wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-9 (IL-9) (Cytokine P40) (T-cell growth factor P40) (P15247)
Organism: Mus musculus (Mouse)
Function: Multifunctional cytokine secreted mainly by T-helper 2 lymphocytes and also mast cells or NKT cells that plays important roles in the immune response against parasites. Affects intestinal epithelial permeability and adaptive immunity. In addition, induces the differentiation of specific T-cell subsets such as IL-17 producing helper T-cells (TH17) and also proliferation and differentiation of mast cells. Mechanistically, exerts its biological effects through a receptor composed of IL9R subunit and a signal transducing subunit IL2RG. Receptor stimulation results in the rapid activation of JAK1 and JAK3 kinase activities leading to STAT1, STAT3 and STAT5-mediated transcriptional programs. Induction of differentiation genes seems to be mediated by STAT1 alone, while protection of cells from apoptosis depends on STAT3 and STAT5.
Subcellular location: Secreted.
Interaction partners:
- Cytokine receptor common subunit gamma
- Interleukin-9 receptor
- Interleukin-7
- Interleukin-4
- Interleukin-5
- Tyrosine-protein kinase JAK3
- Interleukin-6
- Interleukin-2
- Interleukin-15
- Interleukin-10
Sequence:
MLVTYILASVLLFSSVLGQRCSTTWGIRDTNYLIENLKDDPPSKCSCSGNVTSCLCLSVPTDDCTTPCYREGLLQLTNATQKSRLLPVFHRVKRIVEVLKNITCPSFSCEKPCNQTMAGNTLSFLKSLLGTFQKTEMQRQKSRP
Protein: Semaphorin-6C (Semaphorin-Y) (Sema Y) (Q9WTM3)
Organism: Mus musculus (Mouse)
Function: May be a stop signal for the dorsal root ganglion neurons in their target areas, and possibly also for other neurons. May also be involved in the maintenance and remodeling of neuronal connections (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Plexin-A1
- Plexin-A2
- Plexin-A3
- Plexin-D1
- Plexin-A4
Sequence:
MPRAPHSMPLLLLLLLLSSLPQAQAAFPQDPTPLLTSDLQGASPSSWFRGLEDDAVAAELGLDFQRFLTLNRTLLVAARDHVFSFDLQAQEEGEGLVPNKFLTWRSQDMENCAVRGKLTDECYNYIRVLVPWNSQTLLACGTNSFSPMCRSYGITSLQQEGEELSGQARCPFDATQSTVAIFAEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLREPHFVYALEHGEHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSPRALDRHWTSFLKLRLNCSVPGDSTFYFDVLQSLTGPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDDIERGFEGKFKEQRSLDGAWTPVSEDKVPSPRPGSCAGVGAAASFSSSQDLPDDVLLFIKAHPLLDPAVPPATHQPLLTLTSRALLTQVAVDGMAGPHRNTTVLFLGSNDGTVLKVLPPGGQSLGSEPIVLEEIDAYSHARCSGKRSPRAARRIIGLELDTEGHRLFVAFPGCIVYLSLSRCARHGACQRSCLASLDPYCGWHRSRGCMSIRGPGGTDVDLTGNQESTEHGDCQDGATGSQSGPGDSAYGVRRDLSPASASRSIPIPLLLACVAAAFALGASVSGLLVSCACRRANRRRSKDIETPGLPRPLSLRSLARLHGGGPEPPPPPKDGDAAQTPQLYTTFLPPPDGGSPPELACLPTPETTPELPVKHLRASGGPWEWNQNGNNASEGPGRPPRGCSGAGGPAPRVLVRPPPPGCPGQAVEVTTLEELLRYLHGPQPPRKGSEPLASAPFTSRPPASEPGASLFVDSSPMPRDGVPPLRLDVPPEGKRAAPSGRPALSAPAPRLGVGGSRRLPFPTHRAPPGLLTRVPSGGPARYSGGPGRHLLYLGRPEGHRGRSLKRVDVKSPLSPKPPLASPPQPAPHGGHFNF
Protein: Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102) (P35605)
Organism: Bos taurus (Bovine)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi. {ECO:0000250}.
Interaction partners:
- Coatomer subunit epsilon
- Coatomer subunit alpha
- Coatomer subunit beta
- Coatomer subunit gamma-1
- Coatomer subunit delta
- Coatomer subunit zeta-1
- Coatomer subunit gamma-2
- Coatomer subunit zeta
- ADP-ribosylation factor GTPase-activating protein 2
- ADP-ribosylation factor GTPase-activating protein 3
Sequence:
MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSVVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDGFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKGFQPSRSAAQQELDGKPASPTPVIVTSQTANKEEKSLLELEVDLDNLEIEDIDTTDINLDEDILDD
Protein: Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-) (K(+) channel subunit beta-2) (Kv-beta-2) (Neuroimmune protein F5) (P62482)
Organism: Mus musculus (Mouse)
Function: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability. Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore. Modulates the functional properties of KCNA4 (By similarity). Modulates the functional properties of KCNA5. Enhances KCNB2 channel activity. Modulates the functional properties of KCNA5. Binds NADPH and has NADPH-dependent aldoketoreductase activity (By similarity). Has broad substrate specificity and can catalyze the reduction of methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62483}. Membrane {ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:8576199}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P62483}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:11825900}. Synapse, synaptosome {ECO:0000269|PubMed:21357749}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P62483}. Note=Recruited to the cytoplasmic side of the cell membrane via its interaction with pore-forming potassium channel alpha subunits. Associates with microtubules when unphosphorylated. {ECO:0000250|UniProtKB:P62483}.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 2
- Potassium voltage-gated channel subfamily A member 1
- Potassium voltage-gated channel subfamily A member 5
- Potassium voltage-gated channel subfamily A member 4
- Potassium voltage-gated channel subfamily A member 6
- Potassium voltage-gated channel subfamily A member 3
- Voltage-gated potassium channel KCNC1
- Potassium voltage-gated channel subfamily B member 1
- A-type voltage-gated potassium channel KCND2
- A-type voltage-gated potassium channel KCND3
Sequence:
MYPESTTGSPARLSLRQTGSPGMIYSTRYGSPKRQLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNKPYSKKDYRS
Protein: Endoplasmic reticulum vesicle transporter protein (Q94K91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- RNA-binding
- At1g78010
- GTPase Der
- GTPase Der
- Vesicle-associated protein 2-1
- Vesicle-associated membrane protein 724
- Vesicle-associated membrane protein 714
- Eukaryotic aspartyl protease family protein
- Transport/golgi organization-like protein
- Myosin heavy chain-like protein
Sequence:
MGVKQALRSIDAFPRAEDHLLQKTQSGAVVSIVGLLIMATLFLHELSYYLNTLTVHQMSVDLKRGETLPIHVNMTFPSLPCDVLSVDAIDMSGKHEVDLDTNIWKLRLNSHGHIIGTEYISDLVEKGHEHGHSPHKHDGKEEHKNETETEALNILGFDQAAETMIKKVKQALADGEGCRVYGVLDVQRVAGNFHISVHGLNIYVAQMIFGGSKNVNVSHMIHDLSFGPKYPGIHNPLDDTNRILHDTSGTFKYYIKIVPTEYRYLSKDVLSTNQYSVTEYFTPMTEFDRTWPAVYFLYDLSPITVTIKEERRSFLHLITRLCAVLGGTFALTGMLDRWMFRFIESFNKKPSTRA
Protein: Protein GnsB (P77695)
Organism: Escherichia coli (strain K12)
Function: Overexpression increases levels of unsaturated fatty acids and suppresses both the temperature-sensitive fabA6 mutation and cold-sensitive secG null mutation.
Interaction partners:
Sequence:
MNIENLKTKAEADISEYITKKIIELKKKTGKEVTSIQFTAREKMTGLESYDVKINLI
Protein: EG:86E4.4 protein (O46093)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPARIRKRNRLFYDENIINDDKPLRMSLAPKKTPGRPPQSAGGGSSQKIPLTPSKVLKKRKGVVSRYMRSSEQGTNSVSASNQPQLLGKHKKATPSKSQSVGSKLGSGGPKTGRGAHFIGKGTAAALAAVAAAEEEANQAEAAALANKRLGQSIGLRLRNLLKLPKAHKWAIAEWFYSYVDKPLFECRDEFMNHVNELAPRLGTRSLIRHEWVNIRRRMGRPRRCSAKFFSEERKELDRKRQVIRTLQSRKPGEFKDSVSMLSDMPEKIPMTLPLGTKVTARLRSPQDGIFAGTVAAYDSLNAMYRVTFERIGLGTHAIPDYEIVSENFHEMLPLHSFTKDFRPNLMSIYQTNNLGFTTNLGFTANLTNNYLQKKEKIDGGAGAAAGAGSYYFKPQKHLATNNAAARNALSMKLNKSDPLLGQDSVGVSPIRQQLTRNRGYSTSLLEHLVRLEKYIAVKADRIQRLNKMNGTAELAMGDMISHDENGDRHRRQIAVNFQRQYAFNIVTIERINAELMFELTKVQELSSSLTRNPNVQAMISPTYLREECRAKASQTVDDINKGMVKNTRMIKLLKDLTTLLIVTQNLGGDCEVSEVNEVLEGCLEEVRSNLICSENREVFQMSVQGRLEYIAMDISRRLEEKSLSRVADGDDDIKSLKSEDETDEDHVQDHKHGADEEPAADTSKTKAKGSPKQVEGKENSEVDKKDHSSHPMDTDTEKEEKLESGGSENAGYASQQRQDEDQDTEEQHLDLEEQHLDPEEHHLDLEEQHLDPEEQHLDLEEHHLELEEQHLDPEEQSLNPAVTEDTQITIESMKESDEEFQSAAETEEDDMVGLIMEEEEEEEFVYDKDL
Protein: Luciferin sulfotransferase (EC 2.8.2.-) (A0A173GP47)
Organism: Photinus pyralis (Common eastern firefly) (Lampyris pyralis)
Function: Catalyzes the production of firefly sulfoluciferin from luciferin using the sulfo-donor 3'-phosphoadenylyl sulfate (PAPS). Is also able to catalyze the reverse reaction, i.e. the adenosine 3',5'-bisphosphate-dependent desulfonation of sulfoluciferin. Can use either D- or L-luciferin stereoisomer as substrate. Sulfoluciferin, which is not a substrate of P.pyralis luciferase, likely serves as a luciferin storage form in fireflies.
Interaction partners:
Sequence:
MFASILGKIPQYSTISSKCSLKECRKVKKVENSDEIGEIIHRDFLDPFCNEYVLIGEEETSLGINYLQFEEEIRTFEIRDSDIIVASYPKAGTTWTQELVWLIGNDLDFKAAEEHLDKRFPHFELCTIVNFAKMTEMLGSTRPEYIGNSINYLRDLEGTRFIKTHLTYNLLPEQILNGNRKPKIIYVMRDPKDVCVSYYHHGRLIQGWRADFQNFSKVFLSEKIMFGSYWKHVLGYWEHRDKPNVLILTYEEMKKDLLSVIRKTAQFLDKKLNENKIPQLLKHLSFESMKNNRAVNQQDKIESRMKHKLVPEQGAFMRSGTSQNYKGEMSEELILKFDEWTKKSISGSSFVTEPIADLYLNTSQKSVPKM
Protein: Protein transport protein SBH1 (Sec61 complex subunit SBH1) (Sec61 complex subunit beta) (P52870)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post-translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In the cotranslational pathway, ribosomes synthesizing presecretory proteins are targeted to the translocon by the cytosolic signal recognition particle (SRP) and its ER-localized receptor. The association of the Sec61 complex with the ribosome is mediated by the 28S rRNA of the large ribosomal subunit. SRP-independent post-translational translocation requires the association of additional factors, such as the Sec62/63 complex and KAR2.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein.
Interaction partners:
- Protein transport protein SBH2
- Protein transport protein SEC61
- Translocation protein SEC72
- Protein transport protein SSS1
- Translocation protein SEC66
- Translocation protein SEC62
- Sec sixty-one protein homolog
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
Sequence:
MSSPTPPGGQRTLQKRKQGSSQKVAASAPKKNTNSNNSILKIYSDEATGLRVDPLVVLFLAVGFIFSVVALHVISKVAGKLF
Protein: ETS domain-containing protein (H2KYY1)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
- ETS domain-containing protein
Sequence:
MIQIQGQPRPEPLLLVLPTATSPLNISSSNISSKSSRINNNNDNENDEEDDGRDLDVEMKTESEWPRIERPTPKYADGRRISAPAVLAHGLFEIPTSCSVQITVLQQLLDQSSTLSLEPTNSPDSGVGTDSTPETSPSSSTTRRHAFAPPPPRPRPPTVPLPTVTQQIPWQTSTIWPWIQQAQSASTADATQRWLQSALLCPTTSASHPNLLTIPQISVQPQPTAPQTLLTAAPFISSTVFTPTCGDLLTTCTPSNPSLLHPYLLDTSRRFSEPNPAPLAQRTPGKKQKDGQVTYLWEFLLRLLQDDQYSPKFIKWIDQAKGIFKLVDSKAVSRLWGMHKNKPGMNYETMGRALRYYYQRGILQKVDGQRLVYRFVHLPSDVASECDSSCESADSCDSPKISPISLKLMLQPATSASDEA
Protein: Ferredoxin YfhL (EcFd) (P52102)
Organism: Escherichia coli (strain K12)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Interaction partners:
- NADH-quinone oxidoreductase subunit C/D
- Probable pyruvate-flavodoxin oxidoreductase
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit H
Sequence:
MALLITKKCINCDMCEPECPNEAISMGDHIYEINSDKCTECVGHYETPTCQKVCPIPNTIVKDPAHVETEEQLWDKFVLMHHADKI
Protein: Dopamine/Ecdysteroid receptor, isoform A (Dopamine/Ecdysteroid receptor, isoform B) (Dopamine/Ecdysteroid receptor, isoform C) (G-protein coupled receptor) (Q9VZD1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- G protein alpha s subunit subunit alpha)
- Neuronal synaptobrevin, isoform J
- Dopamine receptor 1
Sequence:
MQEMSYLQDNSKVEALTKAVLISILGVAIVLSNLLIIATYANFKGPTEVINYYLLSLAIADLLCGLLVVPFSVYPALTGEWMYGDIVCRFTGYLEVTLWAVSVYTFMWISVDRYLAVRKPLRYETVQTKTRCQCWMVFTWISAALLCCPPILGYSMPIENNMTHICMLDWGNMAAYSATLAILVLGPSLISIVHNYGYIFVMMRKIRSGEPIHDKEYATALAENLSNPSHMMSFALVFAFWVSWLPWILLRLYEVVTGDVIQSTLINFAVVWIGILNSFWKILIMTSMSPQFRIALRVFCLTICCKTKGRLQAELIGLDPDD
Protein: Sulfide:quinone oxidoreductase, mitochondrial (SQOR) (EC 1.8.5.8) (Sulfide quinone oxidoreductase) (Q9R112)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone-10, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro). It is believed the in vivo electron acceptor is glutathione.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9Y6N5}.
Interaction partners:
- Persulfide dioxygenase ETHE1, mitochondrial
- Methanethiol oxidase
- Selenium-binding protein 2
- Sulfite oxidase, mitochondrial
- Thiosulfate sulfurtransferase
Sequence:
MAPLVTVVSSPRARLFACFLRLGTQQAGPLQLHTGACCTAKNHYEVLVLGGGAGGITMATRMKRRVGAENVAIVEPSERHFYQPIWTLVGAGAKELSLSVRSTLSVIPSGVQWIQDRVAELNPDENCIRTDSGKEISYRYLIIALGIQLDYEKIKGLPEGFAYPKIGSNYSVKTVEKTWKALQGFKEGNALFTFPNTPVKCAGAPQKIMYLSEAYFRKTGKRPKANIIFNTALGTIFGVKKYADALQEIIRERDVSVNYKHNLIEVRPDKQEAVFEILDKPGETHVIPYEMLHVTPPMSAPDVLKRSPVADSAGWVDVDKETLQHKKYPNVFGIGDCTNLPTSKTAAAVAAQSGILDRTMCLIMKNQRPIKKYDGYTSCPLVTGYNRVILAEFDYTAQPLETFPFDQSKERITMYLMKADMMPFLYWNMMLRGYWGGPAFLRKLFHLGMN
Protein: 3-oxo-5-alpha-steroid 4-dehydrogenase 2 (EC 1.3.1.22) (5 alpha-SR2) (SR type 2) (Steroid 5-alpha-reductase 2) (S5AR 2) (Type II 5-alpha reductase) (P31213)
Organism: Homo sapiens (Human)
Function: Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Subcellular location: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 17-beta-hydroxysteroid dehydrogenase type 3
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Aldo-keto reductase family 1 member C3
- Aldo-keto reductase family 1 member C2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- Aromatase
- Aldo-keto reductase family 1 member C4
- 17-beta-hydroxysteroid dehydrogenase type 2
- Aldo-keto reductase family 1 member D1
Sequence:
MQVQCQQSPVLAGSATLVALGALALYVAKPSGYGKHTESLKPAATRLPARAAWFLQELPSFAVPAGILARQPLSLFGPPGTVLLGLFCLHYFHRTFVYSLLNRGRPYPAILILRGTAFCTGNGVLQGYYLIYCAEYPDGWYTDIRFSLGVFLFILGMGINIHSDYILRQLRKPGEISYRIPQGGLFTYVSGANFLGEIIEWIGYALATWSLPALAFAFFSLCFLGLRAFHHHRFYLKMFEDYPKSRKALIPFIF
Protein: Activator of transcription and developmental regulator AUTS2 a (Autism susceptibility candidate 2a variant 1a) (Autism susceptibility gene 2 protein isoform X1) (E7F4D0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Polycomb group RING finger protein 5-B
- E3 ubiquitin-protein ligase RING2
- YY1-associated factor 2.
- Casein kinase II subunit beta
- Polycomb group RING finger protein 1
- DDB1- and CUL4-associated factor 7
- RING1 and YY1-binding protein B
- Polycomb group RING finger protein 5-A
- SH2 domain-containing 4A.
- Engulfment and cell motility 2.
Sequence:
MDGPRCSGIRKKRKSRSVRNRERISNGIRNNHVRGSVLRFSSDSEKEDGSTNPSSSSRPRPPRRKRKESSSAEEDIIDGFSIAGFMTLEALEKDMTLKPHERRQNQAGPLRKKKPGRVANGLSLDLHKDRLNHSNHQHSDQENNPRLARTHSKKKKKKHLQKKHRPLKPGQNNCKDSDSESVSGESKPSIRSSSRDRLTDCDSESDQEDKGSDASSEKLFSTAAVKVPDFSVDTLSTNASQELRGLGIPKVSGLERSQEKSQETSREISSATPPLVPTSHSKPPLPAPLHLQPPPSSRGLPLPSRPAQIQNPCPERTLRPLSPPIALPQSQGQELSQAPPHPSQHPPESPSHPKPPRTPSIYHHPPSPALPAQQNPTQPVQHRPPSRCHQRPISAYSGSLTLNGLSSSRSSTPGKPPGPSPAPHLHHHQPAPTGASASFPLPLSANPTASHTFPPSLPSSTLPHHTNMFASPAALPPPPPLTSNTLPVPGHPAGSAYSEQDILRQELNTRFLASQSADRGASLGPPPYLRTEFHQHQHQHQHQHQHTHQHTHQHTFTPFPHAIMPTPAPPMVRTPARNFEKYPTKVDPFYRHSLFHSYPPAVSGIPPVIPPTGPFGSLQGAFQPKTSNPLDVAARPGAVPHTLLQKDPRLTDPFRPVLRKPGKWCAMHVHIAWQIYHHQQKVKQQMQVDPHKLDFGLKPEFLSRPPGPTLFGAIHHPHDLARPASLFSAAGSTHPAAAPFGHPPHHPSNFLTPAPHLEPFSRPPSFGGLASLSTAAFGGLGNPALASNSVFGHKDSPSAQQHFSGPHEPWNRLHRTPPSFPTPPPWLKPGESERSASVSSHERERERDRERERDLDKRDSSVNKDDKEREPVEKRHQNHQSPLPVNPLTLLGHTRPSEPSRNHISSSEPRDKDKDKPKDRERDREHSDWKDSNTDEHKLKENHHSDKDTPVIHDGRVSEDKPANRITASPYMRPGGMDRVNGGLTRDILEKKAEITYEKKNSEVKVKEERKEEQDGPTERSPEQRSTPQAPPPPPPAALHPPSSMPVPMGMASMHPINSISSLERTRMVAPFMGISPIPGAERFPYPAFHWDPMRDPYRGLDIHRRDPLARELLLRNDPLHRLAAPRLYEAERSYRDREPHDFNRDHPHGLTLEQRREQERAHLEERERLHLLREDYEQGRLHPMHHPVLDGHLPHPGLMAPGLPSMHYPRVSPSSAVAAAAQNGILNKTPPTASLSAPPPLIPTLGARSSSPRRTTPLGPDIRDRPPSHTHKDIEAR
Protein: COMM domain-containing protein 1 (Protein Murr1) (Q8K4M5)
Organism: Mus musculus (Mouse)
Function: Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Involved in the regulation of membrane expression and ubiquitination of SLC12A2. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes. Promotes CFTR cell surface expression through regulation of its ubiquitination. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1. Negatively regulates neuroblastoma G1/S phase cell cycle progression and cell proliferation by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a FAM107A- and actin-dependent manner.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8N668}. Cytoplasm {ECO:0000250|UniProtKB:Q8N668}. Endosome membrane {ECO:0000250|UniProtKB:Q8N668}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8N668}. Early endosome {ECO:0000250|UniProtKB:Q8N668}. Recycling endosome {ECO:0000250|UniProtKB:Q8N668}. Note=Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity). {ECO:0000250|UniProtKB:Q8N668}.
Interaction partners:
- Cullin-2
- Coiled-coil domain-containing protein 22
- Coiled-coil domain-containing protein 93
- COMM domain-containing protein 6
- Histone acetyltransferase KAT2A
- Suppressor of cytokine signaling 1
- COMM domain-containing protein 5
- COMM domain-containing protein 2
- COMM domain-containing protein 9
- COMM domain-containing protein 3
Sequence:
MAGDLEGGKSLSGLLSGLAQNAFHGHSGVTEELLHSQLYPEVPPEEFRPFLAKMRGLLKSIASADMDFNQLEAFLTAQTKKQGGITSEQAAVISKFWKSHKIKIRESLMKQSRWDNGLRGLSWRVDGKSQSRHSTQIHSPVAIIELEFGKNGQESEFLCLEFDEVKVKQILKKLSEVEESINRLMQAA
Protein: Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.-) (A0A0H2US80)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MVVKVGINGFGRIGRLAFRRIQNVEGVEVTRINDLTDPVMLAHLLKYDTTQGRFDGTVEVKEGGFEVNGKFIKVSAERDPEQIDWATDGVEIVLEATGFFAKKEAAEKHLKGGAKKVVITAPGGNDVKTVVFNTNHDVLDGTETVISGASCTTNCLAPMAKALQDNFGVVEGLMTTIHAYTGDQMILDGPHRGGDLRRARAGAANIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPTPTGSVTELVAVLEKNVTVDEVNAAMKAASNESYGYTEDPIVSSDIVGMSYGSLFDATQTKVLDVDGKQLVKVVSWYDNEMSYTAQLVRTLEYFAKIAK
Protein: Protein interacting with APP tail-1, isoform B (M9PGT5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGQQLVVLIPKINPNSPKTLYDLSLQALIGSMNTKIPALDRISRLAELPRNLLIDVYEMMSQQESLKDTLLEELAQLEVFARLVRYPFARSQLLRIMASLMASQKMLAKRLSENYVSRYEVVAGHEEEELESSMDTVEDRSTEFSSLYTYDSESTNADSISDFNDEFSADIGSIVGLPHRRATQEELDAINDSGLEELSAVELQVIDLGLRLGSFLSEAGWMQESITVLACLNVRLKDLPTHKHWLQFRLDCLQRLLYAESAHCNFKEAEKTYAELMGLNKWLNKSVPNQLVAITYSQISAMYFARNEYKNSHLWSGLAMRFLKGYANPRTIIDVLRQAAKACVVKRDFARANLLICQAVRRAREYFGPTHQKYGDALLDYGFFLLNVDSVFQSVNIYKEALAVRRGIFGNMNFHVAIAHEDLSYAYYVHEYSTGDFSCAQDHVDKAVNIMQHLVPSNHLMLASAKRVKALLLEEIALDKMADGIDEEDLLLQSEELHNFALLLSLQVFGEVNVQTAKHYGNLGRLYQTMNRFEEAERMHKKAIKIKSELLGHFDYEVGLSIGHLASLYNYQMKKYRDAEQLYMRSIDISLRLFGNSYSGLEYDYLGLCHVYETLHNFEKYLKYAHKLENWQMLRGQNLTQNSSYPAIEVDYSIEEVKAKYFSMCASKKSAHPSVHEEDTVNEN