wanglab/gogpt-training-data huggingface dataset:
Protein: GATA-type domain-containing protein (O62020)
Organism: Caenorhabditis elegans
Interaction partners:
- Actin-related protein 2/3 complex subunit
- Serpentine receptor class delta-45
- Teneurin-1
- PCI domain-containing protein
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-1
- 26S proteasome non-ATPase regulatory subunit 4
- Uncharacterized protein ZK688.5
- Proteasome subunit alpha type-1
Sequence:
MSYEMNSLFSSNQQPLGGGPPPQQQSQQQQQPPQSLWSLQQFSQMGAPDNFGNHAVPFMPTLGMLNQYQNPHPLQMVPPQPLVTPSQVLPPSMAEQQRADTIHGFGVLTWLSAKAGLITCKDKMIISFQLKDFCDQMLNDLTSVLRVGFTLSFHAALNETSEYTATIVSPIYGPDADVLFANSQEVDLEAANPTPPNSKDAYSPALEQKAIPALLAIFQRHGLQQIQLSRSFSLHSQMSNCGDDELFRYVGTSSLKRRQFVERRTHLFRLQNDDSIILQYPAVYQAVYQLASYLLRRGGATSIQSLFDYYGSPDIMPEVRSHTGEGRQDFLNLLTAHNWVFALFPNRTYVSVRRNLPNYDYVGFIKQHFQEMDITRSQQMAYGQPPRGIQRTMSAQMGSSFATGRPQNLLMQHQHAMTPAATRSGSLWDSQSSLSQSGNSGDQWSPLFSPSTWSNNTNANPRLTSLTPLSSMNETLLSGVNYNSLLAMPPSAKNERSIGVQADDFLDRMSYNPIGRTGCTCQCQCGRGGAAIIGNTRGSSSRASGGSASPPSADGASQIDRFSPSNHAGSIGDRTLTAAALGVGLVDQQPAAPNHDGSANQPQRYYDPFGTADLLNGTRLNSLRIGN
Protein: NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9) (Q5AEC9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MFTRSLIKGGGRLATTRSLVNNSTSLVLKNQFKKYSTSTPPKVAKSKSSTIGKIFRYTFYTAVISVIGSAGLIGYKIYEESQPVDQVKQTPLFPNGEKKKTLVILGSGWGAISLLKNLDTTLYNVVIVSPRNYFLFTPLLPSVPTGTVELRSIIEPVRSVTRRCPGQVIYLEAEATNINPKTNELTLKQSTTVVSGHSGKDTSSSKSTVAEYTGVEEITTTLNYDYLVVGVGAQPSTFGIPGVAENSTFLKEVSDASAIRRKLMDVIEAANILPKDDPERKRLLSIVVCGGGPTGVEAAGEIQDYIDQDLKKWVPEVADELKVSLVEALPNVLNTFNKKLIDYTKEVFKDTNINLMTNTMIKKVNDKSLIANHKNPDGSTESIEIPYGLLIWATGNAPRDFTRDLIAKVDEQKNARRGLLVDERLKVDGTDNIFALGDCTFTKYPPTAQVAFQEGEYLANYFDKLHAVESLKYTIANPTPKDNVEKLSRKLARLEKNLPHFIYNYQGSLAYIGSEKAVADLVWGDWSNISSGGNLTFLFWRSAYIYMCLSVKNQVLVVLDWAKVYFFGRDCSKE
Protein: ZZ-type domain-containing protein (Q38AH5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRHGSHPEHPMQAFPNPVAGLLCSICKASAHPSMTEWYHCAQEGCRYTLCRKCQEIDEQLFDTPQVVIRSPILAYDNMDVCLRTRPRNNAHVLCPLYPARLMVAVASARGSIDPTETYYRLGNGGWTNAAHVVRVVPSQQLIEELAGAHLVGGDCSPSDRMSLRDLLDCIDESFRLMEQRSPYGLVMASLIYYPLIQYCSDWGNVSSEGRVAFVRASLGFIHYVFHYVLDELNQWLENYDPMVKTTILSLYVELLGKSLTVARDLALSQAIALPSELGPLVVETARVIVELVPVLDNGRRHHIDMGKSSMRDPSVALHQRDFGEEQLRLLSCCQGIVETAGWLLLHVPVFTYGRSDILPFRVAVSFIPNSECLERLLCQVTTSALEKDATLQKRVHDLDVVEVAVSLAARASCAESQLAVFRVIAAVAHESPGNISQIAPLVIAPLIKLATKALNTLVANAAFDCFTELAYNEPRPNHHSCDVGNEETESPSLCSAVLHPNTAPYQTMHAYKIAGRQVLLCEYCSQTHLPAGSVPSMTPQRAHFHCYCRYCPNEHVTQTSRSPTVGPTSAIQLMINEGITHLMLFWLRCGEFAVANTVGRLSLKIAVPPEVIVTLYHALLRQSLVGYADAALAVAAQAYLPVVKEMQRRYPNAAISQYLSQESSSVGCKSLFADCTPGEDTDGNDVDGLSPSPDIALRSSDGGSVVSSVSPPVTDLFTMPNGYLNVAI
Protein: Bruchpilot, isoform M (A0A0B4KF38)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MGSPYYRDMDEPTSPAGAGHHRSRSASRPPMAHAMDYPRTRYQSLDRGGLVDPHDREFIPIREPRDRSRDRSLERGLYLEDELYGRSARQSPSAMGGYNTGMGPTSDRAYLGDLQHQNTDLQRELGNLKRELELTNQKLGSSMHSIKTFWSPELKKERALRKEESAKYSLINDQLKLLSTENQKQAMLVRQLEEELRLRMRQPNLEMQQQMEAIYAENDHLQREISILRETIKDLECRVETQKQTLIARDESIKKLLEMLQAKGMGKEEERQMFQQMQAMAQKQLDEFRLEIQRRDQEILAMAAKMKTLEEQHQDYQRHIAVLKESLCAKEEHYNMLQTDVEEMRARLEEKNRLIEKKTQGTLQTVQERNRLTSELTELKDHMDIKDRKISVLQRKIENLEDLLKEKDNQVDMARARLSAMQAHHSSSEGALTSLEEAIGDKEKQMAQLRDQRDRAEHEKQEERDLHEREVADYKIKLRAAESEVEKLQTRLERAVTERERLEIKLEASQSELGKSKAELEKATCEMGRSSADWESTKQRIARLELENERLKHDLERSQVLTTFGRTTMTTSQELDRAQERADKASAELRRTQAELRVTQMERDDAVTEVEILKEKLDKALYASQKLIDEKDTSNKEFEKMLEKYDRAQNEIYRLQSRCDTAEADRARLEVEAERSGLAASKAREDLRKLQDESTRLQEACDRAALQLSRAKECEDNARSELEHSRDRFDKLQTDIRRAQGEKEHFQSELERVTYELERAHAAQTKASASVEAAKEEAAHYAVELEKMRDRYEKSQVELRKLQDTDTFGRETRRLKEENERLREKLDKTLMELETIRGKSQYESESFEKYKDKYEKIEMEVQNMESKLHETSLQLELSKGEVAKMLANQEKQRSELERAHIEREKARDKHEKLLKEVDRLRLQQSSVSPGDPVRASTSSSSALSAGERQEIDRLRDRLEKALQSRDATELEAGRLAKELEKAQMHLAKQQENTESTRIEFERMGAELGRLHDRLEKAEAEREALRQANRSGGAGAAPHPQLEKHVQKLESDVKQLAMEREQLVLQLEKSQEILMNFQKELQNAEAELQKTREENRKLRNGHQVPPVAAPPAGPSPAEFQAMQKEIQTLQQKLQESERALQAAGPQQAQAAAAAGASREEIEQWRKVIEQEKSRADMADKAAQEMHKRIQLMDQHIKDQHAQMQKMQQQMQQQQQAAQQAVQQAAQQQQSAAGAGGADPKELEKVRGELQAACTERDRFQQQLELLVTELEKSKMSNQEQAKQLQTAQQQVQQLQQQVQQLQQQMQQLQQAASAGAGATDVQRQQLEQQQKQLEEVRKQIDNQAKATEGERKIIDEQRKQIDAKRKDIEEKEKKMAEFDVQLRKRKEQMDQLEKSLQTQGGGAAAAGELNKKLMDTQRQLEACVKELQNTKEEHKKAATETERLLQLVQMSQEEQNAKEKTIMDLQQALKIAQAKVKQAQTQQQQQQDAGPAGFLKSFF
Protein: Neuromedin-B receptor (NMB-R) (Epididymis tissue protein Li 185a) (Neuromedin-B-preferring bombesin receptor) (P28336)
Organism: Homo sapiens (Human)
Function: Receptor for neuromedin-B. Contributes to the maintenance of basal sigh rate through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR-expressing neurons in the sneeze-evoking region of the brainstem (By similarity). These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response (By similarity). Contributes to induction of acute itch, possibly through its activation on dorsal root ganglion neurons by the NMB peptide (By similarity). Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6. Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to the positive regulation of the expression of the CSF1 receptor CSF1R (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuromedin-B
- Gastrin-releasing peptide
- Bombesin receptor subtype-3
- Gastrin-releasing peptide receptor
- Toll-like receptor 4
- Neurotensin/neuromedin N
Sequence:
MPSKSLSNLSVTTGANESGSVPEGWERDFLPASDGTTTELVIRCVIPSLYLLIITVGLLGNIMLVKIFITNSAMRSVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWMFGKVGCKLIPVIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGALLRTCVKAMGIWVVSVLLAVPEAVFSEVARISSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLAIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFIFCWFPNHILYMYRSFNYNEIDPSLGHMIVTLVARVLSFGNSCVNPFALYLLSESFRRHFNSQLCCGRKSYQERGTSYLLSSSAVRMTSLKSNAKNMVTNSVLLNGHSMKQEMAL
Protein: DNAse I-like superfamily protein (F4J8R6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MRCVNRVDCSWSRPSEAYRILPSGGHLSSGFHQCPLSSLSFRSSFVCCSSSTSGPSDSNPESSSNRSYSRRWQNPLPRRQHPDQIPSSQIARDWIDSDTTPVSQALERFTVVSYNILGDGNSSYHRELYSNVSVPYLKWGYRKRLICEELIRLNPDIISMQEVDKYFDLFSMMEKAGYAGSYKRRTGDNVDGCAMFWKADRFGVLERENIEFSQFGMRDNVAQLAVLELRKSNKSRKILLGNIHVLYNPNQGDVKLGQVRSLCSKAHLLSKKWGDIPIVLCGDFNSTPKSPLYNFLASSELNVMEHDKKELSGQKNCRPTKVLETGSKSSNTITFRSFCSSWTKEEIRVATGQENSYWAAHPLKLNSSYASVKGSANTRDSVGEPLATSYHSKFLGTVDYLWYSDGLLPARVLDTLPIDVLCKTKGLPCQELGSDHLALVSEFVFEPDG
Protein: cAMP-dependent protein kinase type II-alpha regulatory subunit (P05207)
Organism: Sus scrofa (Pig)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Hormone-sensitive lipase
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- Protein kinase cAMP-dependent type II regulatory subunit beta
- Protein kinase cAMP-dependent type I regulatory subunit beta.
- Protein kinase cAMP-dependent X-linked catalytic subunit
- non-specific serine/threonine protein kinase
- A-kinase anchor protein 10, mitochondrial
- 5'-AMP-activated protein kinase subunit gamma-3
Sequence:
SGSQDLEPSSGLVTDAIADSESEDDEDLDVPIPSRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERTVKVDEHVIDQRDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMY
Protein: Probable E3 ubiquitin-protein ligase IRF2BPL (EC 2.3.2.27) (Enhanced at puberty protein 1) (Interferon regulatory factor 2-binding protein-like) (Q2MJS2)
Organism: Macaca mulatta (Rhesus macaque)
Function: Probable E3 ubiquitin protein ligase involved in the proteasome-mediated ubiquitin-dependent degradation of target proteins. Through the degradation of CTNNB1, functions downstream of FOXF2 to negatively regulate the Wnt signaling pathway. Probably plays a role in the development of the central nervous system and in neuronal maintenance (By similarity). Also acts as a transcriptional regulator of genes controlling female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:17627301}.
Interaction partners:
Sequence:
MSAAQVSSSRRQSCYLCDLPRMPWAMIWDFSEPVCRGCVNYEGADRIEFVIETARQLKRAHGCFQDGRSPGPPPPVGVKTVALSAKEAAAAAAAAAAAAAAAQQQQQQQQQQQQQQQQQQQQQQQLNHVDGSSKPAVLAAPSGLERYGLSAAAAAAAAAAAAVEQRSRFEYPPPPVSLGSSSHATRLPNGLGGPNGFPKPTPEEGPPELNRQSPNSSSAAASVASRRGTHGGLVTGLPNPGGGGGPQLTVPPNLLPQTLLNGPASAAVLPPPPPHALGSRGPPTPAPPGAPGGPACLGGTPGVSATSSSASSSTSSSVAEVGVGAGGKRPGSVSSTDQERELKEKQRNAEALAELSESLRNRAEEWANKPKMVRDTLLTLAGCTPYEVRFKKDHSLLGRVFAFDAVSKPGMDYELKLFIEYPTGSGNVYSSASGVAKQMYQDCMKDFGRGLSSGFKYLEYEKKHGSGDWRLLGDLLPEAVRFFKEGVPGADMLPQPYLDASCPMLPTALVSLSRAPSAPPGTGTLPPAAPSGRGAAASLRKRKASPEPPDSAEGALKLGEEQQRQQWMANQSEALKLTMSAGGFAAPGHAAGGPPPPPPPLGPHSNRTTPPESAPQNGPSPMAALMSVADTLGTAHSPKDGSSVHSTTASARRNSSSPVSPASVPGQRRLASRNGDLNLQVAPPPPSAHPGMDQVHPQNIPDSPMANSGPLCCTICHERLEDTHFVQCPSVPSHKFCFPCSRESIKAQGASGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP
Protein: Scavenger receptor class F member 2 (Scavenger receptor expressed by endothelial cells 2 protein) (SREC-II) (P59222)
Organism: Mus musculus (Mouse)
Function: Probable adhesion protein, which mediates homophilic and heterophilic interactions. In contrast to SCARF1, it poorly mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEGAGSRGAGPARRQGARGLGLLLLLWLLPGLAAPQDLNPRGRNVCRTPGSQVLTCCAGWRQLGDECGIAVCEGNSTCSENEVCVRPGECRCRHGYFGANCDTKCPRQFWGPDCKERCSCHPHGQCEDVTGQCTCHARRWGARCEHACQCQHGTCHPRSGACRCEPGWWGAQCASACYCSATSRCDPQTGACLCHVGWWGRSCNNQCACNSSPCEQQSGRCQCRERMFGARCDRYCQCSHGRCHPVDGTCACDPGYRGKYCREPCPAGFYGPGCRRRCGQCKGQQPCTVVEGRCLTCEPGWNGTKCDQPCATGFYGEGCGHRCPPCRDGHACNHVTGKCTHCNAGWIGDRCETKCSNGTYGEDCAFVCSDCGSGHCDFQSGRCLCSPGVHGPHCNVTCPAGLHGVDCAQACSCHEESCDPVTGACHLETNQRKGVMGAGALLTLLLGLLLSLLGCCCACRGKDSARRELTLGRKKAPQRFCGSFSRISMKLPRIPLRRQKLPKVVVAHHDLDNTLNCSFLDPPSGLEQPSPSWSSRASFSSFDTTDEGPVYCVPHEEATADSRDLEATAALTEVAAVSLEPTGTSTPGEEAAVLPASSDSERSASSVEGPSGALYARVARREARPARTRNEAGGLSLSPSPERRKPPPPDPATKPKVSWIHGKHSAAAAAPSPPPAGRKAAPSPSGRKRTPSNSSVQPPGLTEEAPGPASPTPPRARARGRGLGLSEPTDAGGPPRSAPEAASMLAAELRDKTRSLGRAEKPPPPQKAKRSVLPAATVRTASASEASGSEKAAASAPAPETPRKKTPIQKPPRKKSREAAGEPSRAGTAPGAS
Protein: RNA pyrophosphohydrolase (EC 3.6.1.-) ((Di)nucleoside polyphosphate hydrolase) (Ap5A pyrophosphatase) (P0A776)
Organism: Escherichia coli (strain K12)
Function: Master regulator of 5'-end-dependent mRNA decay. Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. Preferentially hydrolyzes diadenosine penta-phosphate with ATP as one of the reaction products. Also able to hydrolyze diadenosine hexa- and tetra-phosphate. Has no activity on diadenosine tri-phosphate, ADP-ribose, NADH and UDP-glucose. In an RNase PH (rph) wild-type strain background, RppH is not required for maturation of tRNAs; however, strains with the truncated rph allele (for example K12 W1485 and its derivatives MG1655 and W3110) require RppH for maturation of certain monocistronic tRNAs with short (<5 nucleotides) leader sequences. In the meningitis causing strain E.coli K1, has been shown to play a role in HBMEC (human brain microvascular endothelial cells) invasion in vitro.
Interaction partners:
- Diaminopimelate epimerase
- Ribonuclease R
- Ribonuclease E
- RNA-binding protein Hfq
- ATP-dependent RNA helicase RhlB
- Phosphoenolpyruvate-dependent phosphotransferase system
- Bis
- NAD-capped RNA hydrolase NudC
- Ribonuclease G
- Polyribonucleotide nucleotidyltransferase
Sequence:
MIDDDGYRPNVGIVICNRQGQVMWARRFGQHSWQFPQGGINPGESAEQAMYRELFEEVGLSRKDVRILASTRNWLRYKLPKRLVRWDTKPVCIGQKQKWFLLQLVSGDAEINMQTSSTPEFDGWRWVSYWYPVRQVVSFKRDVYRRVMKEFASVVMSLQENTPKPQNASAYRRKRG
Protein: Ovocalyxin-32 (OCX-32) (32 kDa eggshell matrix protein) (Q90YI1)
Organism: Gallus gallus (Chicken)
Function: Component of the matrix of the eggshell.
Subcellular location: Secreted.
Interaction partners:
- Ovocleidin-116
- Ovotransferrin
- Ovotransferrin
- Uncharacterized protein.
- Ovotransferrin
- Ovomucoid
Sequence:
MPGLRAALPAALLLLSSFPPAAAERLPWPQVPGVMRPLNPSHREAVWAAWTALHYINSHEASPSRPLALHKVVKAASKMIPRLGWKYYVHCTTEGYIHGENAGSCFATVLYLKKSPPVVHGKCVHAQNKKQIQEEDHRFYEYLQHQKKPITANYIPDSNGNIAHDHLQLWGLAIVGSSYIMWKQSTEHTGYLLAQVSSVKQQIRKDNAVAFKFIVLLHEIPTQQLNVCHMYLVWTLGHPIRVKYSCAPDNHGLEDGSGQDSGSAAGTSHETKGNF
Protein: Lymphocyte antigen 6G6e (Lymphocyte antigen 6 complex locus protein G6e) (Q8K1T6)
Organism: Mus musculus (Mouse)
Function: Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro potentiates alpha-3:beta-4-containing nAChRs maximum response by increasing peak current and slowing down receptor desensitization; the activity is dependent on its cell surface localization.
Subcellular location: Cell surface {ECO:0000305|PubMed:26276394}. Cell membrane {ECO:0000269|PubMed:17008713, ECO:0000305|PubMed:26276394}. Cell projection {ECO:0000269|PubMed:17008713}.
Interaction partners:
- Lymphocyte antigen 6 complex locus protein G6c
Sequence:
MGPSSAFLGVLFLSGTLGLTTSPARGRLRCYTCSFAKPCDPVPRECREDEVCGVSVGTSGRTLVRWPFSRWLLSFLPMAAAATSAFLFCPTEQKEEEVIERKGCLPRAQCPLLGHATYWSRSYSLRHQCCEQDLCNAAASQPPPNLPLMTLLPLAAMIGWGVHDFL
Protein: Lysoplasmalogenase TMEM86B (EC 3.3.2.2) (Transmembrane protein 86B) (Q8N661)
Organism: Homo sapiens (Human)
Function: Enzyme catalyzing the degradation of lysoplasmalogen. Lysoplasmalogens are formed by the hydrolysis of the abundant membrane glycerophospholipids plasmalogens. May control the respective levels of plasmalogens and lysoplasmalogens in cells and modulate cell membrane properties.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9D8N3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:21515882}.
Interaction partners:
- Lysophospholipid acyltransferase LPCAT4
- Glycerophosphocholine cholinephosphodiesterase ENPP6
- Lysophospholipase D GDPD3
- Lysophospholipase D GDPD1
- 85/88 kDa calcium-independent phospholipase A2
Sequence:
MDAGKAGQTLKTHCSAQRPDVCRWLSPFILSCCVYFCLWIPEDQLSWFAALVKCLPVLCLAGFLWVMSPSGGYTQLLQGALVCSAVGDACLIWPAAFVPGMAAFATAHLLYVWAFGFSPLQPGLLLLIILAPGPYLSLVLQHLEPDMVLPVAAYGLILMAMLWRGLAQGGSAGWGALLFTLSDGVLAWDTFAQPLPHAHLVIMTTYYAAQLLITLSALRSPVPKTD
Protein: Transcription factor Jun (Activator protein 1) (AP1) (Proto-oncogene c-Jun) (Transcription factor AP-1 subunit Jun) (V-jun avian sarcoma virus 17 oncogene homolog) (p39) (P05412)
Organism: Homo sapiens (Human)
Function: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. Binds to the USP28 promoter in colorectal cancer (CRC) cells.
Subcellular location: Nucleus.
Interaction partners:
- Mitogen-activated protein kinase 9
- Protein c-Fos
- Mitogen-activated protein kinase 8
- Protein FosB
- Fos-related antigen 2
- Transcription factor JunD
- Fos-related antigen 1
- Transcription factor JunB
- Estrogen receptor
- Histone acetyltransferase p300
Sequence:
MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
Protein: Transcription factor BEE 3 (Basic helix-loop-helix protein 50) (AtbHLH50) (bHLH 50) (Protein Brassinosteroid enhanced expression 3) (Transcription factor EN 76) (bHLH transcription factor bHLH050) (Q8GWK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive regulator of brassinosteroid signaling.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor IBH1
- Transcription factor BIM3
- Transcription factor BIM1
Sequence:
MANLSSDFQTFTMDDPIRQLAELSNTLHHFQTFPPPFSSSLDSLFFHNQFPDHFPGKSLENNFHQGIFFPSNIQNNEESSSQFDTKKRKSLMEAVSTSENSVSDQTLSTSSAQVSINGNISTKNNSSRRGKRSKNREEEKEREVVHVRARRGQATDSHSIAERVRRGKINERLKCLQDIVPGCYKTMGMATMLDEIINYVQSLQNQVEFLSMKLTAASSYYDFNSETDAVESMQKAKAREAVEMGQGRDGSSVFHSSSWTL
Protein: Serine hydroxymethyltransferase 7 (AtSHMT7) (EC 2.1.2.1) (Glycine hydroxymethyltransferase 7) (Serine methylase 7) (Q84WV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion of serine and glycine.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Formate--tetrahydrofolate ligase
- Methylenetetrahydrofolate reductase 1
- Glycine dehydrogenase
- Glycine dehydrogenase
- Aminomethyltransferase, mitochondrial
- Phosphoserine phosphatase, chloroplastic
- AICARFT/IMPCHase bienzyme family protein
- Formyltetrahydrofolate deformylase 1, mitochondrial
- Formyltetrahydrofolate deformylase 2, mitochondrial
- Serine--glyoxylate aminotransferase
Sequence:
MDLSRSQTNFQLGFGCSHASMTPTPTPRAPIADDSINLQVDQSFRSLPTTFSPIPLQLLEQKAEKTTTVDEPKKDGGGGGDQKEDEHFRILGHHMCLKRQRDCPLLLTQSKHPKRSSIGDSDLESRRAAVRAWGDQPIHLADPDIHELMEKEKQRQVRGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIENLCIERALTAFGLESDKWGVNVQPYSCTSANFAVYTGLLLPGERIMGLDSPSGGHMSHGYCTPGGKKISAASIFFESFPYKVNPQTGYIDYDKLEDKALDYRPKILICGGSSYPRDWDFARVRQIADKCGAVLMCDMAHISGLVATKECSNPFDHCDIVTSTTHKGLRGPRGGIIFYRRGPKIRKQGHHSSHCDTSTHYDLEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYIQQMKKNAQALAAALLRRKCRLVTGGTDNHLLLWDLTPMGLTGKVYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTTRGCIESDFETMADFLIKAAQITSALQREHGKSHKEFVKSLCTNKDIAELRNRVEAFALQYEMPASLIRIE
Protein: GH09064p (Gasz) (Q7K5K0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable RNA helicase armi
- Mitochondrial cardiolipin hydrolase
- Inactive peptidyl-prolyl cis-trans isomerase shutdown
- Probable ATP-dependent RNA helicase spindle-E
- Protein vreteno
- Daedalus, isoform A
- Protein aubergine
- Gametocyte-specific factor 1 homolog
- Putative ATP-dependent RNA helicase SoYb
- Protein piwi
Sequence:
MMSNLCKYGPPPDSDSDSSYDGFYFSDKVKRSKPAPYVDPEQKLYDAVVAGDLKTMQEEMRKLVLQVDQPVKGGLNLLMLACREGHYKIVEWLLERAGANVNRQLDSLMPLMMACNTTHKDPCLAERIVGLLLRHGAVINVSEKYGMTPFMFACQNGFAGVVRLLIKDASFDAVDNQGCTAIFHAIEKNHVEVVKLLVEAGANATIANNKGYTPTQVAECHGYYDLLEILPRPASTYLVPTHFLGYNTLRDHIPRIFLKSDCPEYFQELNGILEAINIGNMVQYFAIARISLADFLVMDEQSLREIGIEYPIFRHKILTGILDFHLHHWSNSSIARVKKDEMNNFYEILLITASHLQHLVIIQASLRFILKNQEHNKMGQPSEMQVAAMKSNLQGYRDVLNQITKTVKYLGSFSPSQNPLFIDFNEILAERKRKKVRSYFKYTTIILGISVFICLKCKWFS
Protein: Polycystin-2 (B4DFN3)
Organism: Homo sapiens (Human)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEVKSDLAQQKAEMELSDLIRKGYHKALVKLKLKKNTVDDISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQMRDDLEKEREDLDLDHSSLPRPMSSRSFPRSLDDSEEDDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDERLGRDSEIHREQMERLVREELERWESDDAASQISHGLGTPVGLNGQPRPRSSRPSSSQSTEGMEGAGGNGSSNVHV
Protein: Auxilin (EC 3.1.3.-) (DnaJ homolog subfamily C member 6) (O75061)
Organism: Homo sapiens (Human)
Function: Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q27974}. Note=Appears on coated vesicles in successive transient bursts, immediately after the vesicle release from the plasma membrane. Recruitment to clathrin-coated vesicles depends on temporal variations in phosphoinositide composition of clathrin-coated vesicles. {ECO:0000250|UniProtKB:Q27974}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Clathrin heavy chain 1
- Clathrin heavy chain 2
- Clathrin heavy chain linker domain-containing protein 1
- Synaptojanin-1
- Clathrin light chain A
- Clathrin interactor 1
- DnaJ homolog subfamily C member 13
- Endophilin-A1
- Vacuolar protein sorting-associated protein 35
Sequence:
MKDSENKGASSPDMEPSYGGGLFDMVKGGAGRLFSNLKDNLKDTLKDTSSRVIQSVTSYTKGDLDFTYVTSRIIVMSFPLDNVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAIRLLYAKRPGIGLSPSHRRYLGYMCDLLADKPYRPHFKPLTIKSITVSPIPFFNKQRNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVVVSMYHLRSTIGSRLQAKVTNTQIFQLQFHTGFIPLDTTVLKFTKPELDACDVPEKYPQLFQVTLDVELQPHDKVIDLTPPWEHYCTKDVNPSILFSSHQEHQDTLALGGQAPIDIPPDNPRHYGQSGFFASLCWQDQKSEKSFCEEDHAALVNQESEQSDDELLTLSSPHGNANGDKPHGVKKPSKKQQEPAAPPPPEDVDLLGLEGSAMSNSFSPPAAPPTNSELLSDLFGGGGAAGPTQAGQSGVEDVFHPSGPASTQSTPRRSATSTSASPTLRVGEGATFDPFGAPSKPSGQDLLGSFLNTSSASSDPFLQPTRSPSPTVHASSTPAVNIQPDVSGGWDWHAKPGGFGMGSKSAATSPTGSSHGTPTHQSKPQTLDPFADLGTLGSSSFASKPTTPTGLGGGFPPLSSPQKASPQPMGGGWQQGGAYNWQQPQPKPQPSMPHSSPQNRPNYNVSFSAMPGGQNERGKGSSNLEGKQKAADFEDLLSGQGFNAHKDKKGPRTIAEMRKEEMAKEMDPEKLKILEWIEGKERNIRALLSTMHTVLWAGETKWKPVGMADLVTPEQVKKVYRKAVLVVHPDKATGQPYEQYAKMIFMELNDAWSEFENQGQKPLY