wanglab/gogpt-training-data huggingface dataset:
Protein: Catenin delta-2 (Delta-catenin) (GT24) (Neural plakophilin-related ARM-repeat protein) (NPRAP) (Neurojungin) (Q9UQB3)
Organism: Homo sapiens (Human)
Function: Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses. Involved in the regulation of Wnt signaling. It probably acts on beta-catenin turnover, facilitating beta-catenin interaction with GSK3B, phosphorylation, ubiquitination and degradation (By similarity). Functions as a transcriptional activator when bound to ZBTB33 (By similarity). May be involved in neuronal cell adhesion and tissue morphogenesis and integrity by regulating adhesion molecules.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O35927}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O35927}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35116}. Perikaryon {ECO:0000269|PubMed:22022388}.
Interaction partners:
- Presenilin-1
- Cadherin-17
- Transcriptional regulator Kaiso
- PDZ domain-containing protein 2
- Lymphoid enhancer-binding factor 1
- Transcription factor 7-like 1
- Transcription factor 7-like 2
- Transcription factor 7
- Cadherin-1
- Leucine-rich repeat-containing protein 7
Sequence:
MFARKPPGAAPLGAMPVPDQPSSASEKTSSLSPGLNTSNGDGSETETTSAILASVKEQELQFERLTRELEAERQIVASQLERCKLGSETGSMSSMSSAEEQFQWQSQDGQKDIEDELTTGLELVDSCIRSLQESGILDPQDYSTGERPSLLSQSALQLNSKPEGSFQYPASYHSNQTLALGETTPSQLPARGTQARATGQSFSQGTTSRAGHLAGPEPAPPPPPPPREPFAPSLGSAFHLPDAPPAAAAAALYYSSSTLPAPPRGGSPLAAPQGGSPTKLQRGGSAPEGATYAAPRGSSPKQSPSRLAKSYSTSSPINIVVSSAGLSPIRVTSPPTVQSTISSSPIHQLSSTIGTYATLSPTKRLVHASEQYSKHSQELYATATLQRPGSLAAGSRASYSSQHGHLGPELRALQSPEHHIDPIYEDRVYQKPPMRSLSQSQGDPLPPAHTGTYRTSTAPSSPGVDSVPLQRTGSQHGPQNAAAATFQRASYAAGPASNYADPYRQLQYCPSVESPYSKSGPALPPEGTLARSPSIDSIQKDPREFGWRDPELPEVIQMLQHQFPSVQSNAAAYLQHLCFGDNKIKAEIRRQGGIQLLVDLLDHRMTEVHRSACGALRNLVYGKANDDNKIALKNCGGIPALVRLLRKTTDLEIRELVTGVLWNLSSCDALKMPIIQDALAVLTNAVIIPHSGWENSPLQDDRKIQLHSSQVLRNATGCLRNVSSAGEEARRRMRECDGLTDALLYVIQSALGSSEIDSKTVENCVCILRNLSYRLAAETSQGQHMGTDELDGLLCGEANGKDAESSGCWGKKKKKKKSQDQWDGVGPLPDCAEPPKGIQMLWHPSIVKPYLTLLSECSNPDTLEGAAGALQNLAAGSWKWSVYIRAAVRKEKGLPILVELLRIDNDRVVCAVATALRNMALDVRNKELIGKYAMRDLVHRLPGGNNSNNTASKAMSDDTVTAVCCTLHEVITKNMENAKALRDAGGIEKLVGISKSKGDKHSPKVVKAASQVLNSMWQYRDLRSLYKKDGWSQYHFVASSSTIERDRQRPYSSSRTPSISPVRVSPNNRSASAPASPREMISLKERKTDYECTGSNATYHGAKGEHTSRKDAMTAQNTGISTLYRNSYGAPAEDIKHNQVSAQPVPQEPSRKDYETYQPFQNSTRNYDESFFEDQVHHRPPASEYTMHLGLKSTGNYVDFYSAARPYSELNYETSHYPASPDSWV
Protein: Thymine dioxygenase JBP1 (EC 1.14.11.6) (J-binding protein 1) (Thymidine hydroxylase JBP1) (Q9U6M1)
Organism: Leishmania tarentolae (Sauroleishmania tarentolae)
Function: Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Also specifically binds to base J-containing DNA (J-DNA). Involved in propagation and maintenance of DNA base J synthesis initiated by JBP2 by specifically binding already synthesized DNA base J and propagating J synthesis. Thymine dioxygenase activity and J-DNA-binding are independent functions.
Subcellular location: Nucleus {ECO:0000269|PubMed:17389644, ECO:0000269|PubMed:21415010}. Note=Localizes to discrete spots in the nucleus, probably the J-rich telomeres.
Interaction partners:
Sequence:
MEPDSKKVKLDIFNFPTTRETRTPEEVAESYAEAVKSHPFYDNVHSVVDFYDSGTIKDGRGQIIGVVLREALPKYAASMASELLTSAAVRTSLRSMMFGGEPPLSGIAGYFDYRGSPVELKSRKTSFTYEHEAAWPAVFPVVDYVSEIYRHVAPERWKAQNDAIPDLVRIHGTPFSTLTINSRFRTASHTDVGDFDAGYSCIACLDGQFKGLALSFDDFGINVLLQPRDVMIFDSHHFHSNTEVELSFSGEDWKRLTCVFYYRAALGEPASYAEYQRRLEKSKTDTRFTPVVHHVRVKENGTSVNRPSPVYPISQSPFWVPMVAHCLQHCASAAQCVHEAMTADGSRLAEMMFGESLSTSDGIPLRGEDEKVKANGDSTPRPLSRLGGFSETNLMVSTAVEKKKYLDSEFLLHCISAQLLDMWKQARARWLELVGKEWAHMLALNPERKDFLWKNQSEMNSAFFDLCEVGKQVMLGLLGKEVALPKEEQAFWIMYAVHLSAACAEELHMPEVAMSLRKLNVKLKDFNFGGTRYFKDMPPEEKKRRMERKQRIEEARRHGMPSGSHEKRANWLTNDSFDYQTEDCVIDYAQHKWVLPALHAKEVTKTVRTGELPTTERVVRVLVVIPDPQSKLENVDCKLEVPDMVGSSSEWERLMSSPAVHRVLSAAQRNLQLPDSVTHGNVQTHFAFHSTLPTDIYDFVVLQHVLSRIPDDAQASAYIRRAAALCSGCLFVVETDVQCRQYYTLKYSIRCSYDTVAPLFFQQLHRVCYGTKTARVRTKGELESLIPTVCCARYKLQGSPLNTTVHVVSPFPSCEVQNLSSALCDRA
Protein: Uncharacterized oxidoreductase At1g06690, chloroplastic (EC 1.-.-.-) (Q94A68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:22274653}.
Interaction partners:
- Long-chain-alcohol oxidase FAO4A
- Nuclear pore complex protein NUP107
Sequence:
MAMATHFTFPFNYVVSEGSHGRRSFVRKLVRAVASGDSVAPAISEESKVKLGGSDLKVTKLGIGVWSWGDNSYWNDFQWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLLGRFIRERKERYPGAEVSVATKFAALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLWGNEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRGRIYTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLASEIKPVVGFPVEYL
Protein: Ribosomal protein L18 (G3V203)
Organism: Homo sapiens (Human)
Subcellular location: Rough endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004427}.
Interaction partners:
Sequence:
MGVDIRHNKDRKVRRKEPKSQDIYLRLLVKLYRFLARRTNSTFNQVVLKRLFMSRTNRPPLSLSRMIRKMKLPGRENKTAVVVGTITDDVRVQEVPKLKVCALRVTSRARSRILRAGGKILTFDQLALDSPKGCGTVLLSGPRKGREVYRHFGKAPGTPHSHTK
Protein: Aminotriazole resistance protein (P13090)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Putative component of the machinery responsible for pumping aminotriazole (and possibly other toxic compounds) out of the cell. Probable ATP-dependent export permease. Appears to confer resistance only to aminotriazole.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Fluconazole resistance protein 1
- Azole resistance protein 1
- Protein SGE1
Sequence:
MGNQSLVVLTESKGEYENETELPVKKSSRDNNIGESLTATAFTQSEDEMVDSNQKWQNPNYFKYAWQEYLFIFTCMISQLLNQAGTTQTLSIMNILSDSFGSEGNSKSWLMASFPLVSGSFILISGRLGDIYGLKKMLLVGYVLVIIWSLICGITKYSGSDTFFIISRAFQGLGIAFVLPNVLGIIGNIYVGGTFRKNIVISFVGAMAPIGATLGCLFAGLIGTEDPKQWPWAFYAYSIAAFINFVLSIYAIPSTIPTNIHHFSMDWIGSVLGVIGLILLNFVWNQAPISGWNQAYIIVILIISVIFLVVFIIYEIRFAKTPLLPRAVIKDRHMIQIMLALFFGWGSFGIFTFYYFQFQLNIRQYTALWAGGTYFMFLIWGIIAALLVGFTIKNVSPSVFLFFSMVAFNVGSIMASVTPVHETYFRTQLGTMIILSFGMDLSFPASSIIFSDNLPMEYQGMAGSLVNTVVNYSMSLCLGMGATVETQVNSDGKHLLKGYRGAQYLGIGLASLACMISGLYMVESFIKGRRARAAAEYDCTVA
Protein: Accessory protein 7b (Q7T6S2)
Organism: Severe acute respiratory syndrome coronavirus (SARS-CoV)
Subcellular location: Host membrane {ECO:0000256|ARBA:ARBA00004379}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004379}.
Interaction partners:
Sequence:
MNELTLIDFYLCFLAFLLFLVLIMLIIFWFSLEIQDLEEPCTKV
Protein: Transcription factor (Q6FTT1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002595}.
Interaction partners:
- Phosphorelay intermediate protein YPD1
- Mitogen-activated protein kinase HOG1
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Elongation factor 1-alpha
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
Sequence:
MDYEVNANQIPVLGIEQGLIPDNLDGSVKADTATSTAMNMNDKSEISNDGSHSIHTSNPNNNGENGKNGGKPASNDFVRKLFNILESNQYSNIVRWSNTGDSFVVLDTGKFTTQILPNHFKHSNFASFVRQLNKYDFHKIKRTNEERQKSIYGEQSWEFENPNFKINDEKSLDLIKRKTPAQRKVMLEDASAPSQKTPELLSVQSENKLKSALLSNTVKKDIFNNLRKRVDKMQKDMDTVMMDNYNLKSDYQKLATKYNTLLDSLITFRTVNENLINNFNALCNVLSSKGVELPSSVYENMNINIPVPSGQSPVNISPSPSLGIPIKNSTMSPSLPSMKSLQNTPSLTGKLSTNQRLDLPPNSQGILSDTNVGQTESPEIQMPISSNSSSTTKEVDQNIVLRKGFHVLLVEDDSVSIQLCSKFLRKYGCTVQVVTDGLSAISNLEKFRYDLVLMDIVMPNLDGATATSIVRSFDNQTPIIAMTGNIEDQDLITYLQHGMNDILAKPFTRNDLHSILIRHLKDRIPLCDQNRGSGITSESPNLPPTQHIISSQQNNEQNSSLPQSLPPIHPPNHQSPLFNNRASNITPLAPLNSAMSPQSPSHLERPLTNRSPLGMTPLNDGQPAFKKQHT
Protein: Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic (RA) (RuBisCO activase) (Q9AXG0)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Plastid, chloroplast stroma {ECO:0000256|ARBA:ARBA00004470, ECO:0000256|RuleBase:RU369045}.
Interaction partners:
Sequence:
FNNTRQVPSGSFKVMAAEKEIDEETQTEKDRWKGLAYDISDDQQDITRGKGMVDSLFQAPMNDGTHYAVMSSYEYISQGLKTYNLDNNMDGFYIAPAFMDKLVVHISKNFMSLPNIKVPLILGIWGGKGQGKSFQCELVFAKMGINPIMMSAGELESGNAGEPAKLIRQRYREAADIIKKGKMCALFINDLDAGAGRMGGTTQYTVNNQMVNATLMNIADNPTNVQLPGMYNKEENPRVPIIVTGNDFSTLYAPLIRDGRMEKFYWAPTRDDRIGVCKGIFRTDGVRDEDIVKLVDTFPGQSIDFFGALRARVYDDEVRKWISEVGVASVGKKLVNSREGPPTFEQPKMTIEKLLEYGNMLVAEQENVKRVQLADKYLSEAALGEANEDSINRGTFYGKAAQQVGVPVPEGCTDPNADNFDPTARSDDGTCTYKF
Protein: Inteferon phi 4 (Interferon phi 4) (C5IX16)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Interferon phi 3.
- Interferon phi 2
- Cytokine receptor family member b2
- Interleukin 10 receptor, beta.
- Cytokine receptor family member b1.
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon gamma related precursor
- Cytokine receptor family member B15.
Sequence:
MKVFAAAQFCVLLSVGFSSVLGCRWVKHRLQHHHGVSLDLLRKMGEKVHDDNEDLNPIPYDLINNHRMAEPEKQIQFVIQALVEITALFDDALVPWDAKKMDDFLNIMHEEIDGLRSCGSYKMKRNKKLHLYFNRLRRMTELNTDGGRSWEMVRKRVISLMNQLHSFSFHTHV
Protein: 14-3-3 protein gamma [Cleaved into: 14-3-3 protein gamma, N-terminally processed] (P61982)
Organism: Mus musculus (Mouse)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29678907}. Mitochondrion matrix {ECO:0000250|UniProtKB:P61981}. Note=Translocates to the mitochondrial matrix following induction of MALM (mitochondrial protein catabolic process). {ECO:0000250|UniProtKB:P61981}.
Interaction partners:
- Serine/threonine-protein kinase B-raf
- 14-3-3 protein epsilon
- RAF proto-oncogene serine/threonine-protein kinase
- M-phase inducer phosphatase 2
- Serine/threonine-protein kinase A-Raf
- M-phase inducer phosphatase 3
- 14-3-3 protein zeta/delta
- Forkhead box protein O3
- Transcriptional coactivator YAP1
- WW domain-containing transcription regulator protein 1
Sequence:
MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN
Protein: DLim1 (GH04929p) (LIM homeobox 1, isoform A) (Q9V472)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Cyclin-K
- RE70879p
- Chip, isoform B
- Inhibitory POU protein
Sequence:
MAFGAVLHTSQHNIGRSEPPVGVGDPCAGCNKPILDKFLLNVLERAWHASCVRCCECLQPLTDKCFSRESKLYCRNDFFRRYGTKCSGCGQGIAPSDLVRKPRDKVFHLNCFTCCICRKQLSTGEQLYVLDDNKFICKDDYLLGKAPSCGHNSLSDSLMGSASEDDDDDDPPHLRATALGLGVLGPNGPDSAGGPLGTSDISVQSMSTDSKNTHDDSDQGSLDGDPDGRGDSQAENKSPDDANGSKRRGPRTTIKAKQLEVLKTAFNQTPKPTRHIREQLAKETGLPMRVIQVWFQNKRSKERRMKQITSMGRPPFFGGARKMRGFPMNLSPGGLDDGPGFPYFAADAKFEFGYGGPFHPHDGPYFPGHPGGPMPFNAPGGPMDHSGPIPMVNEFGLTPEATFLGQAGGPPMQLQSAVGPPPPPPPPSAEHLMAAAAAAAQQQAAQQQQQQQQQQQQQQQQNAQQAANQTQQQQQQNGPRTNSPEFMSSANFSEPQNMQNEGLVW
Protein: carboxylesterase (EC 3.1.1.1) (Q9VIC3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEIRVGVGDLLKMGTKLIGHKIVQYRLGTKQTKVVCTRDGQVRGHRRRTLYDEEMYFAFEGIPFAQPPVGELRFRAPQPPHPWLGVRDCTYPRAKPMQKHFVLSIVEGSEDCLYLNVYSKRLRSDKPLPVIVWIYGGGFQFGEAGRDFYSPDYFMQQDVVVVTFNYRVGALGFLSLADRDLDVPGNAGLKDQVMALRWISQNIAQFNGDPQNITVMGESAGAASVHALMTTEQTRGLFHKAIMQSGSMFCEWANEPSGRWAYRLACQLGYSGSENEKEVFRYLQKAPASEMAAQGITLVSQEERRQYVLFPFTPVVEPYITRDCVLPRCHREMLPEAWGNDLPLILGGNSFEGLFSYQSTLHDEEHMLSAFEVLIPREIREKSTQSHLKDLLRQFKVDNFDDATRGRMEFNECLHILSVKHFWHGIHRTVLARLSHAPATPTYLYRFDVDSPHFNHFRQVMCGKHVRGVSHADDLSYLFYHILANKVDKSSMEYQTIQRLVGMWVAFARNDNPNCPQIGPTTWEALDEKGPQMCLNIGKQLEFIVLPESKQNRIWDRLYDKNDLF
Protein: LOC445850 protein (Zw10 kinetochore protein L homeolog) (Q498I0)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MASFVTEVLANSGRLEKEDLGTKIRRLSRRVDELKGEVCDTINKKYDEFLPSMQSAEDLVTQVHGLVSDVDVLKSRIETEVKSDLKVAVNEFTELKQQLEKNTVILGVLKQLQEFDSAIEKYNCALTGKNYISAARHLEKAHSCLKVLKSRKGCELKLLKSFGIELTVQKQNLLYHLGEEWQQLAVWKLPPSKENSSMEMIMKTELHLCTLPSNDESTTVPLLGSVLQAFAILGELNTKLKFFSQLLLNYILKPLVSYPSLHAQMETQQQGVILRFERIETQLEHPPPAEVFIKLRLVFELLHKHLLDVPVEDSPQTGETGKVVLADVLGEMIWEEISEAIIKDCLVYSIPNNSSKLVQYEEVINATEEFENALKGMNYLKGDATELLKYARNVNAHFASKKCQDVIVVARNLMTSEIHNTVKITPDSKITLPVLPKCEDSEKVIKKEKKLSQEAPGLENDVKLNQHTFALPTCRISESVQKLMELAYQTLSEATASSKPCSIQLFYTVRNIFHLFYDVVPTYHKENLQKLPQLSAIHHNNCMYIAHHLLTLGHQFRYHLPSPLSDGAATFVDMVPGFRRLGTESFLAQMRSQKGDLLERLSNARNLSNMEDEDNYTAAHKAIRQVVHQLSRLGKVWQDVLPVAIYCKAMGTLLNTTIVEMIGKITALEDISTEDGERLYTLCRTMIEEGPLLFTPMAEEIKNKKFQEEVPLYVQKWMKFKEQLIILQASLQEIVDRWADGKGPLAVEFSTSEVKNLIRALFQNTERRAAALAKIK
Protein: Retinoic acid early transcript 1L (A0A8I5ZTU3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MTMAKRGTTKCNLSLSLGLLLLLNFLGTAMLEDVHSLSCNLIIRSPTKAEPLWYEGQCSMDGIDFLSFNNVNKTMPLGNQEKMANATEVWTCVTQWIDLLGQDLRDKVSEIKGDTTKTSGHPTLWVTMLSNHSHRHIIGASCVFNISENYSFILDLKTMKWKLINPVPEDIMKEWKDDATLMKHLNLSIAECSQKFNEFLNQHEERTRSRTRAPDIAQPPPTRQFPYKEVLIPVVLIIFIIFICICVKRMCCTQGGRELQLLKDYYINLHKPQRNEGLEETKGEVPNQSTKMLSQEEDPKTLGGPRRASESVELELQMFSSTGS
Protein: SCF E3 ubiquitin ligase complex F-box protein GRR1 (F-box and leucine-rich repeat protein GRR1) (F-box/LRR-repeat protein GRR1) (P24814)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. Probably constitutes the primary response element required for the generation or interpretation of the signal that induces glucose repression.
Subcellular location: Membrane {ECO:0000269|PubMed:1922034}. Note=Associated with the particulate fraction. Probably forms a complex by protein-protein interactions via its leucine-rich segment.
Interaction partners:
- Suppressor of kinetochore protein 1
- Cell division control protein 53
- G1/S-specific cyclin CLN1
- G1/S-specific cyclin CLN2
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- RING-box protein HRT1
- Cell division control protein 4
- Glucose transport transcription regulator RGT1
Sequence:
MDQDNNNHNDSNRLHPPDIHPNLGPQLWLNSSGDFDDNNNNNNNNNNNNSTRPQMPSRTRETATSERNASEVRDATLNNIFRFDSIQRETLLPTNNGQPLNQNFSLTFQPQQQTNALNGIDINTVNTNLMNGVNVQIDQLNRLLPNLPEEERKQIHEFKLIVGKKIQEFLVVIEKRRKKILNEIELDNLKLKELRIDNSPQAISYLHKLQRMRLRALETENMEIRNLRLKILTIIEEYKKSLYAYCHSKLRGQQVENPTDNFIIWINSIDTTESSDLKEGLQDLSRYSRQFINNVLSNPSNQNICTSVTRRSPVFALNMLPSEILHLILDKLNQKYDIVKFLTVSKLWAEIIVKILYYRPHINKKSQLDLFLRTMKLTSEETVFNYRLMIKRLNFSFVGDYMHDTELNYFVGCKNLERLTLVFCKHITSVPISAVLRGCKFLQSVDITGIRDVSDDVFDTLATYCPRVQGFYVPQARNVTFDSLRNFIVHSPMLKRIKITANNNMNDELVELLANKCPLLVEVDITLSPNVTDSSLLKLLTRLVQLREFRITHNTNITDNLFQELSKVVDDMPSLRLIDLSGCENITDKTIESIVNLAPKLRNVFLGKCSRITDASLFQLSKLGKNLQTVHFGHCFNITDNGVRALFHSCTRIQYVDFACCTNLTNRTLYELADLPKLKRIGLVKCTQMTDEGLLNMVSLRGRNDTLERVHLSYCSNLTIYPIYELLMSCPRLSHLSLTAVPSFLRPDITMYCRPAPSDFSENQRQIFCVFSGKGVHKLRHYLVNLTSPAFGPHVDVNDVLTKYIRSKNLIFNGETLEDALRRIITDLNQDSAAIIAATGLNQINGLNNDFLFQNINFERIDEVFSWYLNTFDGIRMSSEEVNSLLLQVNKTFCEDPFSDVDDDQDYVVAPGVNREINSEMCHIVRKFHELNDHIDDFEVNVASLVRVQFQFTGFLLHEMTQTYMQMIELNRQICLVQKTVQESGNIDYQKGLLIWRLLFIDKFIMVVQKYKLSTVVLRLYLKDNITLLTRQRELLIAHQRSAWNNNNDNDANRNANNIVNIVSDAGANDTSNNETNNGNDDNETENPNFWRQFGNRMQISPDQMRNLQMGLRNQNMVRNNNNNTIDESMPDTAIDSQMDEASGTPDEDML
Protein: Heparan sulfate glucosamine 3-O-sulfotransferase 2 (EC 2.8.2.29) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2) (Heparan sulfate 3-O-sulfotransferase 2) (Q673U1)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate (By similarity). Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS (By similarity). Unlike HS3ST1/3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
Sequence:
MAYRVLGRAGPPQPRRARRLLFAFTLSLSCTYLCYSFLCCCDGLGQSRLLGAPRCLRGPSASGQKLLAKSRPCDPPGPTPSEPSAPSAPAAAAPAPRLSGSNHSGSPKPGTKRLPQALIVGVKKGGTRAVLEFIRVHPDVRALGTEPHFFDRNYGRGLDWYRSLMPRTLETQITLEKTPSYFVTQEAPRRIFNMSRDTKLIVVVRNPVTRAISDYTQTLSKKPDIPTFEGLSFRNRSLGLVDVSWNAIRIGMYALHLESWLRYFPLAQIHFVSGERLITDPAGEMGRIQDFLGIKRFITDKHFYFNKTKGFPCLKKPESTLLPRCLGKSKGRTHVQIDPEVIDQLREFYRPYNIKFYETVGQDFRWE
Protein: Autophagy-related protein 39 (Q06159)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a receptor for reticulophagy and nucleophagy. Directs autophagic sequestration of double-membrane vesicles derived from the nuclear envelope and perinuclear endoplasmic reticulum (pnER) into autophagosomes. Is not required for the cytoplasm-to-vacuole targeting pathway, mitophagy, pexophagy, and non-selective autophagy.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26040717}; Single-pass membrane protein {ECO:0000255}. Preautophagosomal structure membrane {ECO:0000269|PubMed:26040717}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Autophagy-related protein 40
- Autophagy-related protein 8
- Autophagy-related protein 11
- Autophagy-related protein 34
- Autophagy-related protein 36
- Autophagy-related protein 32
- Autophagy-related protein 19
- Translocation protein SEC62
- Ubiquitin-like modifier-activating enzyme ATG7
- Nucleus-vacuole junction protein 1
Sequence:
MSEEDDHWNLVRLRRLRKGREGEEQSSKSEISLDSLHESSFAGEDDEDFDADVLSNTSSEESAQMNRIYDFRTSNEFSNAGVNIDQTGVPTISESFDTLSGSNVGGTVLPSMEGSKLKDSTIRNSSTLSDHIIDKSEGKSAKLKMWHVIMLSSLLSMTFSYLALEYSLTGDVLAGFKSQQSLRNNERKLLYGNIDFVDKKSYDSSSDSLSQWAPSGKYYVDFDNHIAYPLKDDDLMGWRRYKTDLVILWYTTKARMKDGWHKRINKINGGRIKLHLFLKNSFKSAQESLRVLHKEQKRRWKRLFVLLHNKYRQFSPHIKRYFDHSCQKAKQCWSGSRLQLRKLRFKSMKPFRVFQFKVRKDTNWFVKQLKRFGLKLQHSRMYKAMSECRKKNYFKCKH
Protein: Importin subunit beta-1 (Importin-95) (Karyopherin subunit beta-1) (Karyopherin-95) (O13864)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Importin beta subunit that functions in nuclear protein import through association with the importin alpha subunit, which binds to the clasical nuclear localization signal (cNLS) in cargo substrates. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by importin beta through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binds to importin beta and the three components separate, leading to release of the cargo. Importin alpha and beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin beta. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06142}. Nucleus envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q06142}.
Interaction partners:
- Importin subunit alpha-2
- Importin subunit alpha-1
- GTP-binding nuclear protein spi1
- Nucleoporin nup60
- Nucleoporin nup124
- Importin subunit beta-3
- H/ACA ribonucleoprotein complex subunit cbf5
- 25S rRNA
- Probable importin c550.11
- Probable importin subunit beta-4
Sequence:
MNAGEFLAQTLSPDANVRLNAEKQLENAARTDFAQYMVLLAQELANDNSMPYIRMAAGLALKNAITAREEARKLEYQQLWQSLPVEIKQQVKSLALQTLGSSEHQAGQSAAQLVAAIAAYELATNQWPDLMVTLVANVGEGQPSALKQHSLQTIGYICESVSPEVLSAQSNAILTAVVAGARKEEPDAAVRLAALGALYDSLEFVRENFNNEYERNYIMQVVCEATQSPEASIQTAAFGCLVKIMHLYYDTMPFYMEKALFALTTQGMYNTNEQVALQAVEFWSTVCEEEIEVNLEIQEAQDLNEVPARQNHGFARAAAADILPVLLKLLCNQDEDADEDDWNISMAAATCLQLFAQVVGDLIVNPVLAFVEQNIQNPDWHQREAAVMAFGSVLEGPNVAMLTPLVNQALPVLINMMVDPVIFVKDTTAWALGQISSFVADAINPEIHLSPMVSALLQGLTDNPRIVANCCWAFMNLVCHFAPVDNHQTSVMTPFYEAIIGSLLHVTDQKGNENNSRTSGYETLGTLITFSSDSVLPMIANVLSIILTRLETSIQMQSQILDVEDRANHDELQSNLCNVLTSIIRRFGPDIRTSSDQIMNLLLQTMQTAPKQSVVHEDVLLAIGAMMNSLEEQFEVYVPSFVPFLSSALSNEQEYQLCSVAVGLVGDLARALNAKILPYCDDFMTRLVQDLQSSVLDRNVKPAILSCFSDIALAIGAAFQTYLEAVMVLLQQASSVQAPPGANFSMIDYVDALRLGIVEAYVGITQAVRTDNRLDLIQPYVHSMFTLLNMITADPECSESLTRAALGLLGDLAESFPKGELKSYFAADWVAALLNSGKTKISSQQTKDLARWATEQVKRQARA
Protein: Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4) (P31645)
Organism: Homo sapiens (Human)
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:0000269|PubMed:12869649, ECO:0000269|PubMed:16870614, ECO:0000269|PubMed:17506858, ECO:0000269|PubMed:27049939}; Multi-pass membrane protein {ECO:0000269|PubMed:27049939}. Endomembrane system {ECO:0000269|PubMed:16870614}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:16870614}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000250|UniProtKB:Q60857}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q60857}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q60857}. Note=Could be part of recycling endosomes (PubMed:16870614). Density of transporter molecules on the plasma membrane is itself regulated by STX1A (By similarity). Density of transporter molecules on the plasma membrane is also regulated by serotonin (PubMed:17506858). Density of transporter molecules seems to be modulated by ITGAV:ITGB3 (By similarity). {ECO:0000250|UniProtKB:P31652, ECO:0000250|UniProtKB:Q60857, ECO:0000269|PubMed:16870614, ECO:0000269|PubMed:17506858}.
Interaction partners:
- D
- 5-hydroxytryptamine receptor 1A
- 5-hydroxytryptamine receptor 2A
- Tryptophan 5-hydroxylase 1
- Catechol O-methyltransferase
- Amine oxidase [flavin-containing] A
- 5-hydroxytryptamine receptor 1B
- Syntaxin-1A
- Tryptophan 5-hydroxylase 2
- Neurotrophic factor BDNF precursor form
Sequence:
METTPLNSQKQLSACEDGEDCQENGVLQKVVPTPGDKVESGQISNGYSAVPSPGAGDDTRHSIPATTTTLVAELHQGERETWGKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLPYTIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYAICIIAFYIASYYNTIMAWALYYLISSFTDQLPWTSCKNSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIHRSKGLQDLGGISWQLALCIMLIFTVIYFSIWKGVKTSGKVVWVTATFPYIILSVLLVRGATLPGAWRGVLFYLKPNWQKLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQDALVTSVVNCMTSFVSGFVIFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFFLMLITLGLDSTFAGLEGVITAVLDEFPHVWAKRRERFVLAVVITCFFGSLVTLTFGGAYVVKLLEEYATGPAVLTVALIEAVAVSWFYGITQFCRDVKEMLGFSPGWFWRICWVAISPLFLLFIICSFLMSPPQLRLFQYNYPYWSIILGYCIGTSSFICIPTYIAYRLIITPGTFKERIIKSITPETPTEIPCGDIRLNAV