wanglab/gogpt-training-data huggingface dataset:
Protein: Histone acetyltransferase (Q84JY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- P300/CBP acetyltransferase-related protein-like protein
- Protein TIFY 4B
- Protein OBERON 4
- Protein TIFY 8
- Protein TIFY 4A
- ATP-dependent DNA helicase Q-like 3
- Protein OBERON 3
- Histone acetyltransferase HAC12
- Protein OBERON 1
- Protein OBERON 2
Sequence:
MPRPGPRPYDCIRRAWHSDRHQPMRGLLIQEIFRIVCEIHSQSTRKNTEWQEKLPVVVLRAEEIMYSKANSEAEYMDMKTLLDRTNDAINTIIRLDETTETGEFLQPCIEAALHLGCTPRRASRSQRNINPRCYLSQDSTNLDNMLSQVFMKPNNFAPKNLAVAQENCPVSKYSAYPLCYSFRPISDSCKSKNSRPASLIDATNGITFGGCECDLSLRLGPLGPPTQKRSKISSNNNN
Protein: Ribonuclease P/MRP protein subunit POP5 (EC 3.1.26.5) (Q9UU90)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ribonuclease MRP protein subunit rmp1
- Probable ribonuclease P protein subunit 1
- Ribonucleases P/MRP protein subunit pop1
- Probable ribonuclease P protein subunit 3
- Ribonuclease P protein subunit rpr2
- Ribonucleases P/MRP protein subunit pop3
- Ribonucleases P/MRP protein subunit POP7
- Uncharacterized protein C6C3.09
- Probable ribonucleases P protein subunit pop8
- Uncharacterized protein C16C4.19
Sequence:
MVRFKSRYLLFEVLYPEAKEFFDYPTIPSDSSITTSSLSKIIRTMVAENFGDVGIGKVASSLTVKYFSPNTSTGILRVSRQHFRLAWAALVLIRELYGKPVIIRVVRVSGTIKKAELAAIERNKSEIHNISLMDEPIEV
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FKL8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Heat shock protein homolog SSE1
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Transcription factor
- Candida glabrata strain CBS138 chromosome D complete sequence
Sequence:
MSSPVIGISFGNTSSSIAYINPKNDVDVIANPDGERAIPSVLSYVGEDEYHGGQALQQLVRNPKNTIINFRDFIGLPFSQCDASRCAAGAPVVEIDGKAGFVVSRGDVEEKLTVDEVVSRHLNRLKLAAEDYIGSSVKQAVLTVSSDFTDEQKAALKASAAQVGLEIVQFINEPSAALLAHVEKYPFKEDVNVVVADFGGVRSDAAVIAIRNGIFTILATAHDQHLGGDNLDAELIEYFAKDFEKTNKCNPTKNARSLAKLRANAMVTKKTLSNATTATISIDSLADGFDYHTSINRMRYELVANKVFSQFTSFIENVIAKAELDPLDIQAVLLSGGVSFTPKLTTNLEFIFPESVEILGPQNENASNNPNELASSGAALQAGLVSNYDNEELAEALQPIVVNTPHLPKAIGLIGAHGEFHPVLLPETSYPVQKKITLKNAKGDLLVGVYEGEHHIQEKTVEPEAKEEDEEDSEEWSDDEPEVIREKLYTLSTKLMELGLKDVKNGAEITFNVNKDGVLRVSARDLKSTTVVKGEL
Protein: RE52507p (Q8IGP7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
LPPFEKNDKIEGTESGFAVCQIQSLDMEDILGVLGSLSDLRRELEVLRKAHFEELDHLFYGTGQPEAEAKPRDSAPAAKSQENSSVTPQQTKKRPKRLTSLAEDQNEPEAPDATANNTSARQSTRVSNSQLLAIAEDEHNSTASLMPPPPVPVSADTTLGSGRPQRAAKLKTEKLLKEPSLNRKMRRPSSEELVKVKVESEQRVSQFNSFTSAQALEENKLAEPELEEPAAETAEQQKPPEEASVTEDVNTTKTLRVKVKREKLSTEAVPPLTNAVSTANVTTVSSVTTEAARPDDTVASNTTTSTEVSKKVRKKKKDVESHRPIKVERFSDLDKSSPVSSRTRKCSSDSRTVQERSIYKDALEDPPVAEQSVAAVAPAAVNETVAISNATLVLGPAPTSDSPIGPAGDATFEVHSNDKKQPLSKQDSLLTEDESVEEKLPTTKLLSSIKAIKLPTRTHELFNPLLQSPVKMRVEAFENAANAQNSMRPKRGKDLQGTPGSNNTPKIGKLPAPTVGRFFTPTQTTSTLPLSSAQPKKGPASASKATSLLKTATGTNLRSVNSTSTKTLSRENSGDDFRKGLHNLAEERKKLREQKHQQAAQQREAKERERAERMAKLAAERAKKQEERKRIEERKRQELEELQRKMRQQEEAEALKKAKFKELEQQKLQQLTGAKPKKMLPPPPKTKYTWEMLHEDDSTDDEGKVTHKRPPAPTWSRSHVRGEAIAMQSHCPTDIIDSFFSVAPTTPDLKQIFPNIDPSQLKRNSSVLWSTPPRYSELPKY
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (Q8IQ91)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVSMSLVQGGAAGGAPQGASAILAAAAPYYQPPAVPQDVQPDRPIGYGAFGVVWAVTDPRDGRRVALKKLPNVFQSLVSSKRVFRELKMLCFFKHENVLSALDILQPPHLDFFQEIYVITELLQSDLHKIIVSPQHLSADHIKVFLYQILRGLKYLHSARILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDQAKHMTQEVVTQYYRAPEILMGARHYSSAVDVWSVGCIFGELLGRRILFQAQNPVQQLELITELLGTPTMEDMRHACEGARTHMLRRAPKPPSFSVLYTLSSHATHEAVHLLCQMLVFDPDKRISVTDALAHPYLDEGRLRYHSCMCKCCFTTSAGMRQYTADFEPSAGQPFDDLWERKLTSVQQVKEEMHKFIAEQLQTGRVPLCINPQSAAFKSFASSTVAHPSELPPSPHQWE
Protein: Uncharacterized fimbrial-like protein YadC (P31058)
Organism: Escherichia coli (strain K12)
Function: Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches.
Subcellular location: Fimbrium {ECO:0000305}.
Interaction partners:
- Uncharacterized fimbrial-like protein YadM
- Uncharacterized fimbrial-like protein YadK
- Uncharacterized fimbrial-like protein YadL
- Uncharacterized fimbrial-like protein YadN
- Outer membrane usher protein HtrE
- Glutamyl-Q tRNA
Sequence:
MKTIFRYILFLALYSCCNTVSAYTSFIVGNNAGVDNYRGPSTAAQMTFNYTSTASNLVFYKPTQLGPTGVKMYWSYLDTGTGGGILYCNTSGRANPGPITIENAMVYSGKDYGGHKLFNTSVPGLYYTMLISRVWSAYDTITDIQSPGIYIGDPSNQEFFFSVTDSDLQTKGCNKADDYDKFWAIGGIVHNITVEFYTDTNFDPTLNQQVQLSSSSNYLYSFKAYSPGTKVVDHSNHIYVNFTLNNVKLTLPTCFTSILTGPSVNGSTVRMGEYSSGTIKNGASPVPFDISLQNCIRVRNIETKLVTGKVGTQNTQLLGNTLTGSTAAKGVGVLIEGLATSKNPLMTLKPNDTNSVYIDYETEDDTSDGVYPNQGNGTSQPLHFQATLKQDGNIAIEPGEFKATSTFQVTYP
Protein: Netrin-3 (Netrin-2-like protein) (O00634)
Organism: Homo sapiens (Human)
Function: Netrins control guidance of CNS commissural axons and peripheral motor axons.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Neogenin
- Netrin receptor UNC5C
- Netrin receptor UNC5B
- Netrin receptor DCC
Sequence:
MPGWPWGLLLTAGTLFAALSPGPPAPADPCHDEGGAPRGCVPGLVNAALGREVLASSTCGRPATRACDASDPRRAHSPALLTSPGGTASPLCWRSESLPRAPLNVTLTVPLGKAFELVFVSLRFCSAPPASVALLKSQDHGRSWAPLGFFSSHCDLDYGRLPAPANGPAGPGPEALCFPAPLAQPDGSGLLAFSMQDSSPPGLDLDSSPVLQDWVTATDVRVVLTRPSTAGDPRDMEAVVPYSYAATDLQVGGRCKCNGHASRCLLDTQGHLICDCRHGTEGPDCGRCKPFYCDRPWQRATARESHACLACSCNGHARRCRFNMELYRLSGRRSGGVCLNCRHNTAGRHCHYCREGFYRDPGRALSDRRACRACDCHPVGAAGKTCNQTTGQCPCKDGVTGLTCNRCAPGFQQSRSPVAPCVKTPIPGPTEDSSPVQPQDCDSHCKPARGSYRISLKKFCKKDYAVQVAVGARGEARGAWTRFPVAVLAVFRSGEERARRGSSALWVPAGDAACGCPRLLPGRRYLLLGGGPGAAAGGAGGRGPGLIAARGSLVLPWRDAWTRRLRRLQRRERRGRCSAA
Protein: Signal-induced proliferation-associated 1-like protein 3 (SIPA1-like protein 3) (SPA-1-like protein 3) (O60292)
Organism: Homo sapiens (Human)
Function: Plays a critical role in epithelial cell morphogenesis, polarity, adhesion and cytoskeletal organization in the lens.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:26231217}. Note=Detected in tricellular junctions. Colocalizes with apical F-actin. {ECO:0000269|PubMed:26231217}.
Interaction partners:
- Leucine zipper putative tumor suppressor 3
Sequence:
MTTYRAIPSDGVDLAASCGARVGDVLPGPHTGDYAPLGFWAQNGSMSQPLGESPATATATATATTRPSPTTPAMPKMGVRARVADWPPKREALREHSNPSPSQDTDGTKATKMAHSMRSIQNGQPPTSTPASSGSKAFHRLSRRRSKDVEFQDGWPRSPGRAFLPLRHRSSSEITLSECDAEDAGEPRGARHTGALPLFREYGSTSSIDVQGMPEQSFFDILNEFRSEQPDARGCQALTELLRADPGPHLMGGGGGAKGDSHNGQPAKDSLLPLQPTKEKEKARKKPARGLGGGDTVDSSIFRKLRSSKPEGEAGRSPGEADEGRSPPEASRPWVCQKSFAHFDVQSMLFDLNEAAANRVSVSQRRNTTTGASAASAASAMASLTASRAHSLGGLDPAFTSTEDLNCKENLEQDLGDDNSNDLLLSCPHFRNEIGGECERNVSFSRASVGSPSSGEGHLAEPALSAYRTNASISVLEVPKEQQRTQSRPRQYSIEHVDLGARYYQDYFVGKEHANYFGVDEKLGPVAVSIKREKLEDHKEHGPQYQYRIIFRTRELITLRGSILEDATPTATKHGTGRGLPLKDALEYVIPELNIHCLRLALNTPKVTEQLLKLDEQGLCRKHKVGILYCKAGQSSEEEMYNNEEAGPAFEEFLSLIGEKVCLKGFTKYAAQLDVKTDSTGTHSLYTMYQDYEIMFHVSTLLPYTPNNRQQLLRKRHIGNDIVTIIFQEPGALPFTPKNIRSHFQHVFIIVRVHNPCTDNVCYSMAVTRSKDAPPFGPPIPSGTTFRKSDVFRDFLLAKVINAENAAHKSDKFHTMATRTRQEYLKDLAENCVSNTPIDSTGKFNLISLTSKKKEKTKARAGAEQHSAGAIAWRVVAQDYAQGVEIDCILGISNEFVVLLDLRTKEVVFNCYCGDVIGWTPDSSTLKIFYGRGDHIFLQATEGSVEDIREIVQRLKVMTSGWETVDMTLRRNGLGQLGFHVKYDGTVAEVEDYGFAWQAGLRQGSRLVEICKVAVVTLTHDQMIDLLRTSVTVKVVIIPPFEDGTPRRGWPETYDMNTSEPKTEQESITPGGRPPYRSNAPWQWSGPASHNSLPASKWATPTTPGHAQSLSRPLKQTPIVPFRESQPLHSKRPVSFPETPYTVSPAGADRVPPYRQPSGSFSTPGSATYVRYKPSPERYTAAPHPLLSLDPHFSHDGTSSGDSSSGGLTSQESTMERQKPEPLWHVPAQARLSAIAGSSGNKHPSRQDAAGKDSPNRHSKGEPQYSSHSSSNTLSSNASSSHSDDRWFDPLDPLEPEQDPLSKGGSSDSGIDTTLYTSSPSCMSLAKAPRPAKPHKPPGSMGLCGGGREAAGRSHHADRRREVSPAPAVAGQSKGYRPKLYSSGSSTPTGLAGGSRDPPRQPSDMGSRVGYPAQVYKTASAETPRPSQLAQPSPFQLSASVPKSFFSKQPVRNKHPTGWKRTEEPPPRPLPFSDPKKQVDTNTKNVFGQPRLRASLRDLRSPRKNYKSTIEDDLKKLIIMDNLGPEQERDTGQSPQKGLQRTLSDESLCSGRREPSFASPAGLEPGLPSDVLFTSTCAFPSSTLPARRQHQHPHPPVGPGATPAAGSGFPEKKSTISASELSLADGRDRPLRRLDPGLMPLPDTAAGLEWSSLVNAAKAYEVQRAVSLFSLNDPALSPDIPPAHSPVHSHLSLERGPPTPRTTPTMSEEPPLDLTGKVYQLEVMLKQLHTDLQKEKQDKVVLQSEVASLRQNNQRLQEESQAASEQLRKFAEIFCREKKEL
Protein: Phosphatidylinositol:ceramide inositolphosphotransferase 2 (EC 2.7.1.227) (Inositol-phosphorylceramide synthase 2) (AtIPCS2) (IPC synthase 2) (Protein ENHANCING RPW8-MEDIATED HR-LIKE CELL DEATH 1) (Sphingolipid synthase 2) (Q9SH93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of the phosphorylinositol group from phosphatidylinositol (PI) to phytoceramide, an essential step in sphingolipid biosynthesis. May play an important role in modulating plant programmed cell death (PCD) associated with defense (e.g. toward Golovinomyces cichoracearum) by promoting sphingolipid metabolism and thus regulating ceramide accumulation.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19001565}; Multi-pass membrane protein {ECO:0000269|PubMed:19001565}.
Interaction partners:
- Ceramide kinase
- Long chain base biosynthesis protein 1
- Ceramide synthase LOH2
- Long chain base biosynthesis protein 2a
- Accelerated cell death 11
- Uncharacterized CRM domain-containing protein At3g25440
- Inositol phosphorylceramide glucuronosyltransferase 1
- Neutral ceramidase 1
- Ceramide synthase LOH1
- TTF-type zinc finger protein with HAT dimerization domain-containing protein
Sequence:
MTLYIRRESSKLWKRFCSEISTEIGLLAENWKYLLAGLICQYIHGLAAKGVHYIHRPGPTLQDLGFFLLPELGQERSYISETVFTSVFLSFFLWTFHPFILKTKKIYTVLIWCRVLAFLVACQFLRVITFYSTQLPGPNYHCREGSKVSRLPWPKSALEVLEINPHGVMYGCGDLIFSSHMIFTLVFVRTYQKYGTKRFIKLFGWLTAIVQSLLIIASRKHYSVDVVVAWYTVNLVVFCLDKKLPELPDRTAVLLPVISKDRTKEENHKLLNGNGVDPADWRPRAQVNGKIDSNGVHTDNTMNGA
Protein: Auxin-responsive protein IAA1 (Indoleacetic acid-induced protein 1) (Q5VRD1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 11
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 7
- Auxin response factor 9
- Auxin response factor 14
- Auxin response factor 1
- Auxin response factor 3
- Auxin response factor 16
- Auxin response factor 15
- Auxin response factor 2
Sequence:
MSVETERSSTESSAASGLDFEDTALTLRLPGSLAAAAAPDPDRKRSSPSSSDAADAADNSSPLAAAADAPPAPKARVVGWPPVRSFRKNALAAKFVKVAVDGAPYLRKVDLEAYSGYDQLLRALQDKFFSHFTIRKFADDERKLVDAVNGTEYVPTYEDKDGDWMLVGDVPWKMFVETCQRLRLMKSSEAVNLAPRAAQ
Protein: LD24232p (Q8MR26)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLYLEDYLEMIEHLPQELRDRFTEMRELDLAVQNNMDSLDKKAHMFFKQCKRDELQHESMDTEFHSLRGEYFKVMEDADEKVAIATQIHELVERYLRRLDSELFKFKCELEADNNGITEILERRSLELDGNSTAATALLLSMNQKENRYYGASSANTMVNSSTGHATGAATGSSGIALVSGAAGTGGALSSISTAQLGSSQRHRKLEKRRETICTVPVQEKRANLNHSLPVVGSGSTTAAAASSSSATTAAAAASLASATTAQTHVSNHIGSIAATHLTLPVAMGVAGGSSSLASSSLATGTGSLVRQLPTNLTHTVLSTSGGATAAAAAGGNSTSVVAAGTAHGHAHVSGHSAAGATVTYNLQQLGGGAAASSAIAAAASQAIVAT
Protein: Interleukin-15 receptor subunit alpha (IL-15 receptor subunit alpha) (IL-15R-alpha) (IL-15RA) (CD antigen CD215) [Cleaved into: Soluble interleukin-15 receptor subunit alpha (sIL-15 receptor subunit alpha) (sIL-15R-alpha) (sIL-15RA)] (Q60819)
Organism: Mus musculus (Mouse)
Function: High-affinity receptor for interleukin-15. Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. In neutrophils, binds and activates kinase SYK in response to IL15 stimulation (By similarity). In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q13261}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13261}. Nucleus membrane {ECO:0000250|UniProtKB:Q13261}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13261}. Cell surface {ECO:0000250|UniProtKB:Q13261}.; SUBCELLULAR LOCATION: [Soluble interleukin-15 receptor subunit alpha]: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Interleukin-15
- Interleukin-2 receptor subunit beta
- Cytokine receptor common subunit gamma
- Interleukin-2
- Interleukin-2 receptor subunit alpha
- Interleukin-7
- Interleukin-9
- Interferon gamma
- Tyrosine-protein kinase JAK3
- Granulocyte-macrophage colony-stimulating factor
Sequence:
MASPQLRGYGVQAIPVLLLLLLLLLLPLRVTPGTTCPPPVSIEHADIRVKNYSVNSRERYVCNSGFKRKAGTSTLIECVINKNTNVAHWTTPSLKCIRDPSLAHYSPVPTVVTPKVTSQPESPSPSAKEPEAFSPKSDTAMTTETAIMPGSRLTPSQTTSAGTTGTGSHKSSRAPSLAATMTLEPTASTSLRITEISPHSSKMTKVAISTSVLLVGAGVVMAFLAWYIKSRQPSQPCRVEVETMETVPMTVRASSKEDEDTGA
Protein: Antigenic cell wall galactomannoprotein, putative (AFU_orthologue AFUA_4G00870) (Q5AY35)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MRFHIPFLLAIFAIAQASPVAAPHELVRRDGAAVIDAVNIVTESMIALNNTVTAYKGGFLGTFTALKIEFQSIALSNDLRDAISTTKSSANFTEEESLNVSGAFLELQPNIDSTLDNIVSKKPQFDNGLLGIGSLAFLVRSNLEKQKELAGELGDAVVLKLTKTYAVIAPLLNAQIQAKFEEAIAAFE
Protein: Tumor protein p53-inducible nuclear protein 2 (Diabetes and obesity-regulated protein) (Q8CFU8)
Organism: Mus musculus (Mouse)
Function: Dual regulator of transcription and autophagy. Positively regulates autophagy and is required for autophagosome formation and processing. May act as a scaffold protein that recruits MAP1LC3A, GABARAP and GABARAPL2 and brings them to the autophagosome membrane by interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase class III complex, they trigger autophagosome development. Acts as a transcriptional activator of THRA.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm, depending on cellular stress conditions, and re-localizes to autophagosomes on autophagy activation. {ECO:0000250}.
Interaction partners:
- Vacuole membrane protein 1
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Gamma-aminobutyric acid receptor-associated protein-like 1
Sequence:
MFQRFTSLFFNTPAPPEDSNCPGAFVSEEDEVDGWLIIDLQDSYTAPPDPGASPAPAGRPPPAPSLMDESWFVTPPACFTAEGPGLGPARLQSNPLEDLLIEHPSMSVYVTGSTIVLESGPPSPHPEAALPDQDLSDGELAPALREPRALHHAAAPMPARAVLLEKAGQVRRLQRARQRAERHTLSAKVLQRQNRARESRSRRPKHQGSFIYQPCQRQFNY
Protein: Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4) (Q60857)
Organism: Mus musculus (Mouse)
Function: Serotonin transporter whose primary function in the central nervous system involves the regulation of serotonergic signaling via transport of serotonin molecules from the synaptic cleft back into the pre-synaptic terminal for re-utilization. Plays a key role in mediating regulation of the availability of serotonin to other receptors of serotonergic systems. Terminates the action of serotonin and recycles it in a sodium-dependent manner.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P31645}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000269|PubMed:29038237}. Cell junction, focal adhesion {ECO:0000269|PubMed:29038237}. Cell projection, neuron projection {ECO:0000269|PubMed:25600870}. Note=Could be part of recycling endosomes. Density of transporter molecules on the plasma membrane is itself regulated by STX1A. Density of transporter molecules on the plasma membrane is also regulated by serotonin (By similarity). Density of transporter molecules seems to be modulated by ITGAV:ITGB3 (PubMed:29038237). {ECO:0000250|UniProtKB:P31645, ECO:0000250|UniProtKB:P31652, ECO:0000269|PubMed:29038237}.
Interaction partners:
- 5-hydroxytryptamine receptor 1A
- 5-hydroxytryptamine receptor 2A
- Tryptophan 5-hydroxylase 1
- Tryptophan 5-hydroxylase 2
- Synaptic vesicular amine transporter
- 5-hydroxytryptamine receptor 1B
- Amine oxidase [flavin-containing] A
- 5-hydroxytryptamine receptor 2B
- 5-hydroxytryptamine receptor 2C
- 5-hydroxytryptamine receptor 1D
Sequence:
METTPLNSQKVLSECKDKEDCQENGVLQKGVPTPADKAGPGQISNGYSAVPSTSAGDEAPHSTPAATTTLVAEIHQGERETWGKKMDFLLSVIGYAVDLGNIWRFPYICYQNGGGAFLLPYTIMAIFGGIPLFYMELALGQYHRNGCISIWKKICPIFKGIGYAICIIAFYIASYYNTIIAWALYYLISSFTDQLPWTSCKNSWNTGNCTNYFAQDNITWTLHSTSPAEEFYLRHVLQIHQSKGLQDLGTISWQLALCIMLIFTIIYFSIWKGVKTSGKVVWVTATFPYIVLSVLLVRGATLPGAWRGVVFYLKPNWQKLLETGVWVDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQDALVTSVVNCMTSFVSGFVIFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFFLMLITLGLDSTFAGLEGVITAVLDEFPHIWAKRREWFVLIVVITCILGSLLTLTSGGAYVVTLLEEYATGPAVLTVALIEAVVVSWFYGITQFCSDVKEMLGFSPGWFWRICWVAISPLFLLFIICSFLMSPPQLRLFQYNYPHWSIILGYCIGTSSVICIPIYIIYRLISTPGTLKERIIKSITPETPTEIPCGDIRMNAV
Protein: DUF190 domain-containing protein (P95087)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Fluoride-specific ion channel FluC 1
- Fluoride-specific ion channel FluC 2
Sequence:
MNEQCLKLTAYFGERQRAVGGAGRFLADAMLDLFGSHNVATSVMLRGTTSFGPKHEFRCDQSLSLSEDPPVTVAAVDIESKIRSLVDDVTAMTDRGLVTLERARLVTRHSGAEEFGDIDSRNGDAAKLTIYAGRQVRVAGAPAYYTICELLHRHGFAGATVLLGVDGTAHGRRRRARFFGRNVNVPLMIIAVGTPAQVAVAAMELTAALPNPLLTIERVRLCKRDGELFARPQQLPQTDDQGRTLWQKLMVHTAEATHHEGLPIHRALVHRLMQSETARGATALRGIWGFYGDHKPHGDKLFQLVRRVPVTTIIVDTPQAIARSFDIVDELTNWHGLVTSEMVPAAVSLTGSRDGTQKTGETPLARYDY
Protein: Intraflagellar transport protein 27 (Flagellar-associated protein 156) (A8HN58)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Small GTPase-like component of the intraflagellar transport (IFT) complex B. Forms a subcomplex within the IFT complex B with IFT25. Has very low GTPase activity either because it lacks the conserved catalytic Gln in position 79 or because it requires some GTPase-activating protein (GAP) for GTP turnover.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:17276912}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:17276912}. Note=Colocalizes with IFT25 at the distal-most portion of basal bodies, probably the transition zones, and concentrates in the basal body region.
Interaction partners:
Sequence:
MVKKEVKPIDITATLRCKVAVVGEATVGKSALISMFTSKGSKFLKDYAMTSGVEVVVAPVTIPDTTVSVELFLLDTAGSDLYKEQISQYWNGVYYAILVFDVSSMESFESCKAWFELLKSARPDRERPLRAVLVANKTDLPPQRHQVRLDMAQDWATTNTLDFFDVSANPPGKDADAPFLSIATTFYRNYEDKVAAFQDACRNY
Protein: BBSome complex member BBS1 (BBS2-like protein 2) (Bardet-Biedl syndrome 1 protein) (Q8NFJ9)
Organism: Homo sapiens (Human)
Function: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Plays a role in olfactory cilium biogenesis/maintenance and trafficking (By similarity).
Subcellular location: Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.
Interaction partners:
- BBSome complex member BBS5
- BBSome complex member BBS4
- BBSome complex member BBS2
- Tetratricopeptide repeat protein 8
- Protein PTHB1
- BBSome complex member BBS7
- Rab-3A-interacting protein
- BBSome complex assembly protein BBS10
- Leucine zipper transcription factor-like protein 1
- Chaperonin-containing T-complex member BBS12
Sequence:
MAAASSSDSDACGAESNEANSKWLDAHYDPMANIHTFSACLALADLHGDGEYKLVVGDLGPGGQQPRLKVLKGPLVMTESPLPALPAAAATFLMEQHEPRTPALALASGPCVYVYKNLRPYFKFSLPQLPPNPLEQDLWNQAKEDRIDPLTLKEMLESIRETAEEPLSIQSLRFLQLELSEMEAFVNQHKSNSIKRQTVITTMTTLKKNLADEDAVSCLVLGTENKELLVLDPEAFTILAKMSLPSVPVFLEVSGQFDVEFRLAAACRNGNIYILRRDSKHPKYCIELSAQPVGLIRVHKVLVVGSTQDSLHGFTHKGKKLWTVQMPAAILTMNLLEQHSRGLQAVMAGLANGEVRIYRDKALLNVIHTPDAVTSLCFGRYGREDNTLIMTTRGGGLIIKILKRTAVFVEGGSEVGPPPAQAMKLNVPRKTRLYVDQTLREREAGTAMHRAFQTDLYLLRLRAARAYLQALESSLSPLSTTAREPLKLHAVVQGLGPTFKLTLHLQNTSTTRPVLGLLVCFLYNEALYSLPRAFFKVPLLVPGLNYPLETFVESLSNKGISDIIKVLVLREGQSAPLLSAHVNMPGSEGLAAA
Protein: Integrin-linked kinase-associated serine/threonine phosphatase 2C (ILKAP) (EC 3.1.3.16) (PP2Cdelta) (Q9Z1Z6)
Organism: Rattus norvegicus (Rat)
Function: Protein phosphatase that may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. Selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. Inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Glycolipid transfer protein domain-containing 2.
Sequence:
MDLFGDLPEPERPPRPSAGKEAQEGPVLFEDLPPTSSTDSGSGGPLLFDGLPPAGSGNSGSLATSGSQVVKNEGKGAKRKAPEEEKNGGEELVEKKVCKASSVIFGLKGYVAERKGEREEMQDAHVILNDITQECNPPSSLITRVSYFAVFDGHGGIRASKFAAQNLHQNLIRKFPKGDVISVEKTVKRCLLDTFKHTDEEFLKQASSQKPAWKDGSTATCVLAVDNILYIANLGDSRAILCRYNEESQKHAALSLSKEHNPTQYEERMRIQKAGGNVRDGRVLGVLEVSRSIGDGQYKRCGVTSVPDIRRCQLTPNDRFILLACDGLFKVFTPEEAVNFILSCLEDEKIQTREGKPAVDARYEAACNRLANKAVQRGSADNVTVMVVRIGH