wanglab/gogpt-training-data huggingface dataset:
Protein: LIM domain-containing protein 1 (Q9QXD8)
Organism: Mus musculus (Mouse)
Function: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18657804}. Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus but is localized predominantly to the cytoplasm. Found in the nucleus but not nucleoli. Colocalizes with VCL in the focal adhesions (By similarity). {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase LATS1
- Protein salvador homolog 1
- Serine/threonine-protein kinase LATS2
- LIM domain-containing protein ajuba
- Wilms tumor protein 1-interacting protein
- Egl nine homolog 1
- Eukaryotic translation initiation factor 4E
- Trinucleotide repeat-containing gene 6A protein
- Probable ATP-dependent RNA helicase DDX6
- Protein argonaute-1
Sequence:
MDKYDDLGLEASKFIEDLNMYEASKDGLFRVDKGAGNNPEFEETRRVFATKMAKIHLQQQQQQQLLQEEALPRAGRSPVNGGNRQGASGKLAADGAAKPPLAVPTVAPGLATTTAAAQPSYPSQEQRIRPSAHGARPGSQNCGSREGPVSSQRPALHGLSPSCEDPSCLTHGDYYDNFSLASPQWGDKPEGCPSVSLGVGSGWPGCPGNDSTLPKSCGDHHPYQPQLSTVCSGRSFESGISGQDGGIGGHSSEKPTGLWSTASSQRVNLGFSSMGLENGTSAQPKGTTVSAPMVPSSASQGACPKRDSGLGYEASGRVFKPLVDTQPWLQDGPKSYLSVSAPLSSTAGKDSTQPGMTTGLDPKFGCVESGTSPKPSPTSNVHPVMSTPSELSCKESSPSWSTDSSLEPVLPGSPTPSRVRLPCQTLAPGPELGPSTAELKLEALTQRLEREMDAHPKADYFGSCVKCSKGVFGAGQACQAMGDLYHDACFTCAACSRKLRGKAFYFVNGKVFCEEDFLYSGFQQSADRCFLCGHLIMDMILQALGKSYHPGCFRCVICNECLDGVPFTVDSENKIYCVRDYHKVLAPKCAACGLPILPPEGSDETIRVVSMDRDYHVECYHCEDCGLELNDEDGHRCYPLEDHLFCHSCHVKRLEKGPSPAPLHQHHF
Protein: Keratin, type I cytoskeletal 27 (Cytokeratin-27) (CK-27) (Keratin-25C) (K25C) (Keratin-27) (K27) (Type I inner root sheath-specific keratin-K25irs3) (Q7Z3Y8)
Organism: Homo sapiens (Human)
Function: Essential for the proper assembly of type I and type II keratin protein complexes and formation of keratin intermediate filaments in the inner root sheath (irs).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Z320}.
Interaction partners:
- Keratin, type I cytoskeletal 25
- Keratin, type II cytoskeletal 71
- Keratin, type II cytoskeletal 74
- Keratin, type I cuticular Ha5
- Keratin-associated protein 9-4
- Keratin-associated protein 3-2
- Keratin-associated protein 17-1
- Keratin-associated protein 9-3
- Keratin-associated protein 3-1
- Keratin-associated protein 9-8
Sequence:
MSVRFSSTSRRLGSCGGTGSVRLSSGGAGFGAGNTCGVPGIGSGFSCAFGGSSSAGGYGGGLGGGSASCAAFTGNEHGLLSGNEKVTMQNLNDRLASYLENVRALEEANADLEQKIKGWYEKFGPGSCRGLDHDYSRYFPIIDELKNQIISATTSNAHVVLQNDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISDDAGATTSARNELIEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIETYCLLIDGEDGSCSKSKGYGGPGNQTKDSSKTTIVKTVVEEIDPRGKVLSSRVHTVEEKSTKVNNKNEQRVSS
Protein: Inner membrane transport protein YbaT (P77400)
Organism: Escherichia coli (strain K12)
Function: Probable amino-acid or metabolite transport protein.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Glutaminase 1
- Glutamate/gamma-aminobutyrate antiporter
- Protein HdeD
- Outer membrane protein Slp
- Glutamate decarboxylase alpha
Sequence:
MMNTEGNNGNKPLGLWNVVSIGIGAMVGAGIFALLGQAALLMEASTWVAFAFGGIVAMFSGYAYARLGASYPSNGGIIDFFRRGLGNGVFSLALSLLYLLTLAVSIAMVARAFGAYAVQFLHEGSQEEHLILLYALGIIAVMTLFNSLSNHAVGRLEVILVGIKMMILLLLIIAGVWSLQPAHISVSAPPSSGAFFSCIGITFLAYAGFGMMANAADKVKDPQVIMPRAFLVAIGVTTLLYISLALVLLSDVSALELEKYADTAVAQAASPLLGHVGYVIVVIGALLATASAINANLFAVFNIMDNMGSERELPKLMNKSLWRQSTWGNIIVVVLIMLMTAALNLGSLASVASATFLICYLAVFVVAIRLRHDIHASLPILIVGTLVMLLVIVGFIYSLWSQGSRALIWIIGSLLLSLIVAMVMKRNKTV
Protein: Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase) (O53823)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741}.
Interaction partners:
Sequence:
MTDLAKGPGKDPGSRGITYASAGVDIEAGDRAIDLFKPLASKATRPEVRGGLGGFAGLFTLRGDYREPVLAASSDGVGTKLAIAQAMDKHDTVGLDLVAMVVDDLVVCGAEPLFLLDYIAVGRIVPERLSAIVAGIADGCMRAGCALLGGETAEHPGLIEPDHYDISATGVGVVEADNVLGPDRVKPGDVIIAMGSSGLHSNGYSLVRKVLLEIDRMNLAGHVEEFGRTLGEELLEPTRIYAKDCLALAAETRVRTFCHVTGGGLAGNLQRVIPHGLIAEVDRGTWTPAPVFTMIAQRGRVRRTEMEKTFNMGVGMIAVVAPEDTTRALAVLTARHLDCWVLGTVCKGGKQGPRAKLVGQHPRF
Protein: ferroxidase (EC 1.16.3.1) (A5PL27)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKILILGIFLFLCSTPAWAKEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGPDRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFHSHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYHSHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVVMFSVVDENFSWYLEDNIKTYCSEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFHGQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQECNKSSSKDNIRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSYKKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGVRFNKNNEGTYYSPNYNPQSRSVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYYSAVDPTKDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLEDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYFSGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRRQSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYKKVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQTESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFPGTYQTLEMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQNEDTKSG
Protein: L-amino acid-D/L-Glu epimerase (EC 5.1.1.-) (L-Xxx-D/L-Glu epimerase) (B0TZW0)
Organism: Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / CCUG 19701 / FSC 153 / O#319-036)
Function: Catalyzes the epimerization of dipeptides with L-Glu in the second position. Has epimerase activity with L-Ala-L-Glu, L-Pro-L-Glu, L-Val-L-Glu, L-Thr-L-Glu and L-Met-L-Glu (in vitro).
Interaction partners:
Sequence:
MSKIIDIKTSIIKIPLKRTFITAVRSTNHIDSLAVELTLDNGVKGYGVAPATTAITGDTLQGMQYIIREIFAPVILGSDLSDYKQTLELAFKKVMFNSAAKMAIDLAYHDLLAKEQDISVAKLLGAKANSIVTDVSISCGNVAETIQNIQNGVEANFTAIKVKTGADFNRDIQLLKALDNEFSKNIKFRFDANQGWNLAQTKQFIEEINKYSLNVEIIEQPVKYYDIKAMAEITKFSNIPVVADESVFDAKDAERVIDEQACNMINIKLAKTGGILEAQKIKKLADSAGISCMVGCMMESPAGILATASFALAEDITVADLDPLDWVAKDLYSDYITFNEPNIILKDNLKGFGFNL
Protein: Facilitated urea transporter (Solute carrier family 14 member 2) (Urea transporter 2) (Zgc:136632) (Q533H0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ammonium transporter Rh type B
- Rhesus blood group-associated glycoprotein
- Urea transporter
- Ammonium transporter Rh type C-like 2
Sequence:
MPGTHLTKKSDPLNVTHLCKTSTSTQYSSAQNTKELQPLMANPVHKITDEKKQQGLEKINSGQRFKANLIKWVSFISGDMAAFGEWMKGQFILLQIMDWVLRGAAQVMFVNNPLSGLIIFAGLILQNRWWALNGFVGTVFATISALILCQNRGAIAAGLYGYNGILVGLLMAVFSNAGDWYWWLLLPNIFMSMACPIVSSALASINSRWDLPVFTLPFNILVCLHMVATGHYNQYFPQILIQPTTSMSNLTWSELDYAQLFRSIPVGIGQVYGCDNAWTGGIFMIALFISSPITFAHATIGSAVGMVSGLALAAPFKNIYMGLWGYNCVLACIAIGGMFYALTWQTHLLAVACAFFCAYLGSAIGNVMSNFGLPACTWPFCLSALTFLLITTETKFIHKLPLAKVAYPEQNLRYYWKMKKEEKTQKGIQAKDTESQLEKEQISISMEKKDLDICTVDVQQEENTL
Protein: Sesquiterpene synthase 14a (ShTPS14a) ((E)-beta-farnesene synthase TPS14a) (EC 4.2.3.47) ((E)-gamma-bisabolene synthase TPS14a) (EC 4.2.3.59) ((Z)-alpha-bisabolene synthase TPS14a) (EC 4.2.3.-) ((Z)-beta-farnesene synthase TPS14a) (EC 4.2.3.-) (Beta-acoradiene synthase TPS14a) (EC 4.2.3.-) (Beta-bisabolene synthase TPS14a) (EC 4.2.3.-) (Beta-myrcene synthase TPS14a) (EC 4.2.3.15) (Limonene synthase TPS14a) (EC 4.2.3.-) (G8H5M9)
Organism: Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum)
Function: Sesquiterpene synthase involved in the biosynthesis of volatile compounds. Mediates the conversion of (2E,6E)-farnesyl diphosphate ((EE)-FPP) into beta-bisabolene, beta-farnesene, (E)-gamma-bisabolene, beta-acoradiene, selinene and (Z)-alpha-bisabolene. Low or no activity with (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP). Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus producing beta-myrcene and limonene.
Interaction partners:
Sequence:
MNQLAMVNTTITRPLANYHSSVWGNYFLSYTPQLTETSSQEKRELEELKEKVRQMLVETPDNSTQKLVLIDTIQRLGVAYHFENHIKISIQNIFDEFEKNKNKDNDDDLCVVALRFRLVRGQRHYMSSDVFTRFTNDDGKFKETLTKDVSGLLNLYEATHLRVHGEEILEDALSFTVTHLKSMSPKLDNSLKAQVSEALFQPIHTNIPRVVARKYIRIYENIESHDDLLLKFAKLDFHILQKMHQRELSELTRWWKYLDYENKYPYARDKLVECYFWATGVYFGPQYKRARKTLTKLIVIITITDDLYDAYATYDELVPYTDAVERCEISAMHSISPYMRPLYQVFLDYFDEMEKELTKDGKAHYVYYAKIETNKWIKSYLKEAEWLKNDIIPKCEEYKRNATITVSSQMILITCLIVAGEFISKETFEWMINESLIAPASSLINRLKDDIIGHEHEQQREHGASFIECYVKEYRASKQEAYVEARRQIANAWKDINTDYLHATQVPTFVLEPALNLSRLVDILQEDDFTDSQNFLKDTITLLFVDSVNSTSCG
Protein: Probable xylan O-acetyltransferase 8 (EC 2.3.1.-) (Protein trichome birefringence-like 8) (OsTBL8) (Q10MX4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues in xylan. Possesses extremely low activity in vitro.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q2QYU2}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVQLPAMKRVKGRAPLSVVVAIIGGLALAGIIFTEDLRGLTEVKEKVTDKEKKRTSLRTVMRTSALLSADQPPPPAVLSVEPATATPPPAPKMAFNATRCSVTDGYWAYDRSKKLPYTDQTCPYVDRQDSCQRNGRPDSDYLYWDWHLDDCLLPRFDPVSMLEKLRGKRIMFVGDSLQLGQWLSFVCLVNSAVPDTPGAKSMERSRTLSVYTVKEYNASIEFYWAPFLVESNSDRNIALGAGGRVLHVDAIEEHGKHWRRADILVFDSYVWWMTGYRIKSVWGSFGDDGYEELDAWVAYRLGLKTWANWVDSNVDPATTRVFFMSISTTHMRSEDWGREGGIRCYNETWPITQRGYRGSGSDRRMMEVMSDVLGRMRTPVTLLNITQLTEHRVDAHVSVYTETGGLLVTDEEKTDPQRYTDCIHWCIPGVPDTWNRLLYAHL
Protein: Bem46-like serine peptidase (Q38DS6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSAERVAVTLLMWVLVALLVSTIFLAAVGYRMRESQNHFLYFPNVPAGSTFVCDSPLERGYRNSEQVHIRTADGLTLRGFIMWPPMELQERPRQQHDMEERMGYMLRVPPLSAASDRSNPNPPFLERLEGSGTGSAHPQCSILYFHGNAGNVGHRIPIAAMLSTKCRCAVLMVDYRGYGQSDSVSPTQEGVMLDAQACLDYLLCHPHIPADRIFVMGTSLGGAVAIHLAAEPHNAKHIAGVIVENTFTSIGDMASEMVRHALNGAQPCFSFLLLSLFEYYVKPLCLHIKWRSIDAVQKICAPMLFLSGLKDNVVPPLQMKKLYSKTFSTRSRRFVEYPEGDHNTLPLIPGYGETVNAFIQDVLRHREQLI
Protein: Elongin-B (EloB) (Elongin 18 kDa subunit) (RNA polymerase II transcription factor SIII subunit B) (SIII p18) (Transcription elongation factor B polypeptide 2) (P62869)
Organism: Mus musculus (Mouse)
Function: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells.
Subcellular location: Nucleus {ECO:0000305|PubMed:33590678}.
Interaction partners:
- Cullin-2
- Cullin-5
- von Hippel-Lindau disease tumor suppressor
- Elongin-C
- E3 ubiquitin-protein ligase RBX1
- RING-box protein 2
- Core-binding factor subunit beta
- Suppressor of cytokine signaling 1
- Hypoxia-inducible factor 1-alpha
- Cytokine-inducible SH2-containing protein
Sequence:
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPEEQRLYKDDQLLDDGKTLGECGFTSQTARPQAPATVGLAFRADDTFEALRIEPFSSPPELPDVMKPQDSGGSANEQAVQ
Protein: Type VI collagen alpha-2 chain (Q1T7A6)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
IGDMFHEKHESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPDLPCQTELYVAQCTQRPVDIVFLLDGSERLGEQNFHKAQRFVEDVSRRLTLARRDDDPLNARVALLQFGGPREQQVAFPLTFNLTVIQEALASSRYLNSFSHVGTGIVHAINQVVLGAPAGARRHAELAFVFLTDGITGNESLEEAVHSMRKQNVVPTVVAVGSDVDADVLSKISLGDEAAVFREKDYDS
Protein: V-type proton ATPase subunit H (V-ATPase subunit H) (Vacuolar proton pump subunit H) (Vacuolar proton pump subunit SFD) (Q9V3J1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit H is essential for V-ATPase activity, but not for the assembly of the complex (By similarity).
Interaction partners:
- V-type proton ATPase subunit G
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- V-type proton ATPase subunit B
- V-type proton ATPase subunit d 1
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase subunit F 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit S1
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MTTALYLPEENIDMIAATSVLQQQAADIRTRTINWASYMQSQMISEEDYKAISALDKSRASFLAQNSSQVVKTLLNLVSHLSKDSTIQYILVLLDDLLQEDRSRVDLFHDTAGKLKQCIWGPFLNLLNRQDGFIVNMSSRILAKFACWGHETMPKSDLNFYLQFLKDQLASNNNEYIQSVARCLQMMLRVDEYRFAFVGVDGISTLIRILSTRVNFQVQYQLIFCLWVLTFNPLLAAKMNKFSVIPILADILSDCAKEKVTRIILAVFRNLIEKPEDSSVAKDHCIAMVQCKVLKQLSILEQRRFDDEDITADVEYLSEKLQNSVQDLSSFDEYATEVRSGRLEWSPVHKSAKFWRENAQRLNEKNYELLRILVHLLETSKDAIILSVACFDIGEYVRHYPRGKHVLEQLGGKQIVMQHLGHEDPNVRYEALLAVQKLMVHNWEYLGKQLEKENENQKQGAAPIAGKA
Protein: Uncharacterized protein (Q385H2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRCFYFKTLSFSLFFYCDRILLAQFFSQAILKFVMFSKSVALVFAIAFVMEVVRAAAPDPAPGGATEKEFPLVWVCLGITVVGIGIALYVAHRRPDELHIPGASDEETEEMTRADGPENNENPGANETAADDGAKKEQATV
Protein: 7-deoxyloganetin glucosyltransferase (EC 2.4.1.324) (Genipin glucosyltransferase) (UDP-glucose glucosyltransferase 2) (GjUGT2) (UDP-glycosyltransferase 85A24) (F8WKW1)
Organism: Gardenia jasminoides (Cape jasmine) (Gardenia augusta)
Function: Iridoid glucosyltransferase acting on genipin and 7-deoxyloganetin. No activity with 7-deoxyloganetic acid. Involved in geniposide biosynthesis.
Interaction partners:
Sequence:
MGSISLPEKHHAVCIPYPAQGHINPMLKLAKILHHKGFHITFVNTEFNHKRLLKSRGPDALNGLPDFQFKTIPDGLPPSDVDATQDIPSLCESTTTRCLDPFRNLLAELNGPSSSQVPPVSCIVSDGVMSFTLEAAAELGVPEILFWTTSACGFLGYMHYAKLIEKGLTPLKDASYLSNGYLEQSLDWIPGMKDIRLKDLPSFLRTTNPDDYMVKFVLQETERAKKASAIILNTFQELEDDVINALSAILPPIYTIGPLQFLQKEVKDERLSVLGSNLWKEEPECLDWLDSKDPNSVVYVNFGSITVMTPGQLVEFAWGLANSKQTFLWIIRPDLVSGDSAILPPEFLEETKDRGLLASWCPQEQVLSHPAIGGFLTHSGWNSTLESICSGVPMICWPFFAEQQTNCWFCCTKWYNGLEIDNNVKRDEVESLVTELMVGEKGMDMKKKALEWKNKAEEAAKSSGGSSYSNLEKVVQVLLSK
Protein: VIP peptides [Cleaved into: Intestinal peptide PHV-42 (Peptide histidine valine 42) (PHV-42); Intestinal peptide PHM-27 (Peptide histidine methioninamide 27) (PHM-27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] (P01282)
Organism: Homo sapiens (Human)
Function: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.
Subcellular location: Secreted.
Interaction partners:
- Vasoactive intestinal polypeptide receptor 2
- Vasoactive intestinal polypeptide receptor 1
- Vasopressin V1a receptor
- Secretin
- Glucagon-like peptide 1 receptor
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Pro-neuropeptide Y
- Protachykinin-1
- Gastric inhibitory polypeptide receptor
- Secretin receptor
Sequence:
MDTRNKAQLLVLLTLLSVLFSQTSAWPLYRAPSALRLGDRIPFEGANEPDQVSLKEDIDMLQNALAENDTPYYDVSRNARHADGVFTSDFSKLLGQLSAKKYLESLMGKRVSSNISEDPVPVKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGESPDFPEELEK
Protein: Transmembrane 6 superfamily member 2 (Q9BZW4)
Organism: Homo sapiens (Human)
Function: Regulator of liver fat metabolism influencing triglyceride secretion and hepatic lipid droplet content. May function as sterol isomerase.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25566323}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:25566323}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hyaluronan and proteoglycan link protein 4
- 1-acylglycerol-3-phosphate O-acyltransferase PNPLA3
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase MBOAT7
- 17-beta-hydroxysteroid dehydrogenase 13
- Neurocan core protein
- Voltage-gated chloride channel TMC4
- Lysophospholipase-like protein 1
- Glucokinase regulatory protein
Sequence:
MDIPPLAGKIAALSLSALPVSYALNHVSALSHPLWVALMSALILGLLFVAVYSLSHGEVSYDPLYAVFAVFAFTSVVDLIIALQEDSYVVGFMEFYTKEGEPYLRTAHGVFICYWDGTVHYLLYLAMAGAICRRKRYRNFGLYWLGSFAMSILVFLTGNILGKYSSEIRPAFFLTIPYLLVPCWAGMKVFSQPRALTRCTANMVQEEQRKGLLQRPADLALVIYLILAGFFTLFRGLVVLDCPTDACFVYIYQYEPYLRDPVAYPKVQMLMYMFYVLPFCGLAAYALTFPGCSWLPDWALVFAGGIGQAQFSHMGASMHLRTPFTYRVPEDTWGCFFVCNLLYALGPHLLAYRCLQWPAFFHQPPPSDPLALHKKQH
Protein: V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (Vacuolar proton pump subunit A) [Cleaved into: Endonuclease PI-SceI (EC 3.1.-.-) (Sce VMA intein) (VMA1-derived endonuclease) (VDE)] (P17255)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:2139027}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit d
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit G
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit D
- V-type proton ATPase subunit E
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
Sequence:
MAGAIENARKEIKRISLEDHAESEYGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETIYDGIQRPLKAIKEESQSIYIPRGIDTPALDRTIKWQFTPGKFQVGDHISGGDIYGSVFENSLISSHKILLPPRSRGTITWIAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHKSDSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVVSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVHNCGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADSTGDVKHAVSSSKFFEPSRGEKEVHGEFEKLLSTMQERFAESTD
Protein: Synapsin-1 (Synapsin I) (B0UXI4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000256|ARBA:ARBA00004234}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Presynapse {ECO:0000256|ARBA:ARBA00034106}.
Interaction partners:
- Synaptotagmin
- Synaptosomal-associated protein 25-A
- Disks large homolog 4
- Ras-related protein Rab-3
- Vesicle-associated membrane protein 2
- Syntaxin 1A
- Synaptotagmin XII
- Gephyrin
- Gephyrin
- Actin alpha 1, skeletal muscle b.
Sequence:
MNYLRRRLSDSNFMSNLPNGYMGDLQRPDPPQQSPAPVLSPGSQERRQPAPSQSTGAGFFSSISNAVKQTTAAAAATFNEATERGIGSGNAKILLVIDDQQTDWAKVFKGKKVHGDCDIKVEQADFSEVNLVAHATGSYSVDIEAIRSGNKITKCIKPDFVLVRQHAFSMAKNGDHRNIVIGLQYAGLPSVNSLHSVYNFCDKPWVFSQLSRLYKQLGPEEFPLIDQVYYPNHKEMITTPGFPVVVKMGHAHSGMGKVKVDNQYDFQDIASVVALTKTYATSEPFIDAKYDIRIQKIGENYKAYMRTSISGNWKTNTGSAMLEQVAMSDRYRMWVDVCSEVFGGLDICAVEALHGKDGRDYIIEVVGCSMPLIGDQQDEDRALMADLVVAKMNETVPRTSAPTTVRSQGPAVSPQPISQSRVPQAQQRPPPQGGPQQAAASTAATRQGAPPQQRPSPQGQPPAQSQSVTSPIAQNPPAQQPRPNQPPQRQASQGSAAPQRPPAAQIPAQRGSPQSQRQGGPQQGGPQTGGQSPKPAGQPQQRPQQPRQGQPTRQPTQGGPQQTQDAPQPAPQGSPRPPTTQQPRPTAPGQGGPGGTRPPLQQKPQPPQKPSPDHPALSGSPQLNKSQSLTNTFNIPETPAAQHQSPSQDEAKAETIRNLRKSFASLFSVE
Protein: AMP deaminase 1 (EC 3.5.4.6) (AMP deaminase isoform M) (Myoadenylate deaminase) (P10759)
Organism: Rattus norvegicus (Rat)
Function: AMP deaminase plays a critical role in energy metabolism.
Interaction partners:
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Adenylosuccinate lyase
- Inosine-5'-monophosphate dehydrogenase 2
- 5'-nucleotidase, cytosolic IA
- Bifunctional purine biosynthesis protein ATIC
- Adenylosuccinate synthetase isozyme 1
- Inosine-5'-monophosphate dehydrogenase 1
- 5'-nucleotidase
- Adenylosuccinate synthetase isozyme 2
Sequence:
MPLFKLTGQGKQIDDAMRSFAEKVFASEVKDEGGRHEISPFDVDEICPISLREMQAHIFHMENLSMSMDGRRKRRFQGRKTVNLSIPQSETSSTKLSHIEEFISSSPTYESVPDFQRVQITGDYASGVTVEDFEVVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEALVAIESFYPVFTPPPKKGEDPFRREDLPANLGYHLKMKGGVIYIYPDEAAASRDEPKPYPYPNLDDFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKNLTLKELFAQLNMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVDAKYQHAEPRLSIYGRSPDEWSKLSSWFVGNRIYCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQTHPDLSVFLKHITGFDSVDDESKHSGHMFSSKSPKPEEWTMENNPSYTYYAYYMYANIMVLNCLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKSTE
Protein: Cilia- and flagella-associated protein 300 (Flagellar and basal body protein) (A8IYS6)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Plays a role in outer and inner dynein arm assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29727692}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:29727692}. Note=Localizes predominantly in the cytoplasm and weakly in flagella. Transported to the flagellar matrix in an intraflagellar transport (IFT)-dependent manner. {ECO:0000269|PubMed:29727692}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- RuvB-like helicase
- Arrestin C-terminal-like domain-containing protein
Sequence:
MTAFVPVSLPSTSALNDAYVKSQLTKWDLLRNLRCVAVRYTKYYHKLQGQELLADLFRDEKVQEAFQVLRKGGAWGQLGGPVTKVDATLLASSLTRMDLFDKLTETSPPIVRSNGDIGKCMEDNREGFQVSDQLRELILVEESEHAALFSEAERDELLWRLFEHVVLGGACCQFEDKVEPYVETSKRLYKELVCAQKDPATGKVQTVSAVYKINSIQGDSGPLELYPSRSRQNFCYAAVDPVRRIVKILYHAYVPYW