSEAHARWVARNRFHHGLLGYTLQVNQSSRSEPQEYNVSIPHFWVPNAGAISFRVKSRSEVYPRKLSSWSEAWGLVCPPEVMPVKTALVTSVATVLGAGLVAAGLLLWWRKSLLYRLCPPIPRLRLPLAGEMVVWEPALEDCEVTPVTDA | Function: Cell surface receptor for IL3 expressed on hematopoietic progenitor cells, monocytes and B-lymphocytes that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells (By similarity). Ligand stimulation rapidly induces hetrodimerization with IL3RB, phosphorylation and enzyme activity of effector proteins such as JAK2 and PI3K that play a role in signaling cell proliferation and differentiation . Activation of JAK2 leads to STAT5-mediated transcriptional program .
PTM: Ubiquitinated at Lys-357 by RNFT2 in response to IL3. Ubiquitination leads ligand-induced degradation by the proteasome.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43195
Sequence Length: 396
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Cell membrane
|
P32927 | MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC | Function: Cell surface receptor that plays a role in immune response and controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Acts by forming an heterodimeric receptor through interaction with different partners such as IL3RA, IL5RA or CSF2RA . In turn, participates in various signaling pathways including interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor/CSF2 pathways. In unstimulated conditions, interacts constitutively with JAK1 and ligand binding leads to JAK1 stimulation and subsequent activation of the JAK-STAT pathway .
PTM: May be phosphorylated by LYN.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 97336
Sequence Length: 897
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Membrane
|
Q8S9S4 | MAAASSSRVLLAAVAVLAAALAGCGAGAALDDPAGLLRRAKEAEFAGWMVGLRRRIHENPELGYEEFATSELVRRELDALGIPYRHPFAVTGVVATVGTGGPPFVALRADMDALPMQESVEWEHKSKVPGKMHGCGHDAHVAMLLGSARILQEHRDELKGTVVLVFQPAEEGGGGAKKMIDDGAVENIEAIFGVHVADVVPIGVVASRPGPVMAGSGFFEAVISGKGGHAALPHHTIDPILAASNVIVSLQQLVSREADPLDSQVVTVGKFQGGGAFNVIPDSVTIGGTFRAFLKESFNQLKQRIEEVIVSQASVQRCNAVVDFLDKDRPFFPPTINSAGLHDFFVKVASEMVGPKNVRDKQPLMGAEDFAFYADAIPATYYYFLGMYNETRGPQAPHHSPYFTINEDALPYGAALQASLAARYLLEHQPPTTGKAKAHDEL | Function: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA).
Sequence Mass (Da): 47135
Sequence Length: 442
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.5.1.-
|
O04373 | MSFFKWVSFVLILHLLNPTLISCSSNGLSQIPSKFLTLAKRNDFFDWMVGIRRRIHENPELGYEEVETSKLVRAELEKMGVSYKYPVAVTGVVGYVGTGHAPFVALRADMDALAMQEMVEWEHKSKVPGKMHACGHDAHTTMLLGAAKLLKEHEEELQGTVVLVFQPAEEGGGGAKKIVEAGVLENVSAIFGLHVTNQLALGQVSSREGPMLAGSGFFKAKISGKGGHAALPQHTIDPILAASNVIVSLQHLVSREADPLDSQVVTVAKFEGGGAFNVIPDSVTIGGTFRAFSTKSFMQLKKRIEQVITRQASVNMCNATVDFIEEEKPFFPPTVNDKALHQFFKNVSGDMLGIENYVEMQPLMGSEDFSFYQQAIPGHFSFVGMQNKARSPMASPHSPYFEVNEELLPYGASLHASMATRYLLELKASTLNKSNKKDEL | Cofactor: The Mn(2+) ion enhances activity.
Function: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA), including IAA-Ala, IAA-Asn, IAA-Cys, IAA-Glu, IAA-Met, IAA-Ser and IAA-Gly . Has a lower efficiency with IAA-Phe, IAA-Leu and IAA-Val and no activity with IAA-Ile . Important for IAA-Leu hydrolysis in roots . Also hydrolyzes amino acid conjugates of jasmonic acid and 12-hydroxy jasmonic acid .
Catalytic Activity: a jasmonyl-L-amino acid + H2O = a jasmonate + an L-alpha-amino acid
Sequence Mass (Da): 48263
Sequence Length: 440
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.5.1.-
|
Q8VYX0 | MDNLRKLNLLSVSLTIIFVSLTIATNLPFFEVKYPNNNPFGMLLRPTPIKNQSLGLPAHVGSDECRVWTKACSDEILRLTYQPDNVAWLKRVRRTIHENPELAFEEYETSRLIRSELDRMGIMYRYPLAKTGIRAWIGSGGPPFVAVRADMDALPIQEAVEWEHISKVAGKMHACGHDAHVTMLLGAAHILKAREHLLKGTVVLLFQPAEEAGNGAKNMIEDGALDDVEAIFAVHVSHIHPTGVIGSRSGPLLAGCGIFRAVITSEDSRGAANLLLAASSAVISLQGIVSREASPLDSQVVSVTSFDGGHSLDVAPDTVVLGGTFRAFSNSSFYYLKKRIQEVLMDQVGVFGCQATVNFFEKQNAIYPPTTNNDATYNHLKKVTIDLLGDSHFTLAPQMMGAEDFAFYSEIIPAAFYFIGIRNEELGSVHIAHSPHFMIDEDSLPVGAAVHAAVAERYLNDKHS | Function: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA). Also hydrolyzes amino acid conjugates of jasmonic acid and 12-hydroxy jasmonic acid.
Catalytic Activity: a jasmonyl-L-amino acid + H2O = a jasmonate + an L-alpha-amino acid
Sequence Mass (Da): 50820
Sequence Length: 464
EC: 3.5.1.-
|
Q9FNN3 | MGSNRPKNFRRRGDDGGDEIDGKVATPSSKPTSTLSSSKPKTLSASAPKKKLLSFADDEEEEEDGAPRVTIKPKNGRDRVKSSSRLGVSGSSHRHSSTKERRPASSNVLPQAGSYSKEALLELQKNTRTLPYSRSSANAEPKVVLKGLIKPPQDHEQQSLKDVVKQVSDLDFDEEGEEEQHEDAFADQAAIIRAKKERMRQSRSAPAPDYISLDGGIVNHSAVEGVSDEDADFQGIFVGPRPQKDDKKGVFDFGDENPTAKETTTSSIYEDEDEEDKLWEEEQFKKGIGKRMDEGSHRTVTSNGIGVPLHSKQQTLPQQQPQMYAYHAGTPMPNVSVAPTIGPATSVDTLPMSQQAELAKKALKDNVKKLKESHAKTLSSLTKTDENLTASLMSITALESSLSAAGDKYVFMQKLRDFISVICDFMQNKGSLIEEIEDQMKELNEKHALSILERRIADNNDEMIELGAAVKAAMTVLNKHGSSSSVIAAATGAALAASTSIRQQMNQPVKLDEFGRDENLQKRREVEQRAAARQKRRARFENKRASAMEVDGPSLKIEGESSTDESDTETSAYKETRDSLLQCADKVFSDASEEYSQLSKVKARFERWKRDYSSTYRDAYMSLTVPSIFSPYVRLELLKWDPLHQDVDFFDMKWHGLLFDYGKPEDGDDFAPDDTDANLVPELVEKVAIPILHHQIVRCWDILSTRETRNAVAATSLVTNYVSASSEALAELFAAIRARLVEAIAAISVPTWDPLVLKAVPNTPQVAAYRFGTSVRLMRNICMWKDILALPVLENLALSDLLFGKVLPHVRSIASNIHDAVTRTERIVASLSGVWTGPSVTRTHSRPLQPLVDCTLTLRRILEKRLGSGLDDAETTGLARRLKRILVELHEHDHAREIVRTFNLKEAV | Function: Transcriptional repressor regulating endoreduplication through control of A-type cyclins expression . Does not bind to promoter sequences (in vitro) and may act by interacting with tissue-specific transcription factors . Enhances the endocycle in endoreduplicating cells in seedlings . Required for efficient splicing .
Sequence Mass (Da): 100775
Sequence Length: 908
Domain: The C-terminal region (474-908) is responsible for the repressor activity.
Subcellular Location: Nucleus
|
Q4X099 | MLLSQTRGRLPSTLRSFSRRALSTTLPRGKDSEETALNKVSRNVTQPISQGASQAMLYATGLTEEDMNKAQVGISSVWYNGNPCNMHLLDLSNRVREGVQKAGLVGFQFNTVGVSDAISMGTKGMRYSLQSRDLIADSIETVMGGQWYDANISIPGCDKNMPGVLMAMGRVNRPSLMVYGGTIKPGCARTQNNADIDIVSAFQAYGQFLTGEITENQRFDIIRNACPGGGACGGMYTANTMATAIEVMGMTLPGSSSNPAESKAKDLECLAAGEAIKRLLKEDIRPSDILTRQAFENAMIVVNITGGSTNAVLHLIAIADSVGIKLDIEDFQKVSDRTPFLADLKPSGKYVMADLHNIGGTPSLLKFLLKEGVIDGSGMTVTGETLAKNLEKVPDFPADQKIIRPLSNPIKKTGHIQILRGSLAPGGSVGKITGKEGTRFVGKARVFDDEDDFIAALERNEIKKEEKTVVVIRYTGPKGGPGMPEMLKPSSALMGAGLGSSCALITDGRFSGGSHGFLIGHIVPEAAVGGPIGLVKDGDTITIDAEKRLLDLDVDETELARRRKEWEALRDAGKLPQTGLTMRGTLGKYARTVKDASHGCITDSVE | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to biosynthesis of branched-chain amino acids . Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively (By similarity). IlvC and the branched-chain amino acid biosynthesis are crucial for virulence and may be a potential target to develop antifungal agents .
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 64757
Sequence Length: 606
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
Subcellular Location: Mitochondrion
EC: 4.2.1.9
|
C1DFH7 | MKVYYDKDCDLSIIQSKKVAIIGYGSQGHAHACNLKDSGVDVYVGLRAGSASVAKAEAHGLTVKSVKDAVAAADVVMILTPDEFQGRLYKDEIEPNLKKGATLAFAHGFSIHYNQVVPRADLDVIMIAPKAPGHTVRSEFVRGGGIPDLIAVYQDASGNAKNLALSYACGVGGGRTGIIETTFKDETETDLFGEQAVLCGGCVELVKAGFETLVEAGYAPEMAYFECLHELKLIVDLMFEGGIANMNYSISNNAEYGEYVTGPEVINEQSRQAMRNALKRIQDGEYAKMFITEGAANYPSMTAYRRNNAAHQIEVVGEKLRTMMPWIAANKIVDKTKN | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 36635
Sequence Length: 338
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
|
P37253 | MVKVYYNGDIKENVLAGKTVAVIGYGSQGHAHALNLKESGVDVIVGVRQGKSFTQAQEDGHKVFSVKEAAAQAEIIMVLLPDEQQQKVYEAEIKDELTAGKSLVFAHGFNVHFHQIVPPADVDVFLVAPKGPGHLVRRTYEQGAGVPALFAIYQDVTGEARDKALAYAKGIGGARAGVLETTFKEETETDLFGEQAVLCGGLSALVKAGFETLTEAGYQPELAYFECLHELKLIVDLMYEEGLAGMRYSISDTAQWGDFVSGPRVVDAKVKESMKEVLKDIQNGTFAKEWIVENQVNRPRFNAINASENEHQIEVVGRKLREMMPFVKQGKKKEAVVSVAQN | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 37458
Sequence Length: 342
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
|
Q0BS26 | MRVYYDRDADLNLIKGKKVAVIGYGSQGHAHVLNMRDSGVKDLVVGLRKGSSAVAKAEGEGLKVMEPAEAAAWADVVMILTPDESQADLYREHLHANLRPGAALAFAHGLNIHFNLIEPRSDIDVFMIAPKGPGHTVRGEYQKGGGVPCLVAVAQNASGNALEIALSYASAVGGGRAGIIETTFKEECETDLFGEQAVLCGGLVELIRAGFETLVEAGYAPEMAYFECLHEVKLIVDLIYEGGIANMNYSISNTAEYGEYVTGPRIVTPETKAEMKRVLEDIQSGRFVRDFMLEMKVNGASFKSIRRRNNEHQIEQVGERLRAMMPWIAKGKLVDKARN | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 36997
Sequence Length: 339
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
|
Q5V520 | MSDELTTTVYYDEDADVSTINDETVAVLGYGSQGHAHALNLHESGVDVIVGLRQDSSSWADAEDAGLRVETPDVAAGEADRVVMLVPDTIQPAVYEAIEDELDAGDTLQFAHGFNIHYGQIEPPEDVDVTMVAPKSPGHLVRRTYERGEGTPGLIAVYQDATGNAKQESLAYAKGIGCTRAGVIETSFQEEVETDLFGEQAVLCGGVTEMVKAGFETLVDAGYAPEMAYFECLNELKLIVDLMYEGGHMGMWNSVSDTAEYGGLTRGEEVIDREGMEKILEEVQNGEFAREWINENQANRPAYKQYRDAEQNHQIEAVGENLRELFAWGEDADAETTEAPADD | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 37488
Sequence Length: 343
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
|
Q18GT4 | MTETKTQTETETDEEEGTDTDTALDTTIYYDDDADREYIDDKTVAVLGYGSQGHAHAQNLADSGIDVIVGLYEGSSSRDAARADGLRVETPATAADEADIVSVLVPDTVQPDVFEAIQDGLDAGDTLQFAHGFNIHYNQIQPPADVDVTMVAPKAPGHLVRRNYEAGEGTPGLVAVYQNTTGTARKEAVAYAHAIGCTRAGAIETTFREETETDLFGEQAVLCGGATALVKQGYETLVDAGYSPEMAYFECLNELKLIVDLMYEGGLSEMWNSVSDTAEYGGLTRGNQVIDESVREEMESILEGVQDGTFAREWISENQANRPSYTQLKAAEEAHEIEAVGEPLRDLFAWSDNEETNDESDVVSEPEAAADD | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH
Sequence Mass (Da): 40281
Sequence Length: 372
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
EC: 1.1.1.86
|
Q89HA2 | MKLRCPAAYGTSHVDDANMKKLRSRITTDGLDRAPHRAFMRAMGLDDAAIAKPMVGIVSMKGEQTPCNMTHDFQVAAAKTGIEEAGGTPREFSTVSVSDGISMNHEGMKFSLFSRELIADSIEAVVHGLAYDALIGYGGCDKTLPGVMMGMVRCNVPSIFIYGGSSLPGRVDGRTLTVLDSYEAVGSFMTGEIDSATLERIERACLPTIGACAGQFTANTMGMVSEAMGLTIPNVSMVPGVYAERAQISRRAGRLIMEMLERGGPLPRDIVTRKSLENGAAIVAATGGSTNAALHLPAIANEAGIAFTIDDVGEVFARTPLIGNLRPGGKYTAKDVHDIGGAAVVIQELIRTGHIDGNCITITGRTLAEEYGAANAPDGEVVYAASAPIMPDGGVAVLKGNLCPDGAVIKVAGLKSQFFEGVARVFEDEEACVAAVRDRSYKAGEVLVIRNEGPVGGPGMREMLGVTALIYGQGMGEKVALITDGRFSGATRGMCIGYVSPEAFVGGPLALVRDGDKIRIDATNRRMDMLVDEPELAARRRDWKPRPPRHRAGALAKYARLVGQAPGGAVTHEGPAEWPWFE | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 61528
Sequence Length: 582
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
|
B9DMJ2 | MRSDQIKKGDQQAPARSLLHATGQIKEPTDMNKPFVAICNSYIDIVPGHVHLRELANIAKEAIREAGAIPFEFNTIGVDDGIAMGHIGMRYSLPSREIIADAAETVINAHWFDGVFYIPNCDKITPGMLMAAVRTNVPAIFCSGGPMKAGLSAQGKALTLSSMFEAVGAFKGGSMTQEEFLDMEQNACPTCGSCAGMFTANSMNCLMEVLGLALPYNGTALAVSDQRREMIRQAAFQLVENIKNDLKPRDIVTKEALDDAFALDMAMGGSTNTVLHTLAIANEAGVDYDLKRINEIAKRTPYLSKIAPSSSYSMHDVHEAGGVPAIINELMKKEGTLHPDRVTVTGKTLRENNEGKEIQNEDVIHPLDNPYDKEGGLSILYGNLAPNGAVIKVGGVDPEIKTFKGKAICFDSHDEAVEAIDNHTVREGHVVVIRYEGPKGGPGMPEMLAPTSSIVGRGLGKDVALITDGRFSGATRGIAVGHVSPEAASGGPIGLIHDGDEITIDLTNRTLDVEVSDEVLEQRKSERKPFKAKVKTGYLARYTALVTSANTGGVMKVPEYLIEE | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic Activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O
Sequence Mass (Da): 60590
Sequence Length: 564
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
EC: 4.2.1.9
|
O76357 | MFVKSLVFLTIAVAYASADCLHCICMRESGCKPIGCNMDVGSLSCGYYQIKLPYYEDCGQPTKKSGETTEAAWKRCANDLSCATTCVENYYNRYKSQCAGTGQGACEVMARNHNGGPQGCKHSGTLGYWNGIKSCCGCS | Function: Has bacteriolytic activity against Gram-positive bacteria. Plays a role in defense against bacterial pathogens. Involved in pharyngeal grinder function by enabling proper lysis of ingested bacteria.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 14995
Sequence Length: 139
Subcellular Location: Late endosome lumen
EC: 3.2.1.17
|
Q557F4 | MSSRDKQDSRKKEFKKSLDSETARRKREENSIGIRKNAREELMLKRRGIVQPNPSTSYQIIVPPEVQEQFQKYENETMENKIKNLPGLVTALNSNDQAYVYSSLVQFRKLLSIHAYPPIDQVIECGIIPKLNQLLQCNNPKVQFESAWALTNIASGNNRQTQTVMESGSVPIFIQLLCAETTDEVKEQCAWALGNIAGDTVDSRNYLLKYGAMNALIPLLHYGEDNGATTTSANSERKIGLIQNVVWTISNLCRGKPQPDFSVVSQCLPAINELIRIENLPSEIYGDLCWALSYLCDGPNTKIQAVIDSGVVPRLVKLLEYPDSIVFTPALRAVGNIVTGESSQTQIVIDNNGVELITRLLAVQKKSIRKESCWALSNITAGEPSQIDVVVSNPKTVTTLISLLSHSEHDIKREACWALSNSTNNSSTKSIQTLVRHNILKHFIDLLNSQDLVILKIVLEGLINIIKEGEKTKTKTGVNPYVNLISEMQGESIIYDLQEHQSKDVYKKAFELIEFFESSDYSDSENSEPNINQNGQYEFSSNYNSNSINI | Function: Functions in nuclear protein import via a substrate-importin alpha-beta transport complex that passes though the nuclear pore complexes (NPC). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (By similarity).
Sequence Mass (Da): 61592
Sequence Length: 550
Domain: The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.
Subcellular Location: Cytoplasm
|
Q22560 | MGDEFRPSHEERSKMYKSNVRDQNEMRRKRREDEVQIRKNRRDEKFERNRQITVQRSLSHEETSELLKSVADGLQSMQETTIHEALTVLHENLNNTVWTIHVLVKVQILHKLSDVYCNRVISQTTRLLISRTLLKISGIDEVKYERYSSDDRCIQSLVFNISTYGSSEDILCDTFQSIACFIIRSITYRNLALDCAIVSELIDASTINMSIILHRSLMWLVFLFCEKLDRCSPHVDEIAPLLEIISNGIQSTDAMVQTDAASSCASLAEWPPIYHYMSDLKLCSKLVANLRNDKGNARPKVKAGINSIIQATGYFTEEMIDAGLLEVLKGFVNVSYMSQEVCFIISNICVEGEQTIDKLISSGVLREVARVMEASEYRSRREAAFVICHCCASANQKHLEYVVELGMLSAFTDLLTCMDVSLVSYILDAIYLLLQFGEMRLLPDNSNPVAIKLEEIGCREKLEFLCESQSVDIHARAYTIIDRFYVDDDAPLNDDPFAGYQRNNIDDTIEKMIREPIMDQPFSF | Function: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).
Sequence Mass (Da): 59925
Sequence Length: 524
Domain: Does not contain ARM repeats, but instead Ser charged repeats. May have specificity for cargos distinct from that of other importin alpha subunits.
Subcellular Location: Cytoplasm
|
P52292 | MSTNENANTPAARLHRFKNKGKDSTEMRRRRIEVNVELRKAKKDDQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGRTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSVFRDLVIKYGAVDPLLALLAVPDMSSLACGYLRNLTWTLSNLCRNKNPAPPIDAVEQILPTLVRLLHHDDPEVLADTCWAISYLTDGPNERIGMVVKTGVVPQLVKLLGASELPIVTPALRAIGNIVTGTDEQTQVVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLVPFLVSVLSKADFKTQKEAVWAVTNYTSGGTVEQIVYLVHCGIIEPLMNLLTAKDTKIILVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQNHENESVYKASLSLIEKYFSVEEEEDQNVVPETTSEGYTFQVQDGAPGTFNF | Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Sequence Mass (Da): 57862
Sequence Length: 529
Domain: Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.
Subcellular Location: Cytoplasm
|
P52293 | MSTNENANLPAARLNRFKNKGKDSTEMRRRRIEVNVELRKAKKDEQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVEDIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSAFRDLVIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRLLHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGNIVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLVPFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASLNLIEKYFSVEEEEDQNVVPETTSEGFAFQVQDGAPGTFNF | Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Sequence Mass (Da): 57928
Sequence Length: 529
Domain: Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.
Subcellular Location: Cytoplasm
|
Q02821 | MDNGTDSSTSKFVPEYRRTNFKNKGRFSADELRRRRDTQQVELRKAKRDEALAKRRNFIPPTDGADSDEEDESSVSADQQFYSQLQQELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEMLQLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDYRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIYSMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIVTGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPPLVKLLEVAEYKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEVTLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIETYFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFNFN | Function: Functions in nuclear protein import as an adapter protein for importin beta nuclear receptors . Binds specifically and directly to substrates containing either a simple or bipartite NLS motif . Promotes docking of import substrates to the nuclear envelope . Together with importin beta KAP95, mediates nuclear import of transcription factor GCN4 . Together with tethering factor STS1, targets the proteasome to the nucleus .
Sequence Mass (Da): 60441
Sequence Length: 542
Domain: The NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding.
Subcellular Location: Cytoplasm
|
C5DYQ1 | MLRVLPTSFKSISTRSAFRACQLSPLTVYCPLKSSQGTDIKSLEDLTKLKSLEGVDPELIRKLINERTIELNVQNELEMLKNLNKQEKMSQEVSLKRFVRPLWVFFLMSSTVYLILHYVWWKLEVVEKEKELQSHVESLEMELDQTLKSQNQNVSSSQNNGNNKTNDKPWYRKWFF | Function: Component of the INA complex (INAC) that promotes the biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the assembly of the peripheral stalk and promotes the assembly of the catalytic F(1)-domain with the membrane-embedded F(0)-domain.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20746
Sequence Length: 176
Subcellular Location: Mitochondrion inner membrane
|
P40576 | MFMARQVLRNGLFLRSLAPIKITARTVASANAGIKRKSRFDKTMIKPLLLVMIFGSILNAVIAEKRNIIDMERKYKLKLDKLKELIRRVHDNNGKVDFDADDELKLVNLRLGIVGKNATGMKEDETDIVVPKEESLEEIWQSIIDEAKKEVIEKTPDAGVKNKEGIVTDLNVLKDLEKSKKEDEKVYLSGDVHMMMNQPGDLNEIAKEHDKIPKFL | Function: Component of the INA complex (INAC) that promotes the biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the assembly of the peripheral stalk and promotes the assembly of the catalytic F(1)-domain with the membrane-embedded F(0)-domain.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24597
Sequence Length: 216
Subcellular Location: Mitochondrion inner membrane
|
Q24008 | MVQFLGKQGTAGELIHMVTLDKTGKKSFGICIVRGEVKDSPNTKTTGIFIKGIVPDSPAHLCGRLKVGDRILSLNGKDVRNSTEQAVIDLIKEADFKIELEIQTFDKSDEQQAKSDPRSNGYMQAKNKFNQEQTTNNNASGGQGMGQGQGQGQGMAGMNRQQSMQKRNTTFTASMRQKHSNYADEDDEDTRDMTGRIRTEAGYEIDRASAGNCKLNKQEKDRDKEQEDEFGYTMAKINKRYNMMKDLRRIEVQRDASKPLGLALAGHKDRQKMACFVAGVDPNGALGSVDIKPGDEIVEVNGNVLKNRCHLNASAVFKNVDGDKLVMITSRRKPNDEGMCVKPIKKFPTASDETKFIFDQFPKARTVQVRKEGFLGIMVIYGKHAEVGSGIFISDLREGSNAELAGVKVGDMLLAVNQDVTLESNYDDATGLLKRAEGVVTMILLTLKSEEAIKAEKAAEEKKKEEAKKEEEKPQEPATAEIKPNKKILIELKVEKKPMGVIVCGGKNNHVTTGCVITHVYPEGQVAADKRLKIFDHICDINGTPIHVGSMTTLKVHQLFHTTYEKAVTLTVFRADPPELEKFNVDLMKKAGKELGLSLSPNEIGCTIADLIQGQYPEIDSKLQRGDIITKFNGDALEGLPFQVCYALFKGANGKVSMEVTRPKPTLRTEAPKA | Function: Involved in the negative feedback regulation of the light-activated signaling cascade in photoreceptors through a calcium-mediated process. Interacts with tetrapeptide ligand located in C-terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototransduction complex.
PTM: Phosphorylated by inaC.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74332
Sequence Length: 674
Domain: Second PDZ domain is a type I PDZ domain that tethers type I PDZ ligand inaC by interaction with its C-terminus.
Subcellular Location: Cell membrane
|
P17181 | MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV | Function: Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) . Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response . Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another . The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors . STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes . Can also act independently of IFNAR2: form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity).
PTM: Ubiquitinated, leading to its internalization and degradation . Polyubiquitinated via 'Lys-48'-linked and 'Lys-63'-linked ubiquitin chains, leading to receptor internalization and lysosomal degradation . The 'Lys-63'-linked ubiquitin chains are cleaved off by the BRISC complex .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63525
Sequence Length: 557
Subcellular Location: Cell membrane
|
Q8I3Y8 | METYKGIQFFSNKGTVKNAFKKSNLGYEVMLDRKEDENFIYSNYEHVETQVEKDSKGMVVCKKYKNTYEILVEKVKEKRLGVLLVGIGGNNATTMLGGICANAKDLSYMNKCDLKRSNYLGSVFLSSNIRLGYNEKDKEHAYAPIYKLIDIYNPENIVYGGWDINNMNLKDCLVRNKVFDNEVIEKIKDDLDYVPLKSVYFKGNFIAGNQQRRVNNILYGKNKLEILEQVREQIRNFKKQNNLNELIVLWSGNTEKNIPHIPGVNDTFLNILHACKKNHESVSPSVIYALAAILENSPFINSSPQNTLVSAVVQLAQQKGIFIIGNDLKTGQTKIKNFLLDFYFGTGLKPKSIVSYNHLGNNDGKNLSSDLQFYSKKVSKSNLICDYVRANENLYVDDEKDTNVLVKKSIDYCEGDSLNEKGKVSADIEDDCTYVESLEKQKVNSEIVIKYVPYVGDDKKAIDEYISEIFMNGKNTIVLYNICQDSMLASPILIDLILLVELSQRVFFKPNQEKKTNEDEHLLNENIQIEDYKLSHTILKPKYSSFKNLDSVLFLSSLFCKSPFNSTVYKTRHSFFSQLESLWNFVRIISGLPIDAHIDLPYMI | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (By similarity). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). De novo-synthesized myo-inositol is essential for incorporation into GPI (glycosylphosphatidylinositol) glycolipids during intra-erythrocytic development .
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 69112
Sequence Length: 604
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
EC: 5.5.1.4
|
Q6AYK3 | MEPAAEILVDSPDVIFGPEAIEARYEYRTTRVSREGGVLRVRPTATRFTFRTARQVPRLGVMLVGWGGNNGSTLTAAVLANRLRLTWPTRTGRKEANYYGSLTQAGTVNLGLDGDGREVFVPFSALLPMVAPNDLVFDGWDISSLNLAEAMRRAQVLDCGLQEQLWPHMESLRPRPSVYIPEFIAANQTARADNLIPGTRAQQLEQIRKDIRDFRSSAGLDKVIVLWTANTERFCEVVPGRNDTAENLLRTIQLGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELASQRHVFVGGDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGQNLSAPLQFRSKEVTKSSVVDDMVQSNRVLYAPGEEPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCEDSLLAAPIMLDLVLLTELCQRVSFCTDSDPEPQGFHPVLSVLSFLFKAPLVPPGSPVVNALFRQRSCIENIFRACVGLPPQNHMLLEHKMERPFPGIKPEEVKATSPLPCKKESTPATNGCTGDANGHTQAPTPELSTA | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
PTM: Phosphorylation at Ser-524 does not appear to affect enzyme activity, and is detected in brain and testis.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 60884
Sequence Length: 557
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
|
P42803 | MFIEKFRVESPNVKYGDGEIESVYSYETTELVHEVRNGSYQWVVKPKSVQYQFKTDTRVPRLGVMLVGWGGNNGSTLTAGVIANREGISWVTKEKVQQANYFGSLTQSSSIRVGSFNGEEIYAPFKSLLPMVNPDEIVFGGWDISDMNLADAMGRAKVLDIDLQKQLRPYMESMVPLPGIYNPDFIAANQGSRANNVIKGPKKQQVQRIIDDIREFKEREKVEKVVVLWTANTERYSDLVVGLNDTMENLLAAVERDEAEISPSSLYALACIMEGVPFVNGSPQNTFVPGLIEMAIKRNSLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQTFRSKEISKSNVVDDMVSSNGILYEPGEHPDHVIVIKYVPYVGDSKRAMDEYTSEIFMGGKSTIILHNTCEDSLLAAPIILDLVLLAELSTRIQLKAEGESKFHSFHPVASILSYLSKAPLVPPGTPVVNALSKQRAMLENILRACVGLAPENNMILEYK | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 56386
Sequence Length: 510
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
|
Q5QQ46 | MPAVRTKSGHGVEYTDEAITATYSYNTTRVEKEANGDVTVQPIQLHLKFRTQRKVQRTGVMLIGWGGNNGTTVTAALMAHKHRXSWRTKTGTKQPDYLGSITQSSTMSVGLTSEMEEVFVPMKALVPMINPAELVIGGWDCSGMNIADAMRRAQVLDVTLQDALYNYLKDMHPLPAAFDLDFVAENQLSRADNIMQTKNKWESVEQLRADIRNFREKNSLEEVIVLWTANTERFSEHITGVHDTADHLIDAIRRNENEIAPSVLYATAAIMEGCSYVNGAPQNTLCAGLIELARRHGVFVVGDDFKSGQTKVKSGLVEFFMDAGIKPECIASYNHLGNNDGYNLAAPKQFRSKEVTKGGVLDDMVSSNSILYPPGSRGPDHCIVIKYLPYVGDSKRALDEYNFSIFMGGEQTVVLHNTCQDSLLAAPLIIDLVVLTELMHRVTVTQCDGEDCCDKKEKMTSYTHMETVLSLLSYLLKAPRVPEGTPVVNGLNRQGQAIKNVLRALVGLPPDNNMQLECRLPFLRGVGS | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). De novo-synthesized myo-inositol is essential for incorporation into GPI (glycosylphosphatidylinositol) glycolipids in the bloodstream form .
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 58400
Sequence Length: 528
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
|
P11986 | MTEDNIAPITSVKVVTDKCTYKDNELLTKYSYENAVVTKTASGRFDVTPTVQDYVFKLDLKKPEKLGIMLIGLGGNNGSTLVASVLANKHNVEFQTKEGVKQPNYFGSMTQCSTLKLGIDAEGNDVYAPFNSLLPMVSPNDFVVSGWDINNADLYEAMQRSQVLEYDLQQRLKAKMSLVKPLPSIYYPDFIAANQDERANNCINLDEKGNVTTRGKWTHLQRIRRDIQNFKEENALDKVIVLWTANTERYVEVSPGVNDTMENLLQSIKNDHEEIAPSTIFAAASILEGVPYINGSPQNTFVPGLVQLAEHEGTFIAGDDLKSGQTKLKSVLAQFLVDAGIKPVSIASYNHLGNNDGYNLSAPKQFRSKEISKSSVIDDIIASNDILYNDKLGKKVDHCIVIKYMKPVGDSKVAMDEYYSELMLGGHNRISIHNVCEDSLLATPLIIDLLVMTEFCTRVSYKKVDPVKEDAGKFENFYPVLTFLSYWLKAPLTRPGFHPVNGLNKQRTALENFLRLLIGLPSQNELRFEERLL | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (Ref.6, Ref.8, PubMed:23902760, PubMed:14684747). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
PTM: Phosphorylation at Ser-184 and Ser-374 is associated with a decrease in activity . Increasingly phosphorylated in presence of valproate .
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 59642
Sequence Length: 533
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
|
Q38862 | MFIESFKVESPNVKYTENEINSVYDYETTEVVHENRNGTYQWVVKPKTVKYDFKTDTRVPKLGVMLVGWGGNNGSTLTAGVIANKEGISWATKDKVQQANYFGSLTQASSIRVGSYNGEEIYAPFKSLLPMVNPEDVVFGGWDISDMNLADAMARARVLDIDLQKQLRPYMENMIPLPGIYDPDFIAANQGSRANSVIKGTKKEQVDHIIKDMREFKEKNKVDKLVVLWTANTERYSNVIVGLNDTTENLLASVEKDESEISPSTLYAIACVLEGIPFINGSPQNTFVPGLIELAISKNCLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQTFRSKEISKSNVVDDMVASNGILFEPGEHPDHVVVIKYVPYVADSKRAMDEYTSEIFMGGRNTIVLHNTCEDSLLAAPIILDLVLLAELSTRIQFKAEGEGKFHSFHPVATILSYLTKAPLVPPGTPVVNALSKQRAMLENILRACVGLAPENNMIMEYK | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 56337
Sequence Length: 510
Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular Location: Cytoplasm
EC: 5.5.1.4
|
Q9Y5U4 | MAEGETESPGPKKCGPYISSVTSQSVNLMIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVIASIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNIQLSLTLAALSIGLWWTFDRSRSGFGLGVGIAFLATVVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE | Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR . Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 . Binds oxysterol, including 22-hydroxycholesterol, 24-hydroxycholesterol, 25-hydroxycholesterol and 27-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum . In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi . Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG2 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2 . Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase RNF139 .
PTM: Phosphorylation at Ser-151 by PCK1 reduces binding to oxysterol, disrupting the interaction between INSIG2 and SCAP, thereby promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24778
Sequence Length: 225
Domain: Binds oxysterols in a pocket within their transmembrane domains and interacts with SCAP via transmembrane domains 3 and 4.
Subcellular Location: Endoplasmic reticulum membrane
|
Q91WG1 | MAEGETESPRPKKCGPYISSVTSQSVNVVIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVITSIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNFQFSLTLAALSVGLWWTFDRSRSGFGLGVGIAFLATVVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE | Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR . Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 . Binds oxysterol, including 22-hydroxycholesterol, 24-hydroxycholesterol, 25-hydroxycholesterol and 27-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum (By similarity). In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi (By similarity). Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG2 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2 (By similarity). Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase RNF139 (By similarity).
PTM: Phosphorylation at Ser-151 by PCK1 reduces binding to oxysterol, disrupting the interaction between INSIG2 and SCAP, thereby promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24915
Sequence Length: 225
Domain: Binds oxysterols in a pocket within their transmembrane domains and interacts with SCAP via transmembrane domains 3 and 4.
Subcellular Location: Endoplasmic reticulum membrane
|
Q80UA9 | MAEGETESPRPKKRGPYISSVTSQSVNVVIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVITSIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNFQFSLTLAALSVGLWWTFDRSRSGFGLGVGIAFLATVVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE | Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Binds oxysterol, including 22-hydroxycholesterol, 24-hydroxycholesterol, 25-hydroxycholesterol and 27-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi. Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG2 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2. Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase RNF139.
PTM: Phosphorylation at Ser-151 by PCK1 reduces binding to oxysterol, disrupting the interaction between INSIG2 and SCAP, thereby promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24968
Sequence Length: 225
Domain: Binds oxysterols in a pocket within their transmembrane domains and interacts with SCAP via transmembrane domains 3 and 4.
Subcellular Location: Endoplasmic reticulum membrane
|
A1T557 | MRLRISEAVVLFLLGAVAALIGDHSHVVTGTTVYHTDAVPFVWSSPFWFPILVGAATASLAELRLHLPAPRDGVTARQALGGVAAVVGTYVTTALVHAFPVVPVTALVCAAAAITWCVLGDGPGAACGVVIAVIGPAVEIALVQLGVFAYHPDSDGLFGVAPFLAPLYFAFGVVAALLGELAVARRPQLGPPVCDTVSRGPGAG | Function: Diacylglycerol-binding protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20710
Sequence Length: 204
Domain: The KxHxx motif mediates association with the coatomer complex.
Subcellular Location: Membrane
|
O23492 | MVEGGIAKADKTEFTECWRTTWKTPYIMRLALSAGIGGLLFGYDTGVISGALLFIKEDFDEVDKKTWLQSTIVSMAVAGAIVGAAVGGWINDKFGRRMSILIADVLFLIGAIVMAFAPAPWVIIVGRIFVGFGVGMASMTSPLYISEASPARIRGALVSTNGLLITGGQFFSYLINLAFVHTPGTWRWMLGVAGVPAIVQFVLMLSLPESPRWLYRKDRIAESRAILERIYPADEVEAEMEALKLSVEAEKADEAIIGDSFSAKLKGAFGNPVVRRGLAAGITVQVAQQFVGINTVMYYSPSIVQFAGYASNKTAMALSLITSGLNALGSIVSMMFVDRYGRRKLMIISMFGIIACLIILATVFSQAAIHAPKIDAFESRTFAPNATCSAYAPLAAENAPPSRWNCMKCLRSECGFCASGVQPYAPGACVVLSDDMKATCSSRGRTFFKDGCPSKFGFLAIVFLGLYIVVYAPGMGTVPWIVNSEIYPLRYRGLGGGIAAVSNWVSNLIVSESFLSLTHALGSSGTFLLFAGFSTIGLFFIWLLVPETKGLQFEEVEKLLEVGFKPSLLRRREKKGKEVDAA | Function: Plasma membrane inositol-proton symporter. Mediates high-affinity myoinositol-proton symport across the plasma membrane. Active with myoinositol, scylloinositol and D-chiroinositol. Low activity with mucoinositol and alloinositol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62892
Sequence Length: 582
Domain: The C-terminal domain (546-582) is required for plasma membrane targeting.
Subcellular Location: Cell membrane
|
Q9VFS6 | MLRQNLLDQLKHFIETVSNGHSCPQLLTSPNLIKLALGFLEELPATRDIVFEYFALLAEISVQLYVSPEMADPKTGMPVSQVKLAGNRQQQQRAPEYEAFNLVKTALQSLVWKGPPAWSPLIANWSLELVAKLSDKYTQRRMTITASCNYWLECSAMHGLMTLINSCFRKLTQPEEEACVEIMLNAFHRFPMTFDWIVARLGGCFPYKIIMQILQCGIKRFVDDYRCHLDSEAGILDYMTSCHEQHLRAAFREMLREGFAPKKPLDVAVVPFLLITTNYSDTILQSLVNVLVEIYTEDMCEVIVQKAPLWLSNKMFAGMQPTLNNAVLRLNERGATLLLTAAKMAEKYVWCQDFLDNSMQELEQWVLNQRNFPLLADLAYEETKYMLWKSCLSTNLFEQQTAVRLLLVVSSQHPNIYYQTISQLLKKSYAQNPNGIGALIRLLGGQSGMVNFPGFTPGFKMVLEDITLDVQVNNRLPVPPGTPTEAFNTFSNLNILARMHKSKNVAPYIKAQHLNQALNECLPKILQIFDCTVNKLVLRIDRDAAERIADKFRAQQSKNSNNNNELCNGKDYGKRTKLEPGEDKVDDEDATRMRLAHLIVDLLNNIEAGSRTTVLRTPLVLKLATLSVKYFFVGLTEKTVIRRAAASHRSYTLLQRQCSARKIARTVCLRELVERALFYHGHLLGQLEVYQLDELEIPEHEHLILQNLHTSSGANSNRSVLHSGIIGRGLRPVLPPSERNCDAEKQALYLKALNACCADLEKPNNVEGYSLVSLLLVELVSTDVMYNGLPFPDEEFTRVTMERDMLIRRAFINSPVLWAVLGLIAGHRPALCYSSVLLRALCATCLHHWRGKNVNRFQPTAANDELMLCTKKMLQLLAMSQLIPPPLTNLHLIIEHFESAEIALLLRECIWNYLKDHVPSPALFHVDNNGLHWRNTNTQLAKVPPQYVDPLRHLMQRKLSTLGPHYHQMFIMGELMEGDSEPDPTARLQIVEID | Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing . Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 . May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 112972
Sequence Length: 994
Subcellular Location: Nucleus membrane
|
Q6P9B9 | MSALCDPPGAPGPPGPAPATHGPAPLSAQELSQEIKAFLTGVDPILGHQLSAREHARCGLLLLRSLPPARAAVLDHLRGVFDESVRAHLAALDETPVAGPPHLRPPPPSHVPAGGPGLEDVVQEVQQVLSEFIRANPKAWAPVISAWSIDLMGQLSSTYSGQHQRVPHATGALNELLQLWMGCRATRTLMDIYVQCLSALIGSCPDACVDALLDTSVQHSPHFDWVVAHIGSSFPGTIISRVLSCGLKDFCVHGGAGGGAGSSGGSSSQTPSTDPFPGSPAIPAEKRVPKIASVVGILGHLASRHGDSIRRELLRMFHDSLAGGSGGRSGDPSLQATVPFLLQLAVMSPALLGTVSGELVDCLKPPAVLSQLQQHLQGFPREELDNMLNLAVHLVSQASGAGAYRLLQFLVDTAMPASVITTQGLAVPDTVREACDRLIQLLLLHLQKLVHHRGGSPGEGVLGPPPPPRLVPFLDALKNHVGELCGETLRLERKRFLWQHQLLGLLSVYTRPSCGPEALGHLLSRARSPEELSLATQLYAGLVVSLSGLLPLAFRSCLARVHAGTLQPPFTARFLRNLALLVGWEQQGGEGPAALGAHFGESASAHLSDLAPLLLHPEEEVAEAAASLLAICPFPSEALSPSQLLGLVRAGVHRFFASLRLHGPPGVASACQLLTRLSQTSPAGLKAVLQLLVEGALHRGNTELFGGQVDGDNETLSVVSASLASASLLDTNRRHTAAVPGPGGIWSVFHAGVIGRGLKPPKFVQSRNQQEVIYNTQSLLSLLVHCCSAPGGTECGECWGAPILSPEAAKAVAVTLVESVCPDAAGAELAWPPEEHARATVERDLRIGRRFREQPLLFELLKLVAAAPPALCYCSVLLRGLLAALLGHWEASRHPDTTHSPWHLEASCTLVAVMAEGSLLPPALGNMHEVFSQLAPFEVRLLLLSVWGFLREHGPLPQKFIFQSERGRFIRDFSREGGGEGGPHLAVLHSVLHRNIDRLGLFSGRFQAPSPSTLLRQGT | Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107995
Sequence Length: 1019
Subcellular Location: Nucleus membrane
|
Q8UVX8 | MGLLSVDLLITLQILPWFFSNCLFLALYDSVVLLKHVILLLSCSKSSRGEWRRMLTSEGLRTVWNSFLLDAYKQVKLGGDAPNSKVVRVTSGCCRRRSFSGKGESECHLLDFASSNRPLVVNFGSATUPPFISQLPTFRKLVEEFSDVADFLLVYIDEAHPADGWAAPGVATKSFEVKKHRSQEERCVAAHKLLEHFSLPPQCQVVADCMDNNTNVAYGVSFERVCIVQRQKIAYLGGKGPFFYNLKEVRHWLEQTYRKRUVPTCELIM | Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine).
Catalytic Activity: 3,3',5-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-thyroxine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30513
Sequence Length: 269
Subcellular Location: Membrane
EC: 1.21.99.4
|
P70551 | MGLLSVDLLITLQILPVFFSNCLFLALYDSVILLKHVALLLSRSKSTRGEWRRMLTSEGLRCVWNSFLLDAYKQVKLGEDAPNSSVVHVSNPEAGNNCASEKTADGAECHLLDFASAERPLVVNFGSATUPPFTRQLPAFRQLVEEFSSVADFLLVYIDEAHPSDGWAVPGDSSMSFEVKKHRNQEDRCAAAHQLLERFSLPPQCQVVADRMDNNANVAYGVAFERVCIVQRRKIAYLGGKGPFSYNLQEVRSWLEKNFSKRUILD | Function: Catalyzes the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development.
PTM: Ubiquitinated by MARCHF6, leading to its degradation by the proteasome. Deubiquitinated by USP20 and USP33 (By similarity).
Location Topology: Single-pass membrane protein
Catalytic Activity: 3,3',5-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-thyroxine
Sequence Mass (Da): 29871
Sequence Length: 266
Subcellular Location: Membrane
EC: 1.21.99.4
|
P55073 | MPRQATSRLVVGEGEGSQGASGPAATMLRSLLLHSLRLCAQTASCLVLFPRFLGTAFMLWLLDFLCIRKHFLGRRRRGQPEPEVELNSEGEEVPPDDPPICVSDDNRLCTLASLKAVWHGQKLDFFKQAHEGGPAPNSEVVLPDGFQSQHILDYAQGNRPLVLNFGSCTUPPFMARMSAFQRLVTKYQRDVDFLIIYIEEAHPSDGWVTTDSPYIIPQHRSLEDRVSAARVLQQGAPGCALVLDTMANSSSSAYGAYFERLYVIQSGTIMYQGGRGPDGYQVSELRTWLERYDEQLHGARPRRV | Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing premature exposure of developing fetal tissues to adult levels of thyroid hormones. Can regulate circulating fetal thyroid hormone concentrations throughout gestation. Essential role for regulation of thyroid hormone inactivation during embryological development.
Catalytic Activity: 3,3',5'-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-thyroxine
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33947
Sequence Length: 304
Subcellular Location: Cell membrane
EC: 1.21.99.3
|
P49898 | MLPAPHTCCRLLQQLLACCLLLPRFLLTVLLLWLLDFPCVRRRVIRGAKEEDPGAPEREDPPLCVSDTNRMCTLESLKAVWYGQKLDFFKSAHLGGGAPNTEVVTLEGQRLCRILDFSKGHRPLVLNFGSCTUPPFMARLQAYQRLAAQRLDFADFLLVYIEEAHPCDGWLSTDAAYQIPTHQCLQDRLRAAQLMLQGAPGCRVVADTMTNASNAAYGAYFERLYVILDGKVVYQGGRGPEGYKIGELRNWLDQYQTRATGNGALVIQV | Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). May play a major role in regulating intracellular T3 levels in developing tadpoles.
Catalytic Activity: 3,3',5'-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-thyroxine
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 30140
Sequence Length: 269
Subcellular Location: Cell membrane
EC: 1.21.99.3
|
Q6U6H1 | MHNLLEIKIIRFLRNVFYFLHVLFNECLDTLKAYYKRWRGMKSEKPLDPSSRRARIIQATGVDLSRDPAMQSLRGVYHMAKSILYADVLRTAVRGGNAPNSSLVNYRTKEKCNILDFMKPGRPLVVNFGSCSUPPFMASFEIFSRIIDSYHERADFLTVYIEEAHSSDLWALKNNKYSIPSHITFEDRMEAAAIFKKSVSFECAFAVDTMKDETNLSYGALPERTAIILDGKVQYIGGIGPFNYDLVELEKELIAVLKK | Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Can also produce 3,3'-diiodothyronine from reverse T3 (rT3, 3,3',5'-triiodothyronine). Does not have significant inner-ring deiodination activity for T4, T3 or rT3.
Catalytic Activity: 3,3',5-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-thyroxine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29676
Sequence Length: 259
Subcellular Location: Membrane
EC: 1.21.99.4
|
Q8NTY7 | MSKSLRVGVVGAGAMGADHIDRINNRTSGAHISAIIEPDAARAAAAAEDAPGAQAFTRIEDAIAADAVDAVLIAVPGQFHEPVLVPALEAGLPILCEKPLTPDSESSLRIVELEQKLDKPHIQVGFMRRFDPEYNNLRKLVESGEAGELLMLRGLHRNPSVGESYTQSMLITDSVVHEFDVIPWLAGSRVVSVEVKYPKTSSLAHSGLKEPILVIMELENGVLVDVEMNVNIQFGYQVATEAVFEKGLARIGQPSGMQRWRDGEFLINEHTDFTTRFATAYDRQIQSWVDAVHEGTLVAGPNAWDGYLVALSCEAGVKALDGGVIPVDAAPRPDFYA | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 36431
Sequence Length: 337
EC: 1.1.1.18
|
A6WFC5 | MRVAVLGVGMMGQDHARRLATLTKGAQLVAVSDVDAARTDAVAAELGVRAVHDPAAAIADPEVDAVVIATPGFTHEGLVLEAIAAGKPTLCEKPLTTSPETARAVVEAERALGRPLVQVGFMRRFDAEYEQLRALVASRELGRPLFLHCVHRNATTPPNFNSEMLILDSVVHEVDIARFLLGEEITAITVLTPGRTAHAPEGLQDPQFVLMETASGTLVDVEIFVNTTFGYEVRTELVAERGSAMTGLGVGLVQHSAAGWGGRIAADFKQRFGAAYDTEFQRWVDAVRSGAGVDGPGVWDGYAAAAVCAAGVQSLRTGRRVEVDLGARS | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 34862
Sequence Length: 329
EC: 1.1.1.18
|
A5YBJ7 | MVVKVGVIGTGAMGRAHIDRLTNVLTGAEVVAVTDIDHEAAEAAVRDFHLNAKVYPDDTSLLQDPDIDAVFVVSFGGAHEATVLKALDTDKFIFTEKPLATTLEGAKRIVDKELTKSKKVIQVGFMRRYDQGIRALKEKLDTGIIGAPLVVRASHINPNVASNYSNEMAITDTLIHEIDEMHWLLDDEYTSIQITYPRQSAEVRNEGLHDPQLATLTTKKGTVIQVLVHVTAQYGYEVKLEVIGETGELQLPNYGLGPILRSNANQQTAVEMSWINRFIQAYNTEVQEFIDQVAKSEPPVGPSAWDGYIAAITAAAANRSQKDQETVLINVAGTPTFYQNKNAIHA | Function: Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively.
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 37964
Sequence Length: 346
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 1/7.
EC: 1.1.1.18
|
Q88S38 | MAEAHVTKVGIVGIGFIGSDHLHRLTKTVANVDVTAVCDIVPGKAQKALDQQGLTATTYEDYHDLVNDPNVEVVVCTANNEAHYEIVMAALKAGKFTFCEKPLALDAKQCMDIIDSEKKLGRRMLQVGFMRHYAPEYVQMKKMIDDGVIGKPLMMDQRHYNQTQPEEYDSSRSIIETAIHEIDIDHWLVNDDYANIRVFSPKQTRHVQNAKIQDPQIVMIETKSGINIINEVFVRCQYGYDIKCDVIGEEGVLELPTVPQVATRLNAQYSTAILTDWKARFESAYDIEFRDFINHVSQNESPVGPSAWDGYIAAVTADAALKSLAEDGAKQDLDFPSTPAFYTESEKVSE | Function: Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively.
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 39180
Sequence Length: 350
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 1/7.
EC: 1.1.1.18
|
Q6WAU1 | MAEVQRYALVTGANKGIGFEICRQLAEKGIIVILTSRNEKRGLEARQKLLKELNVSENRLVFHQLDVTDLASVAAVAVFIKSKFGKLDILVNNAGVSGVEMVGDVSVFNEYIEADFKALQALEAGAKEEPPFKPKANGEMIEKFEGAKDCVVTNYYGPKRLTQALIPLLQLSPSPRIVNVSSSFGSLLLLWNEWAKGVLGDEDRLTEERVDEVVEVFLKDIKEGKLEESQWPPHFAAERVSKAALNAYTKIAAKKYPSFRINAICPGYAKTDITFHAGPLSVAEAAQVPVKLALLPDGGPSGCFFPRDKALALY | Function: Monoterpene synthase that catalyzes the specific reduction of the 1(2)-double bond of (-)-isopiperitenone to produce (+)-cis-isopulegone. Does not catalyze the reverse reaction. Unable to reduce (+)-pulegone, (+)-cis-isopulegone, (-)-menthone or the 1,2-double bond of (-)-carvone. Able to utilize NADH with 20% the efficiency of NADPH.
Catalytic Activity: (2R,5R)-isopulegone + NADP(+) = (6R)-isopiperitenone + H(+) + NADPH
Sequence Mass (Da): 34410
Sequence Length: 314
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.3.1.82
|
Q75EW5 | MVKIIGKGGANYVLAFGNDNDDLYRICVRGRSLRENNRSTVDNYHYALEVVKPQLGEFVCRMELVDLPVCDSLRQVLKSKIEVWDATTVTCLKMPNLVPAGSLSHTVDHFTKIHIGERAIVWEFKPKWLSGNDKYCRNCTLNLLRGQTSISYCHAQLLNPGQAGPILKSLFAGLNVPPAFIEDMEAYIAQPCSVLQRLRVAQEQVDASLGPLDQPDTAASPERCLSMTLKDVSCFVSWHKDASPVAVVVDLDMKPAAKSAHWTALQEQLDRFQPQVRH | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 31047
Sequence Length: 278
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Subcellular Location: Nucleus
EC: 2.7.1.158
|
Q59KN8 | MEISKITSPEDWEYFAKGAANILFKYTGNNDYLKRKLLRLRLLKQEEEYISTCELYDFIELRCKDLFPNQIIDIQLTVLDSNFTNKLNSQGNKLMLNERYGLLLPNILDGDYRKISLSQKCQLYFNDNDQDINSVIFEIKPKWLYDNYTDNYCRTCSLNQLKKVPRHFCPLDLLYTETIEQGLNDLFAPIPQDIYAKIEKLIPLKKLTTIYFNNPDNVFQKLKQYQKINNKNDLIKNLTSYSDVSQNLSLVMTLRDVGLFIKIEKFDKNNHIHTSHNNIKNVYRINDNKSNGTKDQDQEIGTNDEEDNDEKFLITCNIYDLDLKSKMKYKHWLKVENDLQEIYNSSNPNWRYCIKYDQIHH | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 42920
Sequence Length: 361
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Subcellular Location: Nucleus
EC: 2.7.1.158
|
Q6FRN1 | MLVAEGGANILLELDHRGVLYRCNVRDKSLKVNNEYTYKNYRYINQVVRPLLGDCIPEMELVDIPYDRISGIIGDFVGDPDSDHVSALTIKNLRPTNVYGEKIRYDDHFTKVYHDDTMEHILVEIKPKWLHHAKFCRNCTHNNLKNRKIPYCYALMVVDPSHVSDMLLHTGIAFPRKFLIKFVDYFSKSDNILAKLHDIQKNLDSNVSMNDIKSIDDVSDAFLLNMTLKDVSCFIEWTREPDSLEVNVVDVDMKLVSKLDHWVNTHIQLSNSSNLVHH | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 32200
Sequence Length: 278
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Subcellular Location: Nucleus
EC: 2.7.1.158
|
Q6CNG8 | MTLLFVGRGNANVCYLLSGEVYRISLRHQKLSRNNAYVQDNFQFIDSKIRSLPMLADVVVSMRLEEVFVDTKWINVLKDENILIDDSHMQCIVMPLLHAKDSTCEQLDHFNQIYRCSLNDAITWEFKPKWLYQSSDYCRNCTHNSLKGRDIEYCFLHDPELIIETLFAGRQVPEEFLDDILQYLQSSDSITQRLYAAQRFVKDDLSTLMTLRDVTCFLTWSRNTRSVKATIIDVDQKPANKLRHWQSTESALASFPGKKKAHFNHQ | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 31066
Sequence Length: 266
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Subcellular Location: Nucleus
EC: 2.7.1.158
|
B8AVX5 | MEVVLHEGDAKDWVYKGEGAANLILSYTGSSPSMLGKVLRVKKILKDKGQPAPNCIVFSSHEEHLWGKIPGLLESVKNDCLPQAYATIVMSQHLGANHVDGGVRVRVSKNFFELAGKNVLDNRPAWRVNASAIDAGADSALLISDHTLFSGNPRGSSCIAVEIKAKCGFLPSSEYISKENSIKKQVTRYKMHQHLKFHLGEISKTSEYDPLDLFSGSKERIHMAIKSFFSTPQNNFRIFVDGSLVFGGMGGGADSVHPNETEKCLEDLSKVTGLQLSDFIELLSEAIFKSGVLGKLLATQKLDDHDIEGAIHLYYNIISQPCLVCKSITDTELLRKYSTLHSLPLDKSEKIVRDFLISATAKDCSLMISFRPRQSGTTDSEYDSVFLDSVNQSYDYKAYFIDLDVKPLDKMVHYFKLDQKIVNFYTRNGEVGGDPRDPPKGCGPR | Cofactor: Binds 1 zinc ion per subunit.
Function: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). Phytate is a regulator of intracellular signaling, a highly abundant animal antinutrient, and a phosphate store in plant seeds. Also phosphorylates Ins(1,3,4,6)P4 and Ins(1,4,5,6)P4 to produce Ins(1,2,3,4,6)P5 and Ins(1,2,4,5,6)P5.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 49336
Sequence Length: 445
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
EC: 2.7.1.158
|
Q9USK0 | MPLKNYTKTTSKKEPKQLDIAASDQQIEQWSDQIHKLDKAIRSTIDNSRLFYDAWRCMVCIAPSVTASWISLYRQLPPEKQPAASVGTLVDWNKALERQRREVLLALQNFHVIVIAPCKEVKGYVKKAVEMIKRRDKKVKELEKIQKELLVVYELPDPETKKSKIKALQSQLVRVNGELDDLQKHLTLSFPTLIAKSRVFFGQLMKHFYCLQLQMFRKMHNIVRPWDCFQDDIPQTWLVEFSSVCQAAESISLIAVNNNRPPVELPKSGDVLSNREWEAGKIDAMNSLIAQNLHTSASQVSLSPMASTASSSVTNSPVDTHTPSTPIMSRPPSMKALSSGVESQDESVASSNFQVPIISNPLFKSPAPYSPTSVISNHSSTGKSLVISEWAYLASGSANVVFEYVGKNPYFQDKVIRLRRRGQVFTTEQVYEYYQNVIYPLFAGMESFLIEVFLQPVTRDFLLAAQNASGIYLNLNEQYCLVMKDLKDGIEMKPKWLTQSPAAPPDWVVCRTCALSRMRGRPVGFCPLQLDFNNWPKFLCCLQGFVSPDIAMRLFQSGILRKLRDLQEQYSRTDVALAMTLRDVTLYIGKDHITLLDLDPKDMNTKMSKWERDERNLIEGGWYYGRGMKSTDKACRSSIK | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 72766
Sequence Length: 640
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Subcellular Location: Nucleus
EC: 2.7.1.158
|
Q6C6Q7 | MSSLPTPLPPYKWTLLTAGNANVVYKSDETDLLLRLRRNRNAPSTAEVDEYLTGTIRPAIGPFLFHYTVVNLPLGFLESLPEAENLDLGEPLGLLMENLGPKPNETNVLKSHAVKINYSDNWESYTVELKPKWLLQSPTAPKDSINCRTCALQLKREKPRICPLKLFNEDEQTSLQALEDVFPGTQKQFEPLAKFFSNSELFAEIRHMQHGDELGILGYANYVQVPPQFVTAMTMRDVSLFVHVQGDSVNGKIVDADLKSVSEKRDYWASLETDLIEGGWYEKPGTNCLLRN | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 32942
Sequence Length: 292
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Subcellular Location: Nucleus
EC: 2.7.1.158
|
Q06667 | MQVIGRGGANILIDYGDPTWLWRCCIRWPDLLSSNNSYTIKNISYIKDYVEPLLHGLLCPMYLIDVDIEAIRPILSDFILNLDDKVVKVIKIKNLTNNTSNLILNNHFLKSYCSQNLQTVILELKPKWLYYDTDYCRNCTHNAFKGRGTKYCYNQLLMNPAHLELIFGECNIFPVKFKDAMHEYLRNDNNIFKILYDLQKKLTKNTTPISDIKSINDVNDEHLLLMTLRDVTCFIEWNSAENALHVNIIDVDLKPKEKWTHWTKTYSQLTSSQKIYHTSNK | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 32918
Sequence Length: 281
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Subcellular Location: Nucleus
EC: 2.7.1.158
|
A2X5H5 | MASDLRPPEHQVAGHRASADKLGPLVDGEGLFYKPLQAGERGEHEAAFYAAFTAHPAVPPRVRGAFFPRFHGTRFLPAPASPGGAPYPHIVLDDLLAGLPSPCVADVKIGACTWPPRSPDPYVAKCLAKDRETTSALLGFRVSGVRVVDARGGAVWRPDRSELKGIDAAGVRRVLRRYVSTGGGDGLDCALAAAVYGGEGGVLAQLRELKAWFEEQTLYHFYSASILFGYDANAAAAAAPGGGSGGVRVKLVDFAHVDDGDGVIDHNFLGGLCSLIKFIGDIVAEVTEKASSDHS | Function: Inositol phosphate kinase with a broad substrate specificity. Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4), inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) and inositol 1,2,3,4,6-pentakisphosphate (Ins(1,2,3,4,6)P5) but not inositol 1,4-bisphosphate (Ins(1,4)P2), inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), inositol 1,2,6-trisphosphate (Ins(1,2,6)P3), inositol 3,4,5,6-tetrakisphosphate (Ins(3,4,5,6)P4), inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5), inositol 1,2,4,5,6-pentakisphosphate (Ins(1,2,4,5,6)P5) or inositol hexakisphosphate (InsP6). Regulates pollen and root development probably through the regulation of InsP3-mediated calcium accumulation.
Catalytic Activity: 1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+)
Sequence Mass (Da): 31029
Sequence Length: 295
EC: 2.7.1.140
|
Q9PLF1 | MSKTPLSIVHPWHGPVLTRDDYESLCCYIEITPSDSVKFELDKETGLLKVDRPQKFSNFCPCLYGLLPKTYCGDLSGEYSGQQSNRDNIKGDGDPLDICVLTEKNITQGNILLQARPIGGIRILDSGEADDKIIAVLEDDLVYGAMEDISDCPGSVLDMIQHYFLTYKATPESLIQAKPAKIEIIGLYGKKEAQKVIRLAHEDYCNLFM | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 23310
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
Q9Z6Y8 | MSKKPLYVAHPWHSPTLTQDNYESLCCYIEITPYDSVKFELDKATGLLKVDRPQKFSNFCPCLYGLLPQTYCGTASGNYSGEQTRREGIQGDKDPLDVCVLTEKNIHHGNILLQARPIGGLRIIDSGEADDKIIAVLEDDLVFAEIEDISDCPGTVLDMIQHYFLTYKATPNHLIKGSPAKIEIVGIYGKKEAQKVIQLAHEDYLSYIGDTAEVN | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 23981
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
Q8XIQ9 | MKDVIYITGHKNPDSDSICAALAYAEFKNKTQDTPAIPVRLGNVSQETQYILDYFGVEAPQFLETVKLKVEDLEMDKIAPLAPEVSLKMAWNIMRDKNLKSIPVADGNNHLLGMLSTSNITATYMDIWDSNILAKSATSLDNILDTLSAEAQNINEERKVFPGKVVVAAMQAESLKEFISEGDIAIAGDRAEIQAELIELKVSLLIVTGGHTPSKEIIELAKKNNITVITTPHDSFTASRLIVQSLPVDYVMTKDNLVAVSTDDLVEDVKVTMSETRYSNYPVIDENNKVVGSIARFHLISTHKKKVIQVDHNERGQSVHGLEDAEVLEIIDHHRVADIQTGNPIYFRNEPLGSTSTIVAKRFFENGIRPSREAAGLLCGAIISDTLLFKSPTCTPQDVKMCRKLAEIAGIVPETFAKEMFKAGTSLKGKSIEEIFNADFKPFTIEGVKVGVAQVNTMDIEGFMPLKGEMLDYMNQKAESMGLEMIMLLLTDIINEGSQILVAGRSPEIAEEAFKVKLEDSTTFLPGVLSRKKQVVPPLTQIITTRVSK | Cofactor: Binds tightly a transition metal ion; prefers Co(2+) over Mn(2+).
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 60528
Sequence Length: 549
EC: 3.6.1.1
|
Q8NM79 | MSIEVTVEIPKGSRNKYEIDHETGKVYLDRYLFTPMAYPLDYGYIDHTLGEDGDPLDALVILPESVFPAVVVKSRIIGVFKMTDEAGGDDKLLSVLDDPRYDHIQDISDVSDFLKDEIEHFFVHYKDLEKGKHVDGSGWGDKAEAEKIHAEAIDRYKA | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 17905
Sequence Length: 158
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
P19371 | NYTIGNDNVLTEPLSEIKTAGLMYKMGVQ | Function: Inorganic pyrophosphatase is an essential enzyme for the activation of sulfate by sulfate reducing bacteria. This is a high activity pyrophosphatase.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 3201
Sequence Length: 29
Subcellular Location: Periplasm
EC: 3.6.1.1
|
O77460 | MLAKITRSSFYASRAVGRLSGSIPTSPAALASNCRYIQIERKRTKSHEMALYETVEKGAKNSPSYSLYFKNKCGNVISPMHDIPLYANEEKTIYNMVVEVPRWTNAKMEISLKTPMNPIKQDIKKGKLRFVANCFPHKGYIWNYGALPQTWENPDHIEPSTGCKGDNDPIDVIEIGYRVAKRGDVLKVKVLGTIALIDEGETDWKIIAIDVNDPLASKVNDIADVDQYFPGLLRATVEWFKIYKIPDGKPENQFAFNGDAKNADFANTIIAETHKFWQNLVHQSPASGSISTTNITNRNSEHVIPKEEAEKILAEAPDGGQVEEVSDTVDTWHFIHLK | Function: Component of NURF (nucleosome remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin . NURF is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis . Inorganic pyrophosphatase (PPase), hydrolyzes inorganic pyrophosphate to inorganic phosphate, essential for driving critical biosynthetic reactions including transcription, replication, and DNA repair .
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 37939
Sequence Length: 338
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
A2X8Q3 | MAGEADGKAPLGSRYPPAALNERILSSMSQKHVAAHPWHDLEIGPGAPAVFNCVVEIPRGSKVKYELDKATGLIKVDRVLYSSVVYPHNYGFIPRTLCEDGDPMDVLVLMQEQVVPGCFLRARAIGLMPMIDQGEKDDKIIAVCADDPEYRHFRDIKEIPPHRLQEIRRFFEDYKKNENKEVAVNEFLPAEDAINAIKYSMDLYGAYIIESLRK | Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 24160
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
Q5R8T6 | MSGFSTEERAAPFSLEYRVFLKNEKGQYISPFHDIPIYADKDVFHMVVEVPRWSNAKMEIATKDPLNPIKQDVKKRKLRYVANLFPYKGYIWNYGAIPQTWEDPGHNDKHTGCCGDNDPIDVCEIGSKVCARGEIIGVKVLGILAMIDEGETDWKVIAINMDDPDAANYNDINDVKRLKPGYLEATVDWFRRYKVPDGKPENEFAFNAEFKDKDFAIDIIKSTHDHWKALVTKKTNGKGISCMNTTVSESPLKCDPDAARAIVDALPPPCESACTVPTDVDKWFHHQKN | Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 32743
Sequence Length: 289
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
Q9HWZ6 | MSYSKIPAGKDLPNDIYVAIEIPANHAPIKYEIDKDTDCLFVDRFMATPMFYPANYGFIPNTLADDGDPLDVLVVTPYPVAPGSVIRARPVGVLHMTDEAGGDAKLIAVPHDKLSVLYKDVKEYTDLPALLLEQIKHFFENYKDLEKGKWVKVEGWGNADAARAEITKAVAAFQK | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 19396
Sequence Length: 175
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
P58733 | MDLSRIPPQPKAGILNVLIEIPAGSKNKYEFDKDLNAFALDRVLYSSVQYPYDYGFVPITNNLADDGDPLDGMVIMVPPTFPGVATARPIGMLQMVDGGDRDEKFLCVPAKDPRYTYVKSANDLAGHRLDEIFEFFRSYKNLFKKPTEFFGWKGDVAGLPLVEECVKNYYKTYCKNDHGK | Function: Hydrolyzes PPi generated in anabolic reactions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 20332
Sequence Length: 180
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
Q8U438 | MNPFHDLEPGPDVPEVVYAIIEIPKGSRNKYELDKKTGLLKLDRVLYSPFFYPVDYGIIPRTWYEDDDPFDIMVIMREPVYPLTIIEARPIGLFKMIDSGDKDYKVLAVPVEDPYFKDWKDIDDVPKAFLDEIAHFFKRYKELQGKEIIVEGWEGAEAAKREILRAIEMYKEKFGKKE | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 20913
Sequence Length: 178
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
Q8XWX1 | MSFNNVSPGKDIPNDFNVIIEIPAQSDPVKYEADKETGLLHVDRFVGTGMRYPANYGFIPQTLAGDGDPVDVLVVTPFPLVHGCVVRCRTLGMLKMTDESGQDAKLVAVPVNKLSPATAHMTDLSDIGQNLLDQIKHFFEQYKALEPGKWVKVEGWGGIEEAHKEIVDGVANYKK | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 19224
Sequence Length: 175
Subcellular Location: Cytoplasm
EC: 3.6.1.1
|
Q9N1F0 | MVKAPQSEERLAGGGKGNNSVLACGAQASWSIFGADAAEVPGTRSHSRQEAAMPHIPEDEEPPGEPQAAQSPAGQDPATTGISCSPPTIILTGDASSPEGETDKNPVNRAHSPHRRLSHRHLKVSTASLTSVDPAGHVIDLVNDQLPDISISEEDKKKNLALLEEAKLVSERFLTRRGRKSRSSPGESSPAVSPNLSPGASPASSQSNSLTVPTPPGLDVCSGPPSPLPGAPPQKGDEAEVPSPHLGESNVLKGLADRKQNDQRTLSQGRLTARSPTVEKSKEITIEQKENFDPLQRPEAIPKGPASGPGSGGKMALNSPQPGPVESELGKPLAKTAKEGNPLPRGPTQGSGGVAPQASQGKSTVGEPAGSKVGSKAELWPPTSRPPLLRGVSWDSGPEEPGPRLQKVLAKLPLAEEEKRFTGKAGSKLAKAPGLKDFQIQVQPVRMQKLTKLREEHILLRNQNLVGLKLPELSEAAEQEKGHPSELSSAIEEEESKGGLDVMPNISDVLLRKLRVHKSLPGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERERNLTEENTEKELENFKASITSSASLWHHCEHRETYQKLLEDIAVLHRLAARLSSRAEMVGAVRQEKRMSKATEVMMQYVENLKRTYEKDHAELMEFKKLANQNSSRSCGPSEDGVPRTARSMSLSLGKNMPRRRVSVAVVPKFNILNLPGQSPSSSPIPSLPALSESSNGKGNPPVSSALPALLENGKTNGDPDCEASASVPTPSCLEGISQEAKARMEEEAYNKGYQEGLKKTKELQGLREEEEEQKSESPEEPEEVAETEEEEKEQRSSKLEELVHFLQVMYPKLCQHWQVIWMMAAAMLVLTVVLGLYGSHNSCVEQADGSLGKSTCSAAQRDSWWSSGLQHEQPTEQ | Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO-dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation.
PTM: Phosphorylated by PRKG1/cGKI-beta. Phosphorylation at Ser-696 is necessary for PRKG1-induced calcium release in the cytosol.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 98375
Sequence Length: 911
Subcellular Location: Sarcoplasmic reticulum
|
Q9Y6F6 | MGMDLTCPFGISPACGAQASWSIFGADAAEVPGTRGHSQQEAAMPHIPEDEEPPGEPQAAQSPAGQGPPAAGVSCSPTPTIVLTGDATSPEGETDKNLANRVHSPHKRLSHRHLKVSTASLTSVDPAGHIIDLVNDQLPDISISEEDKKKNLALLEEAKLVSERFLTRRGRKSRSSPGDSPSAVSPNLSPSASPTSSRSNSLTVPTPPGLDVCSGPPSPLPGAPPQQKGDEADVSSPHPGEPNVPKGLADRKQNDQRKVSQGRLAPRPPPVEKSKEIAIEQKENFDPLQYPETTPKGLAPVTNSSGKMALNSPQPGPVESELGKQLLKTGWEGSPLPRSPTQDAAGVGPPASQGRGPAGEPMGPEAGSKAELPPTVSRPPLLRGLSWDSGPEEPGPRLQKVLAKLPLAEEEKRFAGKAGGKLAKAPGLKDFQIQVQPVRMQKLTKLREEHILMRNQNLVGLKLPDLSEAAEQEKGLPSELSPAIEEEESKSGLDVMPNISDVLLRKLRVHRSLPGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERERNLTEENTEKELENFKASITSSASLWHHCEHRETYQKLLEDIAVLHRLAARLSSRAEVVGAVRQEKRMSKATEVMMQYVENLKRTYEKDHAELMEFKKLANQNSSRSCGPSEDGVPRTARSMSLTLGKNMPRRRVSVAVVPKFNALNLPGQTPSSSSIPSLPALSESPNGKGSLPVTSALPALLENGKTNGDPDCEASAPALTLSCLEELSQETKARMEEEAYSKGFQEGLKKTKELQDLKEEEEEQKSESPEEPEEVEETEEEEKGPRSSKLEELVHFLQVMYPKLCQHWQVIWMMAAVMLVLTVVLGLYNSYNSCAEQADGPLGRSTCSAAQRDSWWSSGLQHEQPTEQ | Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO-dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation.
PTM: Phosphorylated by PRKG1/cGKI-beta; Ser-386 showed constitutive phosphorylation in platelets whereas Ser-676 is only phosphorylated in presence of cGMP and nitric oxide (NO); Ser-689 is phosphorylated in resting platelets but increases in presence of cGMP and NO. PRKG1 inhibitor prevents phosphorylation of Ser-676 and Ser-689 in response to NO and cGMP.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 97957
Sequence Length: 904
Subcellular Location: Cytoplasm
|
Q9C5S2 | MPPRCPFLRHLFFLLLLLSPWIMSPCGGAADDVTYPIVPSSPGRRSILQIRREPPTEPNTKLVVDRDGKVFLKQQPKETPYWSFSTGSPMHSLYQAPANNNTENATEITRPHIIVEYLNNSKAATTVDGYHNWTVQEFFRQKPLVTDDGVTLGSETTSAYLVDGRSGRLIHVYKSTGDTKITNALVKPASTEDFVNEPLLIRRTDSKLEHFSKTTGKLVWNLTVSHFRAALLCDPVFNSGYDLGPKLQTGIYMPLLCGSQIDVRGPEIVIRVLHDQPMNVKMLPSPSLNHFESENSIMPFGKARESRKLQEQHKQKYTYLFGQWSPVKLLAPLVLLGVVVSVFIKKFSSRGSDVSLKAGPSKKKKNRKSAKDTNRQSVPRGQDQFELIEGGQMLLGFNNFQSGATDGRKIGKLFLSSKEIAKGSNGTVVFEGIYEGRPVAVKRLVRSHHEVAFKEIQNLIASDQHTNIIRWYGVEYDQDFVYLSLERCTCSLDDLIKSYLEFSMTKVLENNDSTEGVAAYKIQLDSLEGVIKGNNFWKVGGHPSPLMLKLMRDIVCGIVHLHELGIVHRDLKPQNVLISKDMTLSAKLSDMGISKRMSRDMSSLGHLATGSGSSGWQAPEQLLQGRQTRAVDMFSLGCVIFYTITGCKHPFGDDLERDVNIVKNKVDLFLVEHVPEASDLISRLLNPDPDLRPSATEVLLHPMFWNSEMRLSFLRDASDRVELENREADSEILKAMESTAPVAIGGKWDEKLEPVFITNIGRYRRYKYDSIRDLLRVIRNKLNHHRELPPEIQELVGTVPEGFDEYFAVRFPKLLIEVYRVISLHCREEEVFRKYFKCDII | Function: Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP60 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator which then induces transcription of UPR target genes. Involved in organ growth regulation. Plays a role in plant immunity and abiotic stress responses.
PTM: Autophosphorylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 95138
Sequence Length: 841
Subcellular Location: Endoplasmic reticulum membrane
|
Q93VJ2 | MRGSALLDLILFLLVSPLAHSFKGSEISKFYDKSISNQISQSDRESGYVLVSTVDGSISLVDMSSQKLDWTFHTNEPIYSSYQAPHYHYTTDEERSSVLGDDFYMDCDKDWRLYNSSVRKGKRVNEIVDASEFIGTLPYTSTDRIVLGKKDTSVFLLDWKTGKLVKRYRMDELYSNTVVENDKEKAIVLSKEAPLLFGSGFKKSEDFPELVYIERKDFKIQCISKFGDVLWSVSYAKMEAKLQNHESVQFISGLSSSVGKNQFPLSYTTSVPMVQLRNVKYETLFPRLGFLDEALYLPFQDRKPNQLAIGDGNQLTLPGNKEAEEVLSLPLPETVISQITDIIDGSTKQAGFASKFSGLIVLIFGFCVTMLSVCGLFFYRLRQSIRIKEPYVSEVPIATPKKKKSKKNGTTKAVHKKENGFISGGNKDPSHEENEKRLLTAFPGLNNSSAEGYRVGKLFVSNKEIAKGSNGTVVLEGSYEGRLVAVKRLVQSHHDVAQKEILNLMASDKHSNIVRWYGVDQDEHFIYISLELCACSLNDLIYASSALLESPMASSSIHSIQINPIFENGKGVELWKENGHPSPVLLKLMRDIVAGLVHLHDIGIVHRDLKPQNVLIVKNSSLCAKLSDMGISKRLPADTSALTRNSTGLGSGSSGWQAPEQLRNERQTRAVDLFSLGCVLFFCMTGGKHPYGDNYERDVNVLNDQKDLFLIESLPEAVHLLTGLLNPDPNLRPRAQDVMHHPLFWNSDMRLSFLRDASDRVELENREEGSQLLAALESTAAVTLNGRWDEKLDSIFLDNIGRYRRYKFDSIRDLLRVIRNKLNHYRELPKELQELLGSVPEGFERYFSSRFPKLLIQVYTVLFDYCNNEEFFFKYSKTTVF | Function: Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP60 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator which then induces transcription of UPR target genes. Involved in organ growth regulation. Plays a role in plant immunity and abiotic stress responses. Required for ER stress-induced autophagy.
PTM: Autophosphorylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 99616
Sequence Length: 881
Subcellular Location: Endoplasmic reticulum membrane
|
Q09499 | MRATFHLFTFIFLLLFSSVICISTPGFRNDHESIGDDEEKTSSTILVSTIDGRLRALDSETGEIKWTLQEEPVLRSPSAVKQGFTFLPNPLDGSLYVLKNSSLKKLPFNIPQLVHASPCKGNDGILYAGSKKDVWFGIDPKTGLKVETLSSASADRICPANQKQTIFLGRTEYRVSMFDEKNRGKTWNATFNDYSAHLLPEVNTWPFKHYASSSHGYILTFDRETGEMRWEQDLKQPVVALYLLRDDGLHKLPFEVMGKETMENVAKNIFTVDQWPTVLGVNAADPQTTSLTNQFFPALFVGESSFGLYAIEALVDHQTITYSPKLLGPPLLEGPAPIALTEMEKEEYLPPRRPIIRNIPPSITHKTSDGEYLLLGYHDRPMMTMATIIPTRYPVPGPHKAIGSTIERPPPQLLGPVEPQKHEDTSFILLLLNNHPIPFYATLVTMFALLLTVIWQCGRQWDQQKSTSRMDSFEIVNNPGESRSAQTSKQSNRGSFGWANRKIEIPEGWMAVGSKLMYSPSDILGTGCEGTVVYRGTFDGREVAVKRVVSEFVKFAHREADLLRESDTHPHVIRYFCMESDSQFRYLALELCIASLNDYVEQKEVQQNVTIALRDIMKQATDGLAHLHASKIVHRDMKPQNVLITMASQRGEMRAVISDFGLCKRVQPGKNSISRGIASGLAGTDGWIAPEVLISASTSYPVDIFSLGCIFYYVLTSGTHPFGKSLHRQANIVNGEYTLNKLADLDDWSLADDLISSMLNVEPLHRLTADAVLNHPFFWTSEKRLAYFSDVSDRVEKEEDNSPVVRRIETDARIVVCGGWREKICDALKEDLRKFRTYKSFSVRDLLRAMRNKKHHYRELPEDVRQSLGDIPDQFLHYFTSRFPRLLLHVYKATEYCSGEAVFKRYYSDDVRARMYPIVEEEERVRKKIKEEMANEVWARAPKPVEQRTPLKLDKRNIKKKSNPNTD | Function: Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation . The active endoribonuclease domain splices xbp-1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes . Unfolded protein response (UPR) transcriptional activation by ire-1, as well as translational attenuation by pek-1 in a complementary pathway, maintains ER homeostasis . Regulates the transcriptional up-regulation of nucleoside-diphosphatase apy-1 and many other genes, upon ER stress . By activating the UPR pathway during non-lethal hypoxia pre-conditioning, confers adaptive protection to subsequent exposure to hypoxia . ire-1 and pek-1 are redundant genes that control a pathway essential for larval development and survival . Plays a role in the nuclear retention of unspliced mRNAs .
PTM: Autophosphorylated mainly on serine residues.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 109822
Sequence Length: 967
Subcellular Location: Endoplasmic reticulum membrane
|
Q7XIT1 | MRSLRRVLLQLVLLAGVAFRGVRFDDAADAAAAAQGSSDLFELPSPSPTLALPGGGDEGASTEIIAAPWPGRHGLFTPPRSTSQPARAVVQPAADFGSQLQFYDNGTIQLVDLLSKLPRWQFSTGPPLSKHITTSKPDLNYVIYLDGSETSDLIEVHNGSGVRLPWKLEEFIAETPYIRDSFVTIGSKVSTTFVVNADSGEIIYKHSLPVALNEVGGPLVEEIPSKLDAARSGTSANIIVVVRTDYSISASDLGEHLFNWTRTSFTANYYARYGHQDMLAQSSCLRGNIPCIRTEGPPIKLYLPDSSSDNAIVLRPVNEVSAVDALEPLLPPKKLPQPAGESNVALDSAQNQTADIALGHFVPADTELTNSVTKFSYRWLFPTFLMLLIMACLVKLADASKYCRQFVIRFLKPFMRDEKLMDPRGKSEGTSKRRKARKKDGLINSTQIFSASDKEGNGTGGSTEAQSNKAHDSTNVELPNGLNGRQIGKLCVYSKEIGKGSNGTVVFEGSYGGREVAVKRLLRSHNDIASKEIENLIASDQDPNIVRMYGFEQDNDFVYISLERCRCSLADLIQLHSVPPFSNTKGTDIELWRQDGLPSAQLLKLMRDVVAGIVHLHSLGIIHRDLKPQNVLISKEGPLRAKLSDMGISKRLQEDMTSVSHHGTGFGSSGWQAPEQLRHGRQTRAIDLFSLGCLIFYCITKGKHPFGEYYERDMKIINNQFDLFIVDHIPEAVHLISQLLDPDPEKRPTAVYVMHHPFFWSPELCLSFLRDTSDRIEKTSETDLIDALEGINVEAFGKNWGEKLDAALLADMGRYRKYSFESTRDLLRLIRNKSGHYREFSDDLKELLGSLPEGFVQYFSSRFPKLLIKVYEVMSEHCKDEEAFSKYFLGSSA | Function: Involved in endoplasmic reticulum (ER) stress response. Senses unfolded proteins in the lumen of the ER via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP50 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response (UPR) transcriptional activator, which then induces transcription of UPR target genes, such as luminal-binding protein (BiP) chaperones.
PTM: Autophosphorylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 99088
Sequence Length: 893
Subcellular Location: Endoplasmic reticulum membrane
|
Q55GJ2 | MTFSKTRNKIIFLLFLIIINIFNINAYIKDENEDDLSLLISTLDGNIYSFNYESGELNWDLKPNGGDSLYSTSQFDRKQQQSTSTSTEITKSSPSILIPTLDGSGLLFQYSNDRLHQVPFSLQELVNTSPLFLKELEDKSSTSSTSTTSESSKDENKVTMFIGNKKTSITVVDSQTGEIIKSMSKDGLWLTDEDDCPVNIIPDEALMFTRSDYQIIALDPKSGVEKWNLSVGEYIPHSTKSFYNSEISLNFEGLIEVASLSQRMYKIYIKKPEKTVVGISHNYWEHILTSSPVSIYAYSSKKHILKKLDFHRKVSPYSNSLIPVASTDLMIPSNFDRTFMFDDYYGQLFIVSPPSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNNNNNNKNESDKSNLTPLTPYDPSKPNGANNNNNNNNDLLDSNKLKNYDIYLYSSIVILITSIIVFIRSKKNFNLINVNNNNNQNNNQNSNQNNNINNKKTPKKKKKKQKNKNNKNNNDEDDENEIENYNDNQNDLIDEFISTNSVIQQQQQQQQQLINSSNKINNGSGKIILDNGNVKIGKLEIITNKILGTGSCGTIVYEGKMEGRKVAVKRMLSQFVKFADREVSILIHSDEHTNVVRYYAKEEDDEFIYLAISFCQKSLDMYVQQTLSLQISPTDSPSIQSSNNNGNGNNGNNNNNNQIIIDNKTKQMILELFKGLEHLHSLNIVHRDIKPHNVLIDPNNRVKISDMGLGKLLDNDDQSLTFTSDSHGWQPAEYLNGTNRNTKKVDIFSLGCVVYYLLTGAHPFGHRYNREKNVLKGKFDIDQIKHLPDIHQLVHSMIQFEPEKRPDIGECINHPFFWEVHKKLSFLVAASDYLEFEKPTSPLNLEIDSHVDLVTDGSGDWWLKIDQVLIDNIGRYRKYNGKSIRDLLRVIRNKFNHYRDLSPEEQTCLGILPDGFFNYFDLKFPQLFIVTYLFILKNLKNDQYFVQYYY | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 112801
Sequence Length: 984
Subcellular Location: Membrane
EC: 2.7.11.1
|
Q5ZLQ4 | MDALRPGSPYQPIIEELRNYPQKRFYNVSKLGGTKYDVLPYSIRVLFESSIRNCDGFLVKETDAMNILDWKTKQNDVEVPFCPARVVLQDFTGIPAMVDFAAMREAVRNAGGDPVKVNPACPTDLTVDHSLQIDFSKCAIQNAPNPGGGEAQKPTAKLSPLKGQPRKLPCRGQSSCKGPCSAGELSRASGQFSAQIENTPILCPFHLQPVPEPETVLKNQEMEFGRNRERLQFFKWSSKVFKNTSIIPPETGMAHQVNLEYLSRVVFDVEDFLYPDSVVGTDSHTTMVNGLGILGWGVGGIETEAVMLGMPVTLTLPEVVGCELTGTASPLATSIDIVLGITKHLRQAEVAGKFVEFFGSGVSQLSVADRTTIANMCPEYGAILSFFPVDNVTLKHLRHTGFDEAKLEVMEAYLKAVKLFRNGESSSREPEYSQVVQISLSSIIPHVSGPKRSQDRVAVNNMKSDFQTCLNEKAGVKGFQIAAEKQNDVVPVQYEGNQYELSHGCVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLEVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEVVGYGCSTCVGNTAPLPEAIRNAIKQGDIIACGVLSGTKNFEGRLCDCVRANYLASPPLVVAYAIAGTVRIDFETEPLGTGFNGRSIYLRDIWPTRKELHTVEEECVISSMFKELKEKMEKGNKRWNSLEAPESPLFPWDLKSTYIRCPSFFDKLAKEPVSLQPIENAHVLLYLGDSVTTDHISPAGSIARSSAAAKYLTNKGLTPREFNSYGARRGNDAVMTRGTFANIKLLNKFIGKPAPKTIHFPSGQTLDVFEAAELYQKEGIPVIILAGKKYGLGSSRDWAAKGPFLLGVKAVLAESYEKVHKSQLIGIGIAPLQFLPGENPNTLGLTGREQFSILFPPELSPKMTLDIKTSTGKVFSVFALFENDVEITLYKNGGSLNFVARRFL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. [4Fe-4S]-binding affects RNA-binding activity, thereby inhibiting activity of the protein.
Function: RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.
PTM: Ubiquitinated and degraded by the proteasome in presence of high level of iron and oxygen.
Sequence Mass (Da): 105362
Sequence Length: 965
Subcellular Location: Cytoplasm
|
P48200 | MDAPKAGYAFEYLIETLNDSSHKKFFDVSKLGTKYDVLPYSIRVLLEAAVRNCDGFLMKKEDVMNILDWKTKQSNVEVPFFPARVLLQDFTGIPAMVDFAAMREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFSKCAIQNAPNPGGGDLQKAGKLSPLKVQPKKLPCRGQTTCRGSCDSGELGRNSGTFSSQIENTPILCPFHLQPVPEPETVLKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPPGTGMAHQINLEYLSRVVFEEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESMETYLKAVKLFRNDQNSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEKQKDIVSIHYEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEPLGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLTKEPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFIGKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSLGLSGRETFSLTFPEELSPGITLNIQTSTGKVFSVIASFEDDVEITLYKHGGLLNFVARKFS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. [4Fe-4S]-binding affects RNA-binding activity, thereby inhibiting activity of the protein.
Function: RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.
PTM: Ubiquitinated and degraded by the proteasome in presence of high level of iron and oxygen. Ubiquitinated by a SCF complex containing FBXL5. Upon iron and oxygen depletion FBXL5 is degraded, preventing ubiquitination and allowing its RNA-binding activity.
Sequence Mass (Da): 105059
Sequence Length: 963
Subcellular Location: Cytoplasm
|
Q9ZUV3 | MTTHKHRRTEKNLCFKQYYKWILCFILTLYFFASFFVDHDQDHRSSTSISKHLLTNHKPKLFASRAMFESKIHDHKLGFTSQQPNIKTDVFNNLKIYVYDLPSKFNKDWLANDRCTNHLFAAEVALHKAFLSLEGDVRTEDPYEADFFFVPVYVSCNFSTINGFPAIGHARSLINDAIKLVSTQYPFWNRTSGSDHVFTATHDFGSCFHTMEDRAIADGVPIFLRNSIILQTFGVTFNHPCQEVENVVIPPYISPESLHKTQKNIPVTKERDIWVFFRGKMELHPKNISGRFYSKRVRTNIWRSYGGDRRFYLQRQRFAGYQSEIARSVFCLCPLGWAPWSPRLVESVALGCVPVIIADGIRLPFPSTVRWPDISLTVAERDVGKLGDILEHVAATNLSVIQRNLEDPSVRRALMFNVPSREGDATWQVLEALSKKLNRSVRRSNSFL | Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the synthesis of the glycosyl sequence at the glucuronoxylan reducing end.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 51694
Sequence Length: 448
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q9SXC4 | MASIRRTLSPMYHDRSHENGGSHKGFTIGGSSSKHNSSQFLSYLTKLLGVTSDPKSSRRGPWRRPFYQFLVFFLLGFVLGLTPFGKMEDVNGSDRFSFEIKQPYVEERLENRKREEAAVDAVSFVAETENGKKEVNFVPKKLLIVVTPTYNRAMQAYYLNRVAQTLRLVESPVLWIVVEGNVASFETSEILRKTGVMYRHLVCKRNMTSIKDRGVHQRNTALEHIELHKLDGIVYFADDDNIYSLELFQSLRQISRFGTWPVAMLAQSKNKAILEGPVCNGSQVIGWHTNEKSKRLRRFHVDMSGFAFNSTILWDPKRWRRPFSHPTRQLDTVKEGFQETSFIEQVVADESEMEGVPPACSSILNWHLHLDALDVPYPQGWAIQKNLQALITMK | Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the elongation of glucuronoxylan xylosyl backbone.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45187
Sequence Length: 394
Subcellular Location: Golgi apparatus membrane
EC: 2.4.2.-
|
Subsets and Splits
No saved queries yet
Save your SQL queries to embed, download, and access them later. Queries will appear here once saved.