wanglab/gogpt-training-data huggingface dataset:
Protein: Double-stranded RNA-binding protein Staufen homolog 2 (Q9NUL3)
Organism: Homo sapiens (Human)
Function: RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell body (By similarity).
Subcellular location: Cytoplasm. Nucleus. Nucleus, nucleolus. Endoplasmic reticulum. Note=Shuttles between the nucleolus, nucleus and the cytoplasm. Nuclear export of isoform 1 is independent of XPO1/CRM1 and requires the exportin XPO5. Nuclear export of isoform 2 and isoform 3 can occur by both XPO1/CRM1-dependent and XPO1/CRM1-independent pathways. Found in large cytoplasmic ribonucleoprotein (RNP) granules which are present in the actin rich regions of myelinating processes and associated with microtubules, polysomes and the endoplasmic reticulum. Also recruited to stress granules (SGs) upon inhibition of translation or oxidative stress. These structures are thought to harbor housekeeping mRNAs when translation is aborted (By similarity). {ECO:0000250}.
Interaction partners:
- Double-stranded RNA-binding protein Staufen homolog 1
- Regulator of nonsense transcripts 1
- Endoribonuclease Dicer
- Fragile X messenger ribonucleoprotein 1
- Insulin-like growth factor 2 mRNA-binding protein 1
- Y-box-binding protein 1
Sequence:
MANPKEKTAMCLVNELARFNRVQPQYKLLNERGPAHSKMFSVQLSLGEQTWESEGSSIKKAQQAVANKALTESTLPKPVQKPPKSNVNNNPGSITPTVELNGLAMKRGEPAIYRPLDPKPFPNYRANYNFRGMYNQRYHCPVPKIFYVQLTVGNNEFFGEGKTRQAARHNAAMKALQALQNEPIPERSPQNGESGKDVDDDKDANKSEISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVSVGEFSAEGEGNSKKLSKKRAATTVLQELKKLPPLPVVEKPKLFFKKRPKTIVKAGPEYGQGMNPISRLAQIQQAKKEKEPDYVLLSERGMPRRREFVMQVKVGNEVATGTGPNKKIAKKNAAEAMLLQLGYKASTNLQDQLEKTGENKGWSGPKPGFPEPTNNTPKGILHLSPDVYQEMEASRHKVISGTTLGYLSPKDMNQPSSSFFSISPTSNSSATIARELLMNGTSSTAEAIGLKGSSPTPPCSPVQPSKQLEYLARIQGFQAALSALKQFSEQGLDPIDGAMNIEKGSLEKQAKHLREKADNNQAPPGSIAQDCKKSNSAV
Protein: Cartilage acidic protein 1 (68 kDa chondrocyte-expressed protein) (CEP-68) (ASPIC) (Protein CRTAC1-B) (Q8R555)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
Sequence:
MAPSADPGMVRMALLLLPPLWLLPLTGGSQRAEPMFTAVTNSVLPPDYDSNPTQLNYGVAVTDVDHDGDFEIVVAGYTGPNLVLKYNRAQNRLVNIAVDERSSPYYALRDRQGNAIGVTACDIDGDGREEIYFLNTNNAFSGVATYTDKLFKFRNNRWEDILSDDVNVARGVASLFAGRSVACVDRTGSGRYSIYIANYAYGDVGPDALIEMDPEASDLSRGILALRDVAAEAGVSKYTAGRGVSVGPILSSSASDIFCDNENGPNFLFHNQGNGTFVDTAASAGVDDPHQHGRGVALADFNRDGKVDIVYGNWNGPHRLYLQMSAHGKVRFRDIASPKFSTPSPVRTVIAADFDNDQELEVFFNNIAYRSSSANRLFRVIRREHGDPLIEELNPGDALEPEGRGTGGVVTDFDGDGMLDLILSHGESMAQPLSVFRGNQGFSNNWLRVVPRTRFGAFARGAKVVLYTKKSGAHLRIIDGGSGYLCEMEPVAHFGLGRDEASSVEVTWPDGKMVSRSVASEEMNSVLEILYPQDEDKLQNTAPLECGQGFSQQDNGHCMDTNECIQFPFVCPRDKPVCVNTYGSYRCRTNKRCNRGYEPNEDGTACVAQVAFLGGYSSAAFRLSEPLSQASYLSLGLGLCLQLYAL
Protein: Acetyl-CoA hydrolase (EC 3.1.2.1) (Acetyl-CoA deacylase) (Acetyl-CoA acylase) (Q9UUJ9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Acetyl-CoA acetyltransferase
- Probable acetyl-coenzyme A synthetase
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Putative aldehyde dehydrogenase-like protein C922.07c
- Homocitrate synthase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- 2-isopropylmalate synthase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Acetyl-CoA carboxylase
Sequence:
MPSLLSSRIRNAEFAKKIVTDPAKLVPYFKNGDYVGWSGFTGVGYPKMIPNALARHVEENNLQGKLRFKLFVGASGGADTECKWAELNMIERRCPHQVGKPISKGINSGRIQFFDKHLSMFPQDLLYGYYTRNRESNTIDTAIIEATAITEDGGIVPGASVGASPELMQLAEKIIIEVNTAIPSFEGLHDIVEIPNPPHRTPININRVDDRIGKPYIKVDPKKVIGIVEADYGDITCANSPQDETSQAIAGHLVDFFHHEVSVGRLPKNLHPLQSGIGNIANAIIGGLAHSPFKDLEVWTEVLQDTFLPLFDSEKLRFATATSTRFSPQGFEKFYSNYDYYKERILLRPQVISNHPEIIRRLGCIAMNTPVEADIYAHANSTNVLGSRMLNGLGGSADFLRNAKLSIMHTPSVRPSKKDPTGITCIVPMATHVDQTEHDLDILVTEQGLADLRGLSPTERAREVIDKCAHPDYKPLLREYFDIAENYCLARGAGHEPHILANAFKMQLNLLEKGTMKIDHW
Protein: Histone deacetylase (EC 3.5.1.98) (A0A8I6G4R8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MNSPNESADGMSGREPSLEILPRTPLHSIPVAVEVKPVLPAAMPSSMGGGGGGSPSPVELRGALAGPMDPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLLGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGTGPGVSSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGSTLTGKFMSTSSIPGCLLGVALEGDTSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQMQLGKILTKTGELSRQPTTHPEETEEELTEQQEALLGEGALTMPREGSTESESTQEDLEEEEDEEEDEEDCIQVKDEDGESGPDEGADLEESSAGYKKLFADAQQLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGSMKSPTDHPTVVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSINAVATLEKVIEIQSKHWSCVQRFATGLGCSLREAQTGEKEEAETVSAMALLSMGAEQAQAAATQEHSPRPAEEPMEQEPAL
Protein: T. brucei spp.-specific protein (Q389D9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLTIRVGNLPVCLCSNLRNTFNPTYAFGVKRNDGTVALLDGKSGHLLLPFDAEGNIIVTPGADYQLVFLSNDSTSSTVHTTQGLGKGGTNKTSHDFELTKALAKDGSIHREKRRLDDGRATSRERFHKGNAHYSVSDSKPTKRRKRDHSVDKDAVVEAEFGSQSINKKERSVKASRKDSNREDSDDPDDIPIFCTLAGKPTPAPISSNHTPTVSPAPKEVYLVDNFDPTTRPAHSEEGALDSSATELISS
Protein: Uncharacterized protein (Q38CL3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSELTAGGKSRGAENLSGVTCGNVNDFVASTDSDTDTLNATARPVTPQQSPPPQSSRAGPRPNEVVGDNWATNRSGGPPGSNVANSGASGVVSDLQFNSQDRAAEGAVPNLSGGFFSLPLNSQLPPHLAAPKDSNNGLNLTDLPTHTNSINCREEVAVPARRTKPKSENCLAKLYYSGMARRKRVEERLEILRARDKELRNCTFKPVITDLAKTMERPGAFPYCRSEEAQLRQRALLETWESKIEKECRPTPKISKGSEQIVQRVRSSSACVIPVADRLYMESARRQCRKQEEEEKGFQQTIPLRRSASDVNALIHRLYELEEKRVATIERKRGELWLDTKPKRRCENSEQLVERLYRPTPRRRRPCKSEPILFSPQVNETTKELSLRANRRRLEQWHQLWSKVWKGYGEKQERQIICCEHLMILKKIDDVARSSGLTGNCTLNDFCTAMEDYERTHGVQHWRLTPLPLKPHVNEDLTFSPVILPSHRERKGSPPAHQRLFEAAKAKQLQQREEERKRREEELRQEEKSRAVSRRASRRSSKQLDIKDPAEKGASAWPCSPTESVSSTDHSRGYKSVELSSLSPSSSPERMPVGFSPPPVWLTPGLIEVAEDLKQLMDEPRGGWSYAQLNHSRTKVDAPPDATLRPSPSVGPKRSGSNHRPLRAPQKKKKRRPVSELLSDELLLECAASRCSPFSWNVSARNREHRDSNRRLRNMGKLLYHKM
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase (EC 2.4.1.109) (G5EB59)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase
- Dolichyl-phosphate-mannose--protein mannosyltransferase
Sequence:
MAEIGFASTTGASFAPDVRRRNVRTEGQARTSGLIEPDDKKHKQRPNSYLSALADWEPLIAPILLTVLSMFTRMYRIGRSNIVTWDEAHFGKFGSHYLKREFYFDVHPPLGKMLVGLSGLLAGYNGSFEFKSGETYPEDLNYTFMRLFNAAFGVVCVPLAYLTARELGFRRGTVWLVSLMVLFENSYATISRFILLDSMLLCFTFTTTFCWAKFHRLQHASFSIEWFTWLFLTGVSIGCVCSVKWVGLFCTALVGLYTIEDLWNKFGDLKMSEATLAKHFAVRVVGLILIPALVYIFSFYIHFLILENSGPGDAQMSSLFQANLKGTQVGKDSPLEIAFGSRVTLKNMGYGGGLLHSHVQTYPEGSSQQQVTCYHHKDANNDWFIYPNRKEPQYDAEAPLRFVGDGDVIRLIHGQTGRNLHSHNIPAPITKNHHEVSCYGNLTIGDDKDHWKVEVVDDVASRDRSRIRTLTTAFRLRHAVLGCYLRAGNTNLPQWGFKQIETTCVKENKPRDVYTHWNIETHTNDRLPPGDPGSYKSPFFKDFVHLNVAMMTSNNALVPDPDKQDDLASKPWQWPILNVGLRMCSWDEKVVKYYLLGNPVVYWGSTLSLAVFGLLTLWYLVRWQRGYNELSQADIDHIHYAGLYPVLGWFLHYVPFIAMARVTYVHHYYPALYYAILTFGFCVDWLTKTLNTKVRFLVYGLLYALVAGVFVYFRVIVFGIEGPSQQWRHLNWLSGWRIAN
Protein: Aspartate--tRNA ligase 2, cytoplasmic (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (Protein IMPAIRED IN BABA-INDUCED DISEASE IMMUNITY 1) (Q9M084)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (By similarity). Involved in the perception of beta-aminobutyric acid (BABA) and required for BABA priming effect in disease resistance.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24776930, ECO:0000305|PubMed:16251277, ECO:0000305|PubMed:16297076}. Endoplasmic reticulum {ECO:0000269|PubMed:24776930}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Glutamyl-tRNA
- Glutamate--tRNA ligase, cytoplasmic
- glutamine--tRNA ligase
- Aspartate--tRNA ligase, chloroplastic/mitochondrial
- Glutamine--tRNA ligase, cytoplasmic
- Proline--tRNA ligase, cytoplasmic
- At4g26980
- Beta-1,3-N-Acetylglucosaminyltransferase family protein
- Eukaryotic translation initiation factor 2 subunit alpha
Sequence:
MSSESEIPPLSSSTAAAEESGEKTSKKAAKKEAAKLEKLRRRQEQEEATRRTASISLEENDEFSNNYGDVTLTELQSSADPKAGKWIEAVEGKEWTDVSDLVEEMLESEVLIRGRVHTNRPTSNKLGFVVLRESGSTVQCVVSQSEKTKVGANMVKYLKQLSRESFVDVIGVVTLPKEPLTGTTQQVEIQVRKVYCINKSLAKLPLSVEDAARSEADIEASLQTPSPAARVNQDTRLNYRVLDLRTPANQAIFQLQYEVEYAFREKLRFKNFVGIHTPKLMAGSSEGGSAVFRLEYKGQPACLAQSPQLHKQMAICGDLRRVFEVGPVFRAEDSFTHRHLCEFVGLDVEMEIRKHYSEIMDLVDELFVFIFTSLNERCKKELQAVGKQYPFEPLKFLPKTLRLTFEEGVQMLKEAGVEVDPLGDLNTESERKLGQLVLEKYNTEFYILHRYPKAVRPFYTMTCADNPLYSNSFDVFIRGEEIISGAQRVHIPEVLEQRAGECGIDVKTISTYIDSFRYGAPLHGGFGVGLERVVMLFCALNNIRKTSLFPRDPQRLSP
Protein: Zinc transporter ZIP3 (Solute carrier family 39 member 3) (Zrt- and Irt-like protein 3) (ZIP-3) (Q9BRY0)
Organism: Homo sapiens (Human)
Function: Acts as a zinc-influx transporter.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q99K24}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q99K24}; Multi-pass membrane protein {ECO:0000255}. Note=Localized primarily at the cell surface but also found in a perinuclear compartment in HC11 cells. In mammary epithelial cell, localized primary to the apical membrane. {ECO:0000250|UniProtKB:Q99K24}.
Interaction partners:
- Zinc transporter ZIP11
- Zinc transporter ZIP4
- Zinc transporter ZIP9
- Zinc transporter SLC39A7
Sequence:
MVKLLVAKILCMVGVFFFMLLGSLLPVKIIETDFEKAHRSKKILSLCNTFGGGVFLATCFNALLPAVREKLQKVLSLGHISTDYPLAETILLLGFFMTVFLEQLILTFRKEKPSFIDLETFNAGSDVGSDSEYESPFMGGARGHALYVEPHGHGPSLSVQGLSRASPVRLLSLAFALSAHSVFEGLALGLQEEGEKVVSLFVGVAVHETLVAVALGISMARSAMPLRDAAKLAVTVSAMIPLGIGLGLGIESAQGVPGSVASVLLQGLAGGTFLFITFLEILAKELEEKSDRLLKVLFLVLGYTVLAGMVFLKW
Protein: Fanconi anemia core complex-associated protein 100 (Fanconi anemia-associated protein of 100 kDa) (Q0VG06)
Organism: Homo sapiens (Human)
Function: Plays a role in Fanconi anemia-associated DNA damage response network. Regulates FANCD2 monoubiquitination and the stability of the FA core complex. Induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed.
Subcellular location: Nucleus {ECO:0000269|PubMed:17396147}.
Interaction partners:
- Fanconi anemia group E protein
- Centromere protein S
- Centromere protein X
- Fanconi anemia group F protein
- Fanconi anemia core complex-associated protein 24
- Fanconi anemia group B protein
- Fanconi anemia group M protein
- Fanconi anemia group C protein
- E3 ubiquitin-protein ligase FANCL
- FA core complex associated protein 20
Sequence:
MAGAAPRVRYLAGFCCPLGGLAAGKPRVLCHEAEVFLSTGSELVYVYDQEGGLLTAAFRFPDQVWHLELLAPRRLLYALCARRGLYCLSLDHPGRSRSTSQDDRDSEDGDQPSPVIPVDPDACILPDAALCAFTLLDSVLVTLVQGPARWKMQLFEQPCPGEDPRPGGQIGEVELSSYTPPAGVPGKPAAPHFLPVLCSVSPSGSRVPHDLLGGSGGFTLEDALFGLLFGADATLLQSPVVLCGLPDGQLCCVILKALVTSRSAPGDPNALVKILHHLEEPVIFIGALKTEPQAAEAAENFLPDEDVHCDCLVAFGHHGRMLAIKASWDESGKLVPELREYCLPGPVLCAACGGGGRVYHSTPSDLCVVDLSRGSTPLGPEQPEEGPGGLPPMLCPASLNICSVVSLSASPRTHEGGTKLLALSAKGRLMTCSLDLDSEMPGPARMTTESAGQKIKELLSGIGNISERVSFLKKAVDQRNKALTSLNEAMNVSCALLSSGTGPRPISCTTSTTWSRLQTQDVLMATCVLENSSSFSLDQGWTLCIQVLTSSCALDLDSACSAITYTIPVDQLGPGARREVTLPLGPGENGGLDLPVTVSCTLFYSLREVVGGALAPSDSEDPFLDECPSDVLPEQEGVCLPLSRHTVDMLQCLRFPGLAPPHTRAPSPLGPTRDPVATFLETCREPGSQPAGPASLRAEYLPPSVASIKVSAELLRAALKDGHSGVPLCCATLQWLLAENAAVDVVRARALSSIQGVAPDGANVHLIVREVAMTDLCPAGPIQAVEIQVESSSLADICRAHHAVVGRMQTMVTEQATQGSSAPDLRVQYLRQIHANHETLLREVQTLRDRLCTEDEASSCATAQRLLQVYRQLRHPSLILL
Protein: Transcription factor UNE12 (Basic helix-loop-helix protein 59) (AtbHLH59) (bHLH 59) (Protein UNFERTILIZED EMBRYO SAC 12) (Transcription factor EN 93) (bHLH transcription factor bHLH059) (O22768)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for ovule fertilization.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Bromodomain testis-specific protein
- Mediator of RNA polymerase II transcription subunit 7b
- Uncharacterized Rho GTPase-activating protein At5g61530
- Transcription factor SRM1
- SPX domain-containing membrane protein At4g11810
- Phosphomannomutase
- At1g20770
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 8
Sequence:
MASNNPHDNLSDQTPSDDFFEQILGLPNFSASSAAGLSGVDGGLGGGAPPMMLQLGSGEEGSHMGGLGGSGPTGFHNQMFPLGLSLDQGKGPGFLRPEGGHGSGKRFSDDVVDNRCSSMKPVFHGQPMQQPPPSAPHQPTSIRPRVRARRGQATDPHSIAERLRRERIAERIRALQELVPTVNKTDRAAMIDEIVDYVKFLRLQVKVLSMSRLGGAGAVAPLVTDMPLSSSVEDETGEGGRTPQPAWEKWSNDGTERQVAKLMEENVGAAMQLLQSKALCMMPISLAMAIYHSQPPDTSSVVKPENNPPQ
Protein: Cadherin-4 (A0A087WX99)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
Interaction partners:
Sequence:
MPKSTGMLHGGRENAGVKFSSCVGTKGTQYETNSMDFKPQKGKKVVALDPSPPPKDTLLPWPQHQNANGLRRRKRDWVIPPINVPENSRGPFPQQLVRIRSDKDNDIPIRYSITGVGADQPPMEVFSIDSMSGRMYVTRPMDREEHASYHLRAHAVDMNGNKVENPIDLYIYVIDMNDNRPEFINQVYNGSVDEGSKPGTYVMTVTANDADDSTTANGMVRYRIVTQTPQSPSQNMFTINSETGDIVTVAAGLDREKVQQYTVIVQATDMEGNLNYGLSNTATAIITVTDVNDNPPEFTASTFAGEVPENRVETVVANLTVMDRDQPHSPNWNAVYRIISGDPSGHFSVRTDPVTNEGMVTVVKAVDYELNRAFMLTVMVSNQAPLASGIQMSFQSTAGVTISIMDINEAPYFPSNHKLIRLEEGVPPGTVLTTFSAVDPDRFMQQAVRYSKLSDPASWLHINATNGQITTAAVLDRESLYTKNNVYEATFLAADNGIPPASGTGTLQIYLIDINDNAPELLPKEAQICEKPNLNAINITAADADVDPNIGPYVFELPFVPAAVRKNWTITRLNGDYAQLSLRILYLEAGMYDVPIIVTDSGNPPLSNTSIIKVKVCPCDDNGDCTTIGAVAAAGLGTGAIVAILICILILLTMVLLFVMWMKRREKERHTKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPEAMGHVPSKAPGVRRVDERPVGAEPQYPIRPMVPHPGDIGDFINEGLRAADNDPTAPPYDSLLVFDYEGSGSTAGSVSSLNSSSSGDQDYDYLNDWGPRFKKLADMYGGGEED
Protein: Charged multivesicular body protein 2B (A0A8I5ZYY9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MMGTRFLIYLFTTQVHKMFPEFPELEIKKMAKIGNKEACRVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
Protein: Mediator of RNA polymerase II transcription subunit 22 (Mediator complex subunit 22) (Surfeit locus protein 5) (Surf-5) (Q62276)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 14
Sequence:
MAQQRALPQSKETLLQSYNKRLKDDIKSIMDNFTEIIKTAKIEDETQVSRATQGEQDNYEMHVRAANIVRAGESLMKLVSDLKQFLILNDFPSVNEAIDQRNQQLRALQEECDRKLITLRDEVSIDLYELEEEYYSSSSSLCEANDLPLCEAYWRLDLDADSADGLSAPLLASPETGAGPLQSAAPVHSHGGGPGPTEHT
Protein: Avian reticuloendotheliosis viral (v-rel) oncogene related B (Relb protein) (Q8K220)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPSRRAARESAPELGALGSSDLSSLSLTVSRTTEIIDEYIKENGFGLDGTQLSEMPRLVPRGPASLSSVTLGPAAPPPPATPSWSCTLGRLVSPGPCPRPYLVITEQPKQRGMRFRYECEGRSAGSILGESSTEASKTLPAIELRDCGGLREVEVTACLVWKDWPHRVHPHSLVGKDCTDGVCRVRLRPHVSPRHSFNNLGIQCVRKKEIEAAIERKIQLGIDPYNAGSLKNHQEVDMNVVRICFQASYRDQQGHLHRMDPILSEPVYDKKSTNTSELRICRINKESGPCTGGEELYLLCDKVQKEDISVVFSTASWEGRADFSQADVHRQIAIVFKTPPYEDLEISEPVTVNVFLQRLTDGVCSEPLPFTYLPRDHDSYGVDKKRKRGLPDVLGELSSSDPHGIESKRRKKKPVFLDHFLPGHSSGLFLPPSALQPADSDFFPASISLPGLEPPGGPDLLDDGFAYDPSAPTLFTMLDLLPPAPPLASAVVGSGGAGATVVESSGPEPLSLDSFAAPGPGDVGTASLVGSNMFPNQYREAAFGGGLLSPGPEAT
Protein: Pectinesterase inhibitor 2 (Pectin methylesterase inhibitor 2) (AtPMEI2) (Q9LUV1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inhibits pectin methylesterase (PME) from flowers, siliques and pollen tube.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:Q9LNF2}.
Interaction partners:
- Pectinesterase PPME1
- At1g10770
- Pectinesterase inhibitor 3
- Pectinesterase inhibitor 5
- Pectinesterase inhibitor 12
- Pectinesterase inhibitor 10
- Pectinesterase inhibitor 4
- Pectinesterase inhibitor 11
- Pectinesterase inhibitor 6
- Pectinesterase 5
Sequence:
MAAYLTNRVLMSSLMFFVMTGSLNAQVADIKAICGKAKNQSFCTSYMKSNPKTSGADLQTLANITFGSAQTSASEGFRKIQSLVKTATNPTMKKAYTSCVQHYKSAISSLNDAKQSLASGDGKGLNIKVSAAMEGPSTCEQDMADFKVDPSAVKNSGDFQNICGIVLVISNMM
Protein: Bacterial non-heme ferritin (EC 1.16.3.2) (Ferritin-1) (P0A998)
Organism: Escherichia coli (strain K12)
Function: Iron-storage protein.
Subcellular location: Cytoplasm.
Interaction partners:
- Bacterioferritin
- Superoxide dismutase
- Bacterioferritin-associated ferredoxin
Sequence:
MLKPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESPFAEYSSLDELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIDKLSLAGKSGEGLYFIDKELSTLDTQN
Protein: Platelet endothelial cell adhesion molecule (PECAM-1) (CD antigen CD31) (P51866)
Organism: Bos taurus (Bovine)
Function: Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-689 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions. Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils. Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal. Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Induces susceptibility to atherosclerosis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P16284}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16284}. Membrane raft {ECO:0000250|UniProtKB:P16284}. Cell junction {ECO:0000250|UniProtKB:P16284}. Note=Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells. Cell surface expression on neutrophils is down-regulated upon fMLP or CXCL8/IL8-mediated stimulation. {ECO:0000250|UniProtKB:P16284}.
Interaction partners:
- Cadherin-5
- Catenin beta-1
- Tyrosine-protein phosphatase non-receptor type
- Vascular endothelial growth factor receptor 2
- CD177 molecule
- CD34 molecule
- Tyrosine-protein phosphatase non-receptor type
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- von Willebrand factor
- CD44 antigen
Sequence:
MQLRWTQRGMMWLGALLTLLLCSSLKGQENSFTINSIHMQILPHSTVQNGENLTLQCLVDVSTTSRVKPLHQVLFYKDDVLLHNVSSRRNTESYLIPHVRVCDSGRYKCNVILNNKEKTTPEYEVWVKGVSDPRVTLDKKEVIEGGVVVVNCSVPEEKAPVHFTIEKFELNIRGAKKKREKTSQNQNFVTLEFTVEEQDRTIRFQCQAKIFSGSNVESSRPIQSDLVTVRESFSNPKFHIIPEGKVMEGDDLQVKCTVQVTHQAQSFPEIIIQKDREIVAHNSLSSEAVYSVMATTEHNGNYTCKVEASRISKVSSVVVNVTELFSKPKLESSATHLDQGEDLNLLCSIPGAPPANFTIQKGGMTVSQTQNFTKRVSEWDSGLYTCVAGVGRVFKRSNTVQITVCEMLSKPSIFHDSRSEVIKGQTIEVSCQSVNGTAPIFYQLSNTSKPVANQSVGSNKPAIFRVKPTKDVEYCCSADNCHSHSKMFSEVLRVKVIAPVDEAQLVVLKGEVEPGEPIVFYCSVNEGSFPITYKFYKEKESKPFYQDTINATQIMWHKTTASKEYEGQYYCTASNRANLSKHVIQSNTLTVRVYLPLEKGLIAVVVIGVIIVTLVLGAKCYFLKKAKAKQMPVEMSRPAVPLLNSNNEKTLSDAGTEADRHYGYNEDVGNHAMKPLNENKEPLTLDVEYTEVEVTSPEPHQGLGTKGTETETVYSEIRKADPDFVENRYSRTEGSLDGS
Protein: Arylsulfatase F (ASF) (EC 3.1.6.1) (P54793)
Organism: Homo sapiens (Human)
Function: Exhibits arylsulfatase activity towards the artificial substrate 4-methylumbelliferyl sulfate.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- CD99 antigen
- Glycoprotein Xg
- Sex comb on midleg-like protein 2
- Formylglycine-generating enzyme
- Glycogenin-2
- cAMP-dependent protein kinase catalytic subunit PRKX
Sequence:
MRPRRPLVFMSLVCALLNTCQAHRVHDDKPNIVLIMVDDLGIGDLGCYGNDTMRTPHIDRLAREGVRLTQHISAASLCSPSRSAFLTGRYPIRSGMVSSGNRRVIQNLAVPAGLPLNETTLAALLKKQGYSTGLIGKWHQGLNCDSRSDQCHHPYNYGFDYYYGMPFTLVDSCWPDPSRNTELAFESQLWLCVQLVAIAILTLTFGKLSGWVSVPWLLIFSMILFIFLLGYAWFSSHTSPLYWDCLLMRGHEITEQPMKAERAGSIMVKEAISFLERHSKETFLLFFSFLHVHTPLPTTDDFTGTSKHGLYGDNVEEMDSMVGKILDAIDDFGLRNNTLVYFTSDHGGHLEARRGHAQLGGWNGIYKGGKGMGGWEGGIRVPGIVRWPGKVPAGRLIKEPTSLMDILPTVASVSGGSLPQDRVIDGRDLMPLLQGNVRHSEHEFLFHYCGSYLHAVRWIPKDDSGSVWKAHYVTPVFQPPASGGCYVTSLCRCFGEQVTYHNPPLLFDLSRDPSESTPLTPATEPLHDFVIKKVANALKEHQETIVPVTYQLSELNQGRTWLKPCCGVFPFCLCDKEEEVSQPRGPNEKR
Protein: Eukaryotic aspartyl protease family protein (Nucellin, putative) (Q9C6Y5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Eukaryotic aspartyl protease family protein
- Phosphatidylinositol/phosphatidylcholine transfer protein SFH11
- Aspartic proteinase A3
- Aspartic proteinase A2
- E3 ubiquitin-protein ligase RDUF2
- Eukaryotic aspartyl protease family protein
- E3 ubiquitin-protein ligase RDUF1
- Aspartic proteinase A1
Sequence:
MISRFSLLLFLFLVIVPLSKSSIFKTFIKSSPSSVVFPLSGNVFPLGYYSVLMQIGSPPKAFQFDIDTGSDLTWVQCDAPCSGCTLPPNLQYKPKGNIIPCSNPICTALHWPNKPHCPNPQEQCDYEVKYADQGSSMGALVTDQFPLKLVNGSFMQPPVAFGCGYDQSYPSAHPPPATAGVLGLGRGKIGLLTQLVSAGLTRNVVGHCLSSKGGGFLFFGDNLVPSIGVAWTPLLSQDNHYTTGPADLLFNGKPTGLKGLKLIFDTGSSYTYFNSKAYQTIINLIGNDLKVSPLKVAKEDKTLPICWKGAKPFKSVLEVKNFFKTITINFTNGRRNTQLYLAPELYLIVSKTGNVCLGLLNGSEVGLQNSNVIGDISMQGLMMIYDNEKQQLGWVSSDCNKLPKT
Protein: V-type proton ATPase proteolipid subunit (D6XKU7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane {ECO:0000256|RuleBase:RU363060}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363060}.
Interaction partners:
- H
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit
- V-type proton ATPase subunit a
- V-type ATPase, C subunit, putative
- Vacuolar ATP synthase subunit D, putative
- ATP synthase, putative
- V-type proton ATPase subunit F
- ATP synthase alpha chain
- V-type proton ATPase subunit H
Sequence:
MLSDDTCQPEAVLFGMLGAAASLALSNIGAAYGTAKSGVAVAHLGIVEPSRVMRGIVPVVMAGILGIYGLIVSVIISNNLKLSGYAMFSGFMHLGAGLAAGFASLASGYAIGIVGDICCFAYAKTEKIFVPMILMLIFAEALGLYGLIMALLMNNRATSYTGGCS