wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein kinase Fes/Fps (EC 2.7.10.2) (Feline sarcoma/Fujinami avian sarcoma oncogene homolog) (Proto-oncogene c-Fes) (Proto-oncogene c-Fps) (p93c-fes) (P07332)
Organism: Homo sapiens (Human)
Function: Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28.
Subcellular location: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle. Golgi apparatus. Cell junction, focal adhesion. Note=Distributed throughout the cytosol when the kinase is not activated. Association with microtubules requires activation of the kinase activity. Shuttles between focal adhesions and cell-cell contacts in epithelial cells. Recruited to the lateral cell membrane in polarized epithelial cells by interaction with phosphorylated EZR. Detected at tubular membrane structures in the cytoplasm and at the cell periphery.
Interaction partners:
- Plexin-A1
- Plexin-A3
- Dihydropyrimidinase-related protein 2
- Plexin-A2
- Cdc42-interacting protein 4
- Dihydropyrimidinase-related protein 5
- Plexin-A4
- Heat shock protein HSP 90-alpha
- Amphiphysin
- Ezrin
Sequence:
MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR
Protein: Probable sucrose-phosphatase 2 (AtSPP2) (EC 3.1.3.24) (Q9SJ66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the final step of sucrose synthesis.
Interaction partners:
- Sucrose-phosphate synthase 1
- Sucrose-phosphate synthase 4
- Probable sucrose-phosphate synthase 3
- Probable sucrose-phosphate synthase 2
- alpha-D-xyloside xylohydrolase
- Sucrose synthase 4
- Sucrose synthase 1
- Sucrose synthase 3
- Sucrose synthase 6
- Sucrose synthase 5
Sequence:
MERLTSPPRLMIVSDLDHTMVDHHDPENLSLLRFNSLWEHAYRHDSLLVFSTGRSPTLYKELRKEKPLLTPDITIMSVGTEITYGNSMVPDHGWVEALNNKWDLGIVKQEASNFPELKLQAETEQRPHKVSFYVEKSKAQEVTKELSQRFLKRGLDVKIIYSGGMDLDILPQGAGKGQALAYLLKKLKTEGKLPVNTLACGDSGNDAELFSIPDVYGVMVSNAQEELLKWHAENAKDNPKVIHAKERCAGGIIQAIGHFKLGPNLSPRDVSDFLEIKVENVNPGHEVVKFFLFYERWRRGEVENSEAYTASLKASVHPGGVFVHPSGTEKSLRDTIDELRKYHGDKQGKKFRVWADQVLATDTTPGTWIVKLDKWEQDGDERRCCTTTVKFTSKEGEGLVWEHVQQTWSKETMVKDDSSWII
Protein: Small ribosomal subunit protein uS2 (Q383I8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_03015}.
Interaction partners:
- 40S ribosomal protein S15a, putative
- Ribosomal protein S19, putative
- 40S ribosomal protein S26
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S16, putative
- 40S ribosomal protein S8
- 40S ribosomal protein S18, putative
- 40S ribosomal protein S4
- 40S ribosomal protein S5, putative
- Small ribosomal subunit protein uS4
Sequence:
MTETSRRDLIFLVLSPFSPSLSSKALRNSHTRNMTSVSSGAKVLRMKESDVQKLLAMHCHLGTKNSSSAMKKYIHGRTSDGTNIIDIHMTWEKLILAARVIAAVENPQDVTVCSTRLFGQRAIFKFSQLVGTSFLGGRFIPGTFTNQIQKKFMQPRVLVVTDPRTDHQALREASLVNIPVIAFCDTDAPLEFVDIAIPCNNRGRHSISMMYWLLAREVLRLRGTIPRSVPWEVKVDLFFYRDPEEALKQEEATAAAEVHEEADEGYGWVERDNTWEQ
Protein: SWR1-complex protein 4 (ESA1-associated factor 2) (P53201)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- Vacuolar protein sorting-associated protein 71
- Enhancer of polycomb-like protein 1
- Chromatin modification-related protein EAF1
- Actin-related protein 4
- Chromatin modification-related protein YNG2
- RuvB-like protein 1
- Protein AF-9 homolog
- Chromatin modification-related protein EAF6
- SWR1-complex protein 7
Sequence:
MSSSDIFDVLNIKQKSRSPTNGQVSVPSSSAANRPKPQVTGMQRELFNLLGENQPPVVIKSGNNFKEKMLSTSKPSPWSFVEFKANNSVTLRHWVKGSKELIGDTPKESPYSKFNQHLSIPSFTKEEYEAFMNENEGTQKSVESEKNHNENFTNEKKDESKNSWSFEEIEYLFNLCKKYDLRWFLIFDRYSYNNSRTLEDLKEKFYYTCRNYFKASDPSNPLLSSLNFSAEKEIERKKYLQRLLSRSAAEIAEEEALVVESKKFEMAAKRTLAERESLLRLLDSPHSDQTITQYLTSQGMSQLYNALLADKTRKRKHDLNIPENPWMKQQQQFAQHRQLQQLNVKKSEVKENLSPKKTKRQRQEMQTALKRKSESAYAEQLLKDFNSDERKALGVITHGEKLSPGVYLRSTKLSTFKPALQNKILAILQELSLPSRPVMPSFDVMERQEELLKKINTLIDLKKHVDKYEAGMSITK
Protein: Acyl-coenzyme A synthetase ACSM2A, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2A) (Benzoate--CoA ligase) (EC 6.2.1.25) (Butyrate--CoA ligase 2A) (Butyryl-coenzyme A synthetase 2A) (Middle-chain acyl-CoA synthetase 2A) (Q08AH3)
Organism: Homo sapiens (Human)
Function: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism (By similarity). Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q68CK6}.
Interaction partners:
- Acyl-coenzyme A synthetase ACSM2B, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Hydroxysteroid dehydrogenase-like protein 2
Sequence:
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKAGKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ
Protein: Kar9p (Q5AKW6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Dynein heavy chain, cytoplasmic
- Microtubule-binding protein
- Oxidant-induced cell-cycle arrest protein 5
- Myosin 2
- CAP-Gly domain-containing protein
- Kinesin-like protein
Sequence:
MSTSSFLSNGNRHSMLRNSNPLPPPPPPIKLSHVLSTIPNFSFFDELINLPQPSTSNPSESFNLSQRDVFQITKVLEDINLYLNDLLMIFNNVEQASKNVVDVLDWYFEGKSLLQDLLRNIENIDSIISQLLLVVESSNNHESIGNNLLAIFEEISDLVLDVKKSSIMFKKYLDISINYREIIDSVIKSLSNEIEDCIKCILKLKELKLASPKNVLPNFTLQSIISKMKINDLSSGTFSFKSMRLPTFSDLDEKLYNDYLELESKIDPLRTSLSIVPLRIDDFNTMCAGQFFVKSRENVLDAYEVLVSKWNMLLKEKNSYKKDNINVKWNEIFEYLIEEIFKECGRLIREVGSSSSNVTIPPATGGGGGTTITDEVGNKYKMCSNSITLIQKAFKENIITDPELVTIFNHDLVPKWEELNNIITNNGNQSRTEKRISMYGGTGSVSGSTVESNGLRSFQTGSRSSSSGERPISNGIGIDFNLAVESTSVPLSVHKSDRIKDVISSAGTGAPSEGIPPRSKNLRHSLISVFEDSSMREDEDEATTLVKSPSSKVVKEENQTCGQNKDFNNSFEKSQKLIENNQHQSEQNRIDFAAYIEKVIHSPIKIESKLPKIPLEYIKQGCHITHKRPDFANTRIPRVILMESPYSSPQSNAKRLEKLNAANGVGSFVSPLRNKKNESYSFNRSRASSNATVIGRPNSLLHEMKVPNLTFSKRLTYNLESFHESGGVGGGIGGFSSFESRFDEENLLHSLKETSIWK
Protein: Histone H4 (P02309)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2A.1
- FACT complex subunit SPT16
- Histone H3
- Histone H2B.2
- Histone H2A.2
- Histone acetyltransferase GCN5
- Histone H3-like centromeric protein CSE4
- Histone acetyltransferase type B catalytic subunit
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Histone chaperone ASF1
Sequence:
MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG
Protein: Small t antigen (ST) (ST-AG) (P68835)
Organism: Murine polyomavirus (strain A2) (MPyV)
Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters. Late during the infection cycle, ST may induce dephosphorylation of host MTOR, leading to the inhibition of cap-dependent translation. May establish and maintain high levels of viral genomes during persistent infection in cell culture.
Subcellular location: Host cytoplasm. Host nucleus {ECO:0000250|UniProtKB:P03081}.
Interaction partners:
Sequence:
MDRVLSRADKERLLELLKLPRQLWGDFGRMQQAYKQQSLLLHPDKGGSHALMQELNSLWGTFKTEVYNLRMNLGGTGFQVRRLHADGWNLSTKDTFGDRYYQRFCRMPLTCLVNVKYSSCSCILCLLRKQHRELKDKCDARCLVLGECFCLECYMQWFGTPTRDVLNLYADFIASMPIDWLDLDVHSVYNPRLSP
Protein: EF-hand domain-containing protein (Q385J2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFPPVFNMWRRVRFSLEGPVSLFTRRRRHMMLSSNNVTSKRLLWNPFTPSQTEGGAASASTSGTSGNSDFANQHIAAKVHRDAMLHNERLFDACLELLSLCGASASACPAGGSPRAEMDAESTDAIMAVVHDTLQGTCKTPADQFNIVYKALCLPTVANNRQLQRSLLVVLEAVLPEALFRVFESADLFVVGPDNAKSREALVLFVRALLGVVEVPEGVEREEVVFVYLDDVRTAFPSLRTNAAFVELEKNTTAIALRAKLFDLISQLCAEFDPEGSGRINLRELQQVAERVLGPEQAQLLLEGTCADKNGKIRYMQLASLLLRAPPRRKR
Protein: Unconventional myosin-Ib (MYH-1c) (Myosin I alpha) (MMI-alpha) (MMIa) (O43795)
Organism: Homo sapiens (Human)
Function: Motor protein that may participate in process critical to neuronal development and function such as cell migration, neurite outgrowth and vesicular transport.
Interaction partners:
- Unconventional myosin-Ic
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Calmodulin-1
Sequence:
MAKMEVKTSLLDNMIGVGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATHQHFESRMSKCSRFLNDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRNPRTLFKLEDLRKQRLEDLATLIQKIYRGWKCRTHFLLMKKSQIVIAAWYRRYAQQKRYQQTKSSALVIQSYIRGWKARKILRELKHQKRCKEAVTTIAAYWHGTQARRELRRLKEEARNKHAIAVIWAYWLGSKARRELKRLKEEARRKHAVAVIWAYWLGLKVRREYRKFFRANAGKKIYEFTLQRIVQKYFLEMKNKMPSLSPIDKNWPSRPYLFLDSTHKELKRIFHLWRCKKYRDQFTDQQKLIYEEKLEASELFKDKKALYPSSVGQPFQGAYLEINKNPKYKKLKDAIEEKIIIAEVVNKINRANGKSTSRIFLLTNNNLLLADQKSGQIKSEVPLVDVTKVSMSSQNDGFFAVHLKEGSEAASKGDFLFSSDHLIEMATKLYRTTLSQTKQKLNIEISDEFLVQFRQDKVCVKFIQGNQKNGSVPTCKRKNNRLLEVAVP
Protein: DUF1325 family protein (Q1ZXN8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 9
- Transcriptional regulator
- Probable transcription-associated protein 1
- Myb domain-containing protein
- Transcription initiation factor TFIID subunit 12
- Transcription and mRNA export factor ENY2
- TATA-binding protein-associated-factor
- Transcription initiation factor TFIID subunit 5
- Molybdopterin synthase catalytic subunit
- Ubiquitin carboxyl-terminal hydrolase
Sequence:
MSDAQLLSYFNRIEKILNETKIYTKLMSINKEGLAPNYYDEDELLFPLEIGHEMYNKTLKVYLESKAYIDSIEKTLNKCIDKIGKNDKASHLINQNKINNASSNSSSSSDEEKSDQVGQKRKPKTKGPGSKMNKRPKQPPPQQDEVNSTVPHINSTTTSSTSTNIKDKEKEKEKEREKFDKLEKESSSVNGVHNSKDSKSSTPNKESHSNNNNNANNNIINNNSSLNNSNNNNNTNNNNNNNNSSNNNSNNSNNNSNGNGNSSNGNNNNNSNGNHNSSGNGFHGMQPGQLVAARDSKSNQWILAKVSSFSQKTQKYEVIDEDEEESKRFSVGQKDIIQLPSHTNLPPTFSNNTKVLAMFPDTTAFYPAVVVNVQKVKGKPTFYHLHFEDDQENGETPNRRVNAQHVVALNK
Protein: 4-coumarate:CoA ligase 1 (Ph-4CL1) (Ph4CL1) (EC 6.2.1.12) ((E)-caffeate:CoA ligase 4CL1) (EC 6.2.1.-) (Benzoate:CoA ligase 4CL1) (EC 6.2.1.25) (Trans-cinnamate:CoA ligase 4CL1) (EC 6.2.1.-) (Trans-ferulate:CoA ligase 4CL1) (EC 6.2.1.-) (I3PB37)
Organism: Petunia hybrida (Petunia)
Function: Catalyzes the formation of CoA esters of trans-cinnamic acid, 4-coumaric acid, ferulic acid, benzoic acid and caffeic acid.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22649270}.
Interaction partners:
Sequence:
MPMETETNQGDLIFRSKLPDIYIPKHLPLHSYCFENISEFSSRPCLINGANNHIYTYADVELTSRKVAAGLNKLGIQQKDTIMILLPNSPEFVFAFMGASYLGAISTMANPLFTPAEVVKQAKASNAKLIITQACFVNKVKDYAFDNNLNVICIDSAPEGCIHFSELTQADEHDIPDVKIQSDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENANLYMHSEDVLMCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVQFCELIEKYKVTIGPFVPPIVLAIAKSPVVDNYDLSSVRTVMSGAAPLGKELEDAVRIKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFDIKSGACGTVVRNAEMKIVDPDTGCSLPRNQPGEICIRGDQIMKGYLNDPAATTRTIDKEGWLHTGDIGYIDNDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSDITEDEVKDFVSKQVIFYKRIKRVFFVETVPKSPSGKILRKDLRARLAAGVPN
Protein: Inositol hexakisphosphate kinase 2 (InsP6 kinase 2) (EC 2.7.4.-) (P(i)-uptake stimulator) (PiUS) (Q9R0U1)
Organism: Rattus norvegicus (Rat)
Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UHH9}.
Interaction partners:
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
- Inositol-pentakisphosphate 2-kinase
- Kinase
- Inositol hexakisphosphate kinase 1
Sequence:
MSPAFRTMDVEPRTKGILLEPFVHQVGGHSCVLRFNETTLCKPLVPREHQFYETLPAEMRRFTPQYKGVVSVRFEEDEDRNLCLIAYPLKGDHGPVDIVDNSDCEPKSKLLRWTNKKHHVLETEKSPKDWVRQHRKEEKMKSHKLEEEFEWLKKSEVLYYSVEKKGTVSSQLKHYNPWSMKCHQQQLQRMKENAKHRNQYKFILLENLTCRYEVPCVLDLKMGTRQHGDDASEEKAANQIRKCQQSTSAVIGVRVCGMQVYQAGTGQLMFMNKYHGRKLSVQGFKEALFQFFHNGRYLRRELLGPVLKKLTELKAVLERQESYRFYSSSLLVIYDGKEWPEVTLDSDAEDLEDLSEESADESAGAYAYKPLGASSVDVRMIDFAHTTCRLYGEDSVVHEGQDAGYIFGLQSLIDIVTEISEESGE
Protein: Histamine H1 receptor (H1R) (HH1R) (P70174)
Organism: Mus musculus (Mouse)
Function: In peripheral tissues, the H1 subclass of histamine receptors mediates the contraction of smooth muscles, increase in capillary permeability due to contraction of terminal venules, and catecholamine release from adrenal medulla, as well as mediating neurotransmission in the central nervous system. Involved in circadian rhythm of locomotor activity and exploratory behavior. Also involved in responsiveness to pertussis toxin through its control of susceptibility to histamine hypersensitivity and enhancement of antigen-specific delayed-type hypersensitivity responses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8917588}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35367}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Transient receptor potential cation channel subfamily V member 1
- Histidine decarboxylase
- Guanine nucleotide-binding protein subunit alpha-11
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
- Guanine nucleotide-binding protein subunit alpha-14
- Guanine nucleotide-binding protein subunit alpha-15
Sequence:
MSLPNTSSASEDKMCEGNRTAMASPQLLPLVVVLSSISLVTVGLNLLVLYAVRSERKLHTVGNLYIVSLSVADLIVGAVVMPMNILYLIMTKWSLGRPLCLFWLSMDYVASTASIFSVFILCIDRYRSVQQPLRYLRYRTKTRASATILGAWFLSFLWVIPILGWHHFTPLAPELREDKCETDFYNVTWFKIMTAIINFYLPTLLMLWFYVKIYKAVRRHCQHRQLTNGSLPTFLEIKLRSEDAKEGAKKPGKESPWGVQKRPSRDPTGGLDQKSTSEDPKVTSPTVFSQEGERETVTRPCFRLDVMQTQPVPEGDARGSKANDQTLSQPKMDEQSLSTCRRISETSEDQTLVDRQSFSRTTDSDTSIEPGLGKVKARSRSNSGLDYIKVTWKRLRSHSRQYVSGLHLNRERKAAKQLGCIMAAFILCWIPYFIFFMVIAFCNSCCSEPVHMFTIWLGYINSTLNPLIYPLCNENFKKTFKKILHIRS
Protein: Small COPII coat GTPase SAR1 (EC 3.6.5.2) (Q23445)
Organism: Caenorhabditis elegans
Function: Involved in transport from the endoplasmic reticulum to the Golgi apparatus (By similarity). Also plays a role in transporting the tyrosine kinase receptor let-23 from the endoplasmic reticulum to the plasma membrane of vulval precursor cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NR31}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NR31}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9NR31}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NR31}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NR31}. Note=Active at endoplasmic reticulum exit sites (ERES) where it inserts into the membrane and recruits the remainder of the coat protein complex II/COPII. {ECO:0000250|UniProtKB:Q9NR31}.
Interaction partners:
- WD_REPEATS_REGION domain-containing protein
- Protein transport protein SEC23
- WD_REPEATS_REGION domain-containing protein
- Yeast SEC homolog
- Protein SEC13 homolog
- RAB family
- Protein transport protein Sec24C
- Protein transport protein sec-16A.1
- ANK_REP_REGION domain-containing protein
- Large ribosomal subunit protein uL24
Sequence:
MSFLWDWFNGVLNMLGLANKKGKLVFLGLDNAGKTTLLHMLKDDRIAQHVPTLHPTSEQMSLGGISFTTYDLGGHAQARRVWKDYFPAVDAVVFLIDVADAERMQESRVELESLLQDEQIASVPVLILGNKIDKPGALSEDQLKWQLNIQHMCTGKGDVSRNEMASRPMEVFMCSVLQRQGYGEGIRWLGQYL
Protein: Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase [Includes: Apolipoprotein N-acyltransferase (ALP N-acyltransferase) (EC 2.3.1.269); Polyprenol monophosphomannose synthase (PPM synthase) (Polyprenol-P-Man synthase) (Ppm1) (EC 2.4.1.-) (Dolichol-phosphate mannose synthase) (EC 2.4.1.83)] (O53493)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12427759}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Conserved protein
- Probable transmembrane protein FxsA
- GDP-mannose-dependent alpha-mannosyltransferase
- Serine protease PepD
- Lipoprotein signal peptidase
- GDP-mannose-dependent alpha-
- Probable UDP-glucose 4-epimerase GalE3
Sequence:
MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLTHRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRLLPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALVGCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPTVTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDIDPFVNPDAGQRISAAAEAIGAPILIGTLMDVPGRPRENPEWTNTAIVWNPGTGPADRHDKAIVQPFGEYLPMPWLFRHLSGYADRAGHFVPGNGTGVVRIAGVPVGVATCWEVIFDRAPRKSILGGAQLLTVPSNNATFNKTMSEQQLAFAKVRAVEHDRYVVVAGTTGISAVIAPDGGELIRTDFFQPAYLDSQVRLKTRLTPATRWGPILQWILVGAAAAVVLVAMRQNGWFPRPRRSEPKGENDDSDAPPGRSEASGPPALSESDDELIQPEQGGRHSSGFGRHRATSRSYMTTGQPAPPAPGNRPSQRVLVIIPTFNERENLPVIHRRLTQACPAVHVLVVDDSSPDGTGQLADELAQADPGRTHVMHRTAKNGLGAAYLAGFAWGLSREYSVLVEMDADGSHAPEQLQRLLDAVDAGADLAIGSRYVAGGTVRNWPWRRLVLSKTANTYSRLALGIGIHDITAGYRAYRREALEAIDLDGVDSKGYCFQIDLTWRTVSNGFVVTEVPITFTERELGVSKMSGSNIREALVKVARWGIEGRLSRSDHARARPDIARPGAGGSRVSRADVTE
Protein: Ras-related protein Rab (Q63483)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046278}; Lipid-anchor {ECO:0000256|ARBA:ARBA00046278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00046278}. Membrane {ECO:0000256|RuleBase:RU367128}; Lipid-anchor {ECO:0000256|RuleBase:RU367128}.
Interaction partners:
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Ankyrin repeat domain-containing protein 27
- Geranylgeranyl transferase type-2 subunit alpha
- Rab proteins geranylgeranyltransferase component A 1
- HPS4, biogenesis of lysosomal organelles complex 3 subunit 2
Sequence:
MQTPHKEHLYKLLVIGDLGVGKTSIIKRYVHQNFSSHYRATIGVDFALKVLHWDPETVVRLQLWDIAGQERFGNMTRVYYREAMGAFIVFDVTRPATFEAVAKWKNDLDSKLTLPNGKPVSVVLLANKCDQGKDVLVNNGLKMDQFCKEHGFVGWFETSAKENINIDEASRCLVKHILANECDFIESIEPDIVKPHLTSPKVVSCSGCAKS
Protein: Ceramide transfer protein (CERT) (Collagen type IV alpha-3-binding protein) (Goodpasture antigen-binding protein) (GPBP) (START domain-containing protein 11) (StARD11) (StAR-related lipid transfer protein 11) (Q9EQG9)
Organism: Mus musculus (Mouse)
Function: Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5P4}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y5P4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y5P4}. Note=Preferentially localized to the Golgi apparatus. {ECO:0000250|UniProtKB:Q9Y5P4}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein A
- Steroidogenic acute regulatory protein, mitochondrial
- StAR-related lipid transfer protein 3
- StAR-related lipid transfer protein 7, mitochondrial
- START domain-containing protein 10
- Ceramide kinase
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase 3
Sequence:
MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNTLSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPEHRQQWVDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDVCADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHNTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREESWQKRHDREVEKRRRVEEAYKNVMEELKKKPRFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDTFSSVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMNYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIVYQTHKRVWPASQRDVLYLSAIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINIAMICQTLVSPPEGDQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF
Protein: GEO11741p1 (RT02906p) (Seminal fluid protein 79) (B4ZJA5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- TIL domain-containing protein
- Seminal fluid protein 84E
- GEO11768p1
Sequence:
MKLLSAALVLLMSSALAMAQKNTNTNENNIVIGKV
Protein: Exocrine gland-secreted peptide 1 (Q3LHH8)
Organism: Mus musculus (Mouse)
Function: Male-specific phermone which is recognized by the Vmn2r116/V2rp5 receptor in the vomeronasal organ (VNO) and enhances female sexual receptive behavior (lordosis) upon male mounting, resulting in successful copulation.
Subcellular location: Secreted {ECO:0000269|PubMed:16208374, ECO:0000269|PubMed:20596023}. Note=Secreted by the extraorbital lacrimal gland into tears. {ECO:0000269|PubMed:16208374, ECO:0000269|PubMed:20596023}.
Interaction partners:
Sequence:
MTSLPVLLFLIILLLPSMITEGRVLTQTGKEATIFADQKTNHEADLKNPDPQEVQRALARILCALGELDKLVKDQANAGQQEFKLPKDFTGRSKCRSLGRIK