wanglab/gogpt-training-data huggingface dataset:
Protein: N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (N-acyl phosphatidylethanolamine phospholipase D) (NAPE-PLD) (NAPE-hydrolyzing phospholipase D) (EC 3.1.4.54) (Q58CN9)
Organism: Bos taurus (Bovine)
Function: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid (By similarity). Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
Interaction partners:
- Fatty-acid amide hydrolase 1
- Monoacylglycerol lipase ABHD6
- Diacylglycerol lipase-alpha
- Glycerophosphodiester phosphodiesterase 1
- G protein-coupled receptor 55
- N-acylethanolamine-hydrolyzing acid amidase
- Diacylglycerol lipase-beta
- 
- Lysophosphatidylserine lipase ABHD12
- Transient receptor potential cation channel subfamily V member 1
Sequence:
MDENETNQLLMTSNQYPKEAVRKRQNSRNSGGSDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNPSIPSLLRWVITERDHSSVPCSKELDKELPVLKPYFIDDPEEAGVRGAGLRVTWLGHATVMVEMDELILLTDPIFSARASPSQRMGPKRFRRAPCTVEELPRIDAVLVSHNHYDHLDCNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCSAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVKIHIDVQAKKSVAIHWGTFALANEHYLEPPAKLCEALEKYRLKTEDFLVLKHGESRYLNTDDEDVE
Protein: Zinc finger protein indra (Q8IRH5)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:35895823}. Nucleus, nucleolus {ECO:0000269|PubMed:35895823}. Note=Localizes to the nucleolus (the site of rDNA transcription) during interphase and rDNA loci during metaphase. {ECO:0000269|PubMed:35895823}.
Interaction partners:
- Relative of woc, isoform C
Sequence:
MRNILLCENMTKVQKEVRCDHCGTSQGSKSVFSGQKVFLGRKITDVLETITHRSIPSSLPIKICFVCTSTFMSSAALIEKVRETVDRVQEQPAKKTKVAEIEEPSTQESDKKAVKVPKKNTTLRQRSKSIAAFPPSFVNGANTNTEIEIISASPKKLDKTPKKQISRLFEDNLNDSVKLTPAKEVSSTKKAFLNLFGNGGNDAIEVLTESEEEEDSDKGPITINTNNFQCPECEFHAKFPKPYKEHLQKEHGLQRPRIYPCTLCIKTFGVLKTLKNHLRDTHSRTFESEAKTKAKESKEKEAKSGAKNKIDAKAKETNAVSQRKKPKEKKSKEKKTEIKCNVETKVVDEIDDQVNNKKGTDSEDADQTQATKIASFKALNESLMKKRMLENVIDSEYTFAINGSSASTPRADSNNFQCEICDCELMTAKQMQEHMKTVHSIDKPKVFKCHVCEKSLATKQSLKTHMTLHADGAEAPNSSKRKILQDEDEDVDILGTTQIENTAEKVEGPKKSQQSPTKAAKFTNRKILQEEDEVVEIVDAFKTDNTAEDDEGPAEEKIIRSRNNIQHQVDGGMIAPRSPAKKTKKTSHVDLSVSTTNGNSPAKSEKRKKQDKSEDTLPSSDVDIVEEINYNVRPHKKARLESIGDSTADESTLSCDRCGKFVKSRQRLDSHMEKKHAAKLQCTLCKEVYQNQMDYVAHFSNCGSEGGLPCGVANCKKVFTEANFLSSHLRKRH
Protein: Late embryogenesis abundant protein (LEA) family protein (F4IYB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MGWYTSFLVVVASLAVGVIFSPETFGSLTNGENSAKISIFLKLAHLLSFATAWGAALWATFIGGIIMFKNLPRHQFGNLQSKLFPAYFTLVGSCCAISLSAFGYLHPWKSSSTVEKYQIGFLLSAFAFNLTNLFVFTPMTIDMMKQRHKVERENNIGDEVGWSKNREKAKSIPKLAAMNKKFGMIHGLSSLANIFSFGSLAMHSWYLAGKLNL
Protein: Adrenocorticotropic hormone receptor (ACTH receptor) (ACTH-R) (Adrenocorticotropin receptor) (Melanocortin receptor 2) (MC2-R) (Q01718)
Organism: Homo sapiens (Human)
Function: Receptor for corticotropin (ACTH). This receptor is mediated by G proteins (G(s)) which activate adenylate cyclase (cAMP).
Subcellular location: Cell membrane {ECO:0000269|PubMed:19535343, ECO:0000269|PubMed:21862608}; Multi-pass membrane protein.
Interaction partners:
- Melanocortin-2 receptor accessory protein
- Pro-opiomelanocortin
- Melanocortin-2 receptor accessory protein 2
- VIP peptides
- Guanine nucleotide-binding protein G
- Pro-glucagon
- Thyrotropin subunit beta
- Gastric inhibitory polypeptide
- Follitropin subunit beta
- Pituitary adenylate cyclase-activating polypeptide
Sequence:
MKHIINSYENINNTARNNSDCPRVVLPEEIFFTISIVGVLENLIVLLAVFKNKNLQAPMYFFICSLAISDMLGSLYKILENILIILRNMGYLKPRGSFETTADDIIDSLFVLSLLGSIFSLSVIAADRYITIFHALRYHSIVTMRRTVVVLTVIWTFCTGTGITMVIFSHHVPTVITFTSLFPLMLVFILCLYVHMFLLARSHTRKISTLPRANMKGAITLTILLGVFIFCWAPFVLHVLLMTFCPSNPYCACYMSLFQVNGMLIMCNAVIDPFIYAFRSPELRDAFKKMIFCSRYW
Protein: Universal stress protein D (P0AAB8)
Organism: Escherichia coli (strain K12)
Function: Required for resistance to DNA-damaging agents.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- UPF0381 protein YiiS
- Universal stress protein UP12
- Universal stress protein F
- Universal stress protein E
- Universal stress protein B
- Cell division protein ZapB
- Outer membrane porin F
- Cell division protein FtsN
Sequence:
MAYKHIGVAISGNEEDALLVNKALELARHNDAHLTLIHIDDGLSELYPGIYFPATEDILQLLKNKSDNKLYKLTKNIQWPKTKLRIERGEMPETLLEIMQKEQCDLLVCGHHHSFINRLMPAYRGMINKMSADLLIVPFIDK
Protein: Nucleolar and coiled-body phosphoprotein 1 (140 kDa nucleolar phosphoprotein) (Nopp140) (Nucleolar 130 kDa protein) (Nucleolar phosphoprotein p130) (P41777)
Organism: Rattus norvegicus (Rat)
Function: Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification. Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification. Involved in nucleologenesis, possibly by playing a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1623516}. Nucleus, nucleolus {ECO:0000269|PubMed:1623516}. Note=Shuttles on curvilinear tracks between nucleolus and cytoplasm. These tracks extend from the dense fibrillar component of the nucleolus across the nucleoplasm to a limited number of nuclear pore complexes. {ECO:0000269|PubMed:1623516}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit DKC1
- Nucleolar protein 56
- Nucleolar protein 58
- rRNA 2'-O-methyltransferase fibrillarin
- H/ACA ribonucleoprotein complex subunit 1
- Ribonucloprotein
- H/ACA ribonucleoprotein complex subunit 3
- Fibrillarin-like 1
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase I subunit RPA1
Sequence:
MADTGLRRVVPSDLYPLVLGFLRDNQLSEVASKFAKATGATQQDANASSLLDIYSFWLKSTKAPKVKLQSNGPVAKKAKKETSSSDSSEDSSEEEDKAQVPTQKAAAPAKRASLPQHAGKAAAKASESSSSEESSEEEEEEDKKKKPVQQKAVKPQAKAVRPPPKKAESSESESDSSSEDEAPQTQKPKAAATAAKAPTKAQTKAPAKPGPPAKAQPKAANGKAGSSSSSSSSSSSDDSEEEKKAAAPLKKTAPKKQVVAKAPVKVTAAPTQKSSSSEDSSSEEEEEQKKPMKKKAGPYSSVPPPSVSLSKKSVGAQSPKKAAAQTQPADSSADSSEESDSSSEEEKKTPAKTVVSKTPAKPAPVKKKAESSSDSSDSDSSEDEAPAKPVSATKSPLSKPAVTPKPPAAKAVATPKQPAGSGQKPQSRKADSSSSEEESSSSEEEATKKSVTTPKARVTAKAAPSLPAKQAPRAGGDSSSDSESSSSEEEKKTPPKPPAKKKAAGAAVPKPTPVKKAAAESSSSSSSSEDSSEEEKKKPKSKATPKPQAGKANGVPASQNGKAGKESEEEEEDTEQNKKAAGTKPGSGKKRKHNETADEAATPQSKKVKLQTPNTFPKRKKGEKRASSPFRRVREEEIEVDSRVADNSFDAKRGAAGDWGERANQVLKFTKGKSFRHEKTKKKRGSYRGGSISVQVNSVKFDSE
Protein: Transmembrane protein 14C (Q9P0S9)
Organism: Homo sapiens (Human)
Function: Required for normal heme biosynthesis.
Subcellular location: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- Protoporphyrinogen oxidase
- ATP-binding cassette sub-family B member 10, mitochondrial
- Ferrochelatase, mitochondrial
Sequence:
MQDTGSVVPLHWFGFGYAALVASGGIIGYVKAGSVPSLAAGLLFGSLAGLGAYQLSQDPRNVWVFLATSGTLAGIMGMRFYHSGKFMPAGLIAGASLLMVAKVGVSMFNRPH
Protein: Corneodesmosin (Q6MG23)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGSSRAPRMGRVGGHGLMALLMAGFILPGTLAKSIGPFSDPCKDSILLLLLLLSWCFHTTPLGCPLCPITCLETHFFKSLTGKSSKHTSTLGAGISQSVPLPVCRLRQNPISHLRTKVHFSATPPPALI
Protein: Fe(3+) dicitrate transport protein FecA (Iron(III) dicitrate transport protein FecA) (P13036)
Organism: Escherichia coli (strain K12)
Function: FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system.
Subcellular location: Cell outer membrane {ECO:0000255|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Ferric citrate uptake sigma factor regulator FecR
- Fe
- Protein TonB
- Fe
- Fe
- Ferric citrate uptake sigma factor FecI
- Fe
- Biopolymer transport protein ExbB
- Biopolymer transport protein ExbD
- Ferrienterobactin receptor
Sequence:
MTPLRVFRKTTPLVNTIRLSLLPLAGLSFSAFAAQVNIAPGSLDKALNQYAAHSGFTLSVDASLTRGKQSNGLHGDYDVESGLQQLLDGSGLQVKPLGNNSWTLEPAPAPKEDALTVVGDWLGDARENDVFEHAGARDVIRREDFAKTGATTMREVLNRIPGVSAPENNGTGSHDLAMNFGIRGLNPRLASRSTVLMDGIPVPFAPYGQPQLSLAPVSLGNMDAIDVVRGGGAVRYGPQSVGGVVNFVTRAIPQDFGIEAGVEGQLSPTSSQNNPKETHNLMVGGTADNGFGTALLYSGTRGSDWREHSATRIDDLMLKSKYAPDEVHTFNSLLQYYDGEADMPGGLSRADYDADRWQSTRPYDRFWGRRKLASLGYQFQPDSQHKFNIQGFYTQTLRSGYLEQGKRITLSPRNYWVRGIEPRYSQIFMIGPSAHEVGVGYRYLNESTHEMRYYTATSSGQLPSGSSPYDRDTRSGTEAHAWYLDDKIDIGNWTITPGMRFEHIESYQNNAITGTHEEVSYNAPLPALNVLYHLTDSWNLYANTEGSFGTVQYSQIGKAVQSGNVEPEKARTWELGTRYDDGALTAEMGLFLINFNNQYDSNQTNDTVTARGKTRHTGLETQARYDLGTLTPTLDNVSIYASYAYVNAEIREKGDTYGNLVPFSPKHKGTLGVDYKPGNWTFNLNSDFQSSQFADNANTVKESADGSTGRIPGFMLWGARVAYDFGPQMADLNLAFGVKNIFDQDYFIRSYDDNNKGIYAGQPRTLYMQGSLKF
Protein: Mitochondrial transcription termination factor 4 (B5MBW3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAFGRQVLDWHRLIPLTWACMARQTPHLGEQRRTTASLLRKLTTASNGGVIEELSCVRSNNYVQEPECRRNLVQCLLEKQGTPVVQGSLELERVMSSLLDMGFSNAHINELLSVRRGASLQQLLDIISEFILLGLNPEPVCVVLKKSPQLLKLPIMQMRKRSSYLQKLGLGEAASSYSVTA
Protein: Dachshund d (Zgc:158869) (A1L2G2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAVPAALIPPSALVHPCPISTSSSASSASSSSCSATAASSSSPSATSASPSQSATQNLFRADLISTNCTSSIPLAGKPVYSTPSPVENTPQNNECRMVELRGAKVASFTVDGQELICLPQAFDLFLKHLVGGLHTVYTKLKRLEITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFETLYNDCTNASSRPGRPPKRTQSVTSPENPHIMPHTVPGLMSPGIIPPTGLTAAAAAAAAATNAAIAEAMKVKKIKLEVMSSYHGSNTHNGPDSENGDLSSSVGLELPFMMMPHPLIPVSLPPASVTMAMSQMNHLSTIANMAAAAQGQSAPSRMVTSVIKERVPDSPSPAPSLEDGRRPGSRPSSQRSSSVSSSPAHTESSSDRMPVHQNGLSMNHALLGLSPSILPGPKEGDLAHDIVHNAKRMHLEKEETPMCTPTARDSYERLSLAGQTLPPGSPSPFLFPDGLSSIETLLTNIQGLLKVAIDNARAQEKQVQLEKTELKMELFRERELRETLEKQLAVEQKNRAIIQKRLKKEKKAKRKLQEALEYESKRREQAEQTLKQTSPTESLRSLNDSLTQEIETDRSSGRTDAERTIQADGRLFLKTTVMY
Protein: DUF7168 domain-containing protein (E7DN98)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MAQKLMLKNNIALAQVEQFDEPKQFETSQAVGKEAGRIFWWERELGHILATNFRCFCINQRDMRLNKSRIIFFGEKQDAELVSKIYEAALLYLRYRIDRLPTREPSYKNSYLKGFLSALAIRFKKQVEEYSLMVLPSEQTKNALQDTFRNLKKEGIDRPQHDFNLEAYIEGRFHGENAKIMPDEILEGGN
Protein: Cellular tumor antigen p53 (Q801Z7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.
Interaction partners:
Sequence:
MSQSSTADEGPTFEHLWSTLEPDSTYFELPQAGHSGDRASSSLPGNRAEVCMDVYHMRDMRDMNDNVMSQYSLLSSSMDQGLGNRAASTSPYSSETTSNVPTPSPYSQPNSTFEAMSPAPAIPSNTDYPGPHNFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKLASSPPNGSVIRAMPIYKKAEHVTEVVKRCPNHKLGRDFNESQTAPASHLIRVEGNNLCQYVDDPVTGRQSVLVPYESPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLETRDGQVLGRRSFEGRICACPGRDRKADEDHFREQQALNESVAKNGNANKRNFKQTPTNITGPSINIKKRRHGEEEMYYIPVRGRENFDILMKIKDSLELVEFVPQQLVDSYRQQQQQLLQRQNHVASPSSYGTLNNMNKIHGPISKLPSVNQLVTQQTQQSAGPSASLSHMGANMLGGHHMQSNGDVNGAHQSQSIVSTSHCTPPPPYNPDPSLVSFLTSLGCQNCIDYFTSQGLQSVYHLQTLTMEDLGALKIPEQFRLAIWRGLQEMKQGHDYGQQLIRSSSNMATMAIGPSGELQRQRVMEAVHFRVRHTITIPNRGPANGPEEWPDFGFDMPDCRLHKHSIKEEFAEGDVH
Protein: Protein EIN6 ENHANCER (Protein ENHANCER OF ETHYLENE INSENSITIVITY 6) (Q8RWS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair (By similarity). Together with REF6/EIN6, involved in the epigenetic chromatin-dependent regulatory mechanism that monitors the expression of the essential multifunctional plant stress regulator EIN2 via H3K27me3 repressive histone demethylation and histone variant H2A.Z eviction, thus modulating responses to ethylene (ET), especially during embryogenesis. The INO80 complex controls ethylene-induced H2A.Z eviction dynamics.
Subcellular location: Nucleus {ECO:0000269|PubMed:31418686}. Cytoplasm {ECO:0000269|PubMed:31418686}.
Interaction partners:
- Actin-related protein 9
- Actin-related protein 5
- Actin-related protein 4
- RuvB-like protein 1
- DNA-binding protein-like
- RuvB-like helicase
- Chromatin-remodeling ATPase INO80
- Ubiquitin carboxyl-terminal hydrolase 2
- Ubiquitin carboxyl-terminal hydrolase
- RuvB-like helicase
Sequence:
MERELMEADIVVASRLSFKKKQAYEKYPKAQSSSRRWKHLKQILQAENFPDLPPDLPTYVNIESPPSTQPCKRLCDITGYEAPYVDPRTNLRYANAHVFQTVRSLSSDQVHQYLSIRNAAVVLK
Protein: Wolframin (E7F921)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Activating transcription factor 6
- Wolfram syndrome 1a
Sequence:
MDTSLLESQLSAPASPVSPAFSVSGHNIHPVSSSSTPSPAPSAMTPPPHHASQMGRSQLNAASNSSTAFPGQSAFPPQGEIKEELSIDDLKQRAKNGDAKAQTEIGRYYLRLAEQEDEEVNAVTAVTWLLQAAKNGRKDAVKLLQRCLHDRRGITAENREEVCSLACESRFQRSVRKAALLMYWKLNPERKKNITASELLENVSQLNTDGASRSPLSSPIQKQRKILESLVSRDETDCIGVEEFVENTKQYAEGISPSMEGVAGDDDDDDEEPVKHPDELPLHQKVLKFPLHAVLEVKEVLIDWASRAGMQWISALIPTHHVNTLIFFFIISNLTLEFFVLVIPLIIFYLSFVSMVICTLRVFQNSKAWENFRALTVMLSHFEPGIDLEQAESNFTWNHLEPYLYFLLSTLFLIFSFPVADKSWLPCSELAMVAVFFTVSSYLSLRPSAQQHAKFALLSQVASAIFTFINRLLGGWVGRIIGGAWFSMRLGDWLVMHVGVPCVLYLYLLFLCTRMATAGGARGTYCVLLPNLVCFIWCEVCVTLLQESTVLGLMRSVVGYLLFFFALPVLSLALAAVMLVQLVQWFLALELTKMIVTVCICVLPVLLRWWTRFSVSPLAVLRSLRRSSVVKLILVWISALVLFSWFYVYRSEGMKVYNSTLTWQEYSDLCGPRAWKERNMAHAQIICSHLEGHRVTWEGRFKYVRVTEIENGAQAVVNLLPVLIADWVRCLYGEEYPACDENQTGPAEPLCQLKTLAKHKCHVKRFDHYKFEVTMGMPQKGRNGAQDFDDGTKDIVLRASNEFRRVLLVLSSGSVVEFSTVLEGRLGSKWPVFELKALNCKTCASPLIPIRRQVKIEQDWRVNARNALAFAFNFVFHPLLSAEMDATAATTEVSV
Protein: AT19154p (Synthesis of cytochrome c oxidase) (Q9VMX4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|PIRNR:PIRNR037736}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase assembly protein COX11
- SURF1-like protein
- Copper transport protein ATOX1
- RE54691p
- P-type Cu
- Cytochrome c oxidase subunit 1
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase copper chaperone
- Cytochrome c oxidase subunit 3
Sequence:
MSRSLQRLVGSCRRWAQQPAIRHYAAPADSTKGKGPISWRSLAVIGALGAGGVGFMLYVKSEKDEARMKERQRQLGKAAIGGSWELVDSQGAVRKSEDFLGKWLLIYFGFTHCPDICPDELEKMAAVVDEVEKSPQTPAVQPIFITVDPERDSKEVVAKYVKEFSPKLLGLTGTVEQIRKVCKAFRVYFSAGPRDEDNDYIVDHTIIMYLVNPDGEFVDYYGQNRDKDQCVASILVNIAKWNSMNKKGWFS
Protein: Growth/differentiation factor 9 (Q9QYW4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Bone morphogenetic protein receptor type-2
- Activin receptor type-1B
- Muellerian-inhibiting factor
- Bone morphogenetic protein 15
- Serine/threonine-protein kinase receptor
- NOBOX oogenesis homeobox
- Lutropin-choriogonadotropic hormone receptor
- Zona pellucida sperm-binding protein 2
- Factor in the germline alpha
- Follicle-stimulating hormone receptor
Sequence:
MAFPSRFLLGVCCFAWLCLLISLSSQASTGESQAGASENLESEADPWSLLLPVDGTDRSGLLPPLFKVLSDRRGETPKLQPDSRALYYMKKLYKTYATKEGVPKPSRSHLYNTVRLFSPCAQQEQAPSNQMTGPLPMVDLLFNLDRVTAMEHLLKSVLLYTLNNSAASSSTVTCVCDLVVKEPMSSSKATPRAPYSFTLRKHRWIEMDVTSLLQPLVASSERSIHLSVNFTCTRDQAPENGTFNMPLSVPPSLILYLNDTSTQAYHSWQSLQSTQRHSQHPGQGSVTTRPVEEEATEVERSPRHRRGQKTLSSETKKPLTASFNLSEYFRQFLFPQNECELHDFRLSFSQLKWDNWIVAPHRYNPRYCKGDCPRAVRHRYGSPVHTMVQNIIYEKLDPSVPRPSCVPGKYSPLSVLTIEPDGSIAYKEYEDMIATRCTCR
Protein: Procathepsin L (EC 3.4.22.15) (Cathepsin L1) [Cleaved into: Cathepsin L heavy chain; Cathepsin L light chain; Cathepsin L] (Q10991)
Organism: Ovis aries (Sheep)
Function: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P06797}. Apical cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane protein {ECO:0000250|UniProtKB:P06797}; Extracellular side {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Secreted, extracellular space {ECO:0000250|UniProtKB:P06797}. Secreted {ECO:0000250|UniProtKB:P06797}. Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages. {ECO:0000250|UniProtKB:P06797}.
Interaction partners:
- Thyroglobulin type-1 domain-containing protein
- Cathepsin S
- Serpin domain-containing protein
- BH3-interacting domain death agonist
- Procathepsin L
- Uncharacterized protein
- Bcl-2-like protein 1
- Transmembrane protease serine 2
- Legumain
- Cathepsin D
Sequence:
VPKSVDWTKKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDSSRPQGNQGCNGGLMDNAFQYIKENGGLDSEESYPYEATDTSCNYKPEYSAAKDTGFVDIPQREKALMKAVATVGPISVAIDAGHSSFQFYKSGIYYDPDCSSKDLDHGVLVVGYGFEGTNNKFWIVKNSWGPEWGNKGYVKMAKDQNNHCGIATAASYPTV
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FUQ8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MKFSTVAPLAFAAAVAHASNPTPMQLAELNAVMEDLKTNLQDYMNLAMDPNSGFSLADMPSGLIQLGMAVGTATDDSYTSMYSDVDFAGVDKMVTMVPWYSSRLKPLIDSLYAAENPAPSTSSASQATPAPAASSSAAPAAGSSTPAPAPVSSAAPSSYAPAPMVNSTMPMANGTTTQTTTHLSTKTSTICDEECHKSMSTATAFKNVTDTQTTTYCPESSLFKNGTSTVTNMHTTTSTVCETCISKPATSSAKPATSAKPASSAKPAVSSAKPAVTSAKSSAGKTTVTTSTIKVSLTSSKAAAPSSVVIQHQTVNGAAKVAAGMGAGVLAAAALLL
Protein: DNA polymerase nu (H0YA88)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XLVEKYCEKSITVKVNSTYGNSSRNIVNQNVRENLKTLYRLTMDLCSKLKDYGLWQLFRTLELPLIPILAVMESHAIQVNKEEMEKTSALLGARLKELEQEAHFVAGERFLITSNNQLREILFGKLKLHLLSQRNSLPRTGLQKYPSTSEALNALRDLHPLPKIILEYRQVHKIKSTFVDGLLACMKKGSISSTWNQTGTVTGRLSAKHPNIQGISKHPIQITTPKNFKGKEDKILTISPRAMFVSSKGHTFLAADFSQIELRILTHLSGDPELLKLFQESERDDVFSTLTSQWKDVPVEQVTHADREQTKKVVYAVVYGAGKERLAACLGVPIQEAAQFLESFLQKYKKIKDFARAAIAQCHQTGCVVSIMGRRRPLPRIHAHDQQLRAQAERQAVNFVVQGSAADLCKLAMIHVFTAVAASHTLTARLVAQIHDELLFEVEDPQIPECAALVRRTMESLEQVPLKVSLSAGRSWGHLVPLQEAWGPPPGPCRTESPSNSLAAPGSPASTQPPPLHFSPSFCL
Protein: RT04067p (Seminal fluid protein 35C, isoform A) (Seminal fluid protein 35C, isoform B) (D1Z365)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKLFFLVILACMLIGIAWGENCNKPCGKCILPTCNYDGKCYFEGTSACALENEKCRRKKNNLDQFVKTVSGFCEMGVKMCK
Protein: ADP ribosylation factor 4 (dARF II) (P40945)
Organism: Drosophila melanogaster (Fruit fly)
Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus.
Interaction partners:
- ADP-ribosylation factor 1
- ADP-ribosylation factor 6
- Coatomer subunit gamma
- non-specific serine/threonine protein kinase
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- AP complex subunit beta
- AP-1 complex subunit gamma
- Adaptor protein complex 1, mu subunit
Sequence:
MGLTISSLLTRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRITEAERELQNMLQEDELRDAVLLVFANKQDLPNAMTAAELTDKLRLNQLRNRHWFIQSTCATQGHGLYEGLDWLSAELAKK
Protein: Tyrosine-protein phosphatase 1 (EC 3.1.3.48) (Protein-tyrosine phosphatase 1) (P28191)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Rap guanine nucleotide exchange factor
Sequence:
MRLGSNSYDVQRTEAIGQTPVKTPPPNQIRCTVTFLDSTSYHFEIEKNSLGIVLLEKVFNYLEIIEKDYFGLVFIAVDNSSAQQKKWLDPSKNLRKQMICPPYHLFFRVKFYVRDPNRLRDEFTRFQFYQQVRQNLEEGRLPCNEGSLALLASYVVQAEVGDFEEKTHGMSRTCLCYKIQFATLPDDFSDRVAELHQLHIGQTPDVAEQNFLDHARRLEMYGMDVYDGVDANHLPIEIGVGAVGIKVFHEGIKMNEYAWVRIRKLSFKKKQFQVLVANEDGVSETIMIFNIMSAKICKLLWKCCIEQHTFFRLKTPPKTPQRKVFNFGSKFRYSGRTEYQTLEENEHRKSAGHRNFHRSLSKSSFLRSTFSGNTQSIDSSRYTNTTTTDSPELPSSGQLLARRLLSAARHDTDSSDALGYASDGAVVCAPLTTPLSPRRTRDYATDSESSAPSLRQQRLSKEAIYYGTQESCDEKSWTPSMACTSTSPGIHASTASVRPVSSGSTPNGASRKSANSGYSGYGYATQTQQPTSTTNASYSPYLNGTISRSSGAAVAKAAARGLPPTNQQAYNTSSPRNSVASYSSFASAGIGGSPPRSKRSPQSNKSSSPVGEDQVVTIKMRPDRHGRFGFNVKGGADQNYPVIVSRVAPGSSADKCQPRLNEGDQVLFIDGRDVSTMSHDHVVQFIRSARSGLNGGELHLTIRPNVYRLGEEVDEPDSTMVPEPARVADSVPNSDKLSKSLQLLADSLNSGKVVDHFEMLYRKKPGMSMNICRLTANLAKNRYRDVCPYDDTRVTLQASPSGDYINANYVNMEIPSSGIVNRYIACQGPLAHTSSDFWVMVWEQHCTTIVMLTTITERGRVKCHQYWPRVFETQEYGRLMIKCIKDKQTTNCCYREFSIRDRNSSEERRVTQMQYIAWPDHGVPDDPKHFIQFVDEVRKARQGSVDPIVVHCSAGIGRTGVLILMETAACLVESNEPVYPLDIVRTMRDQRAMLIQTPGQYTFVCESILRAYHDGTIKPLAEYSKR