wanglab/gogpt-training-data huggingface dataset:
Protein: CheY1 (Response regulator) (Q52879)
Organism: Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
- Chemotaxis protein CheA
- CheY2
- STAS domain-containing protein
- Chemotaxis protein CheW
- Flagellar motor switch protein FliN
- Chemotaxis protein methyltransferase
- Chemotaxis protein CheD
- Methyl-accepting-chemotaxis-protein
- Chemotaxis protein
- Response regulator
Sequence:
MKKRVLTVDDSRTIRNMLLVTLNNAGFETIQAEDGVEGLEKLDTANPDVIVTDINMPRLDGFGFIEGVRKNDRYRAVPILVLTTESDAEKKNRARQAGATGWIVKPFDPTKLIDAIERVTA
Protein: ABC transporter B family member 20 (ABC transporter ABCB.20) (AtABCB20) (Multidrug resistance protein 14) (P-glycoprotein 20) (Q9M3B9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- ABC transporter E family member 2
Sequence:
MMISRGLFGWSPPHMQPLTPVSEVSEPPESPSPYLDPGAESGGGTGTAAALAEADEEMDDQDELEPPPAAVPFSQLFACADRFDWVLMIVGSVAAAAHGTALIVYLHYFAKIVDVLAFSNDSSQQRSEHQFDRLVQLSLTIVYIAGGVFISGWIEVSCWILTGERQTAVIRSKYVQVLLNQDMSFFDTYGNNGDIVSQVLSDVLLIQSALSEKVGNYIHNMATFISGLVIGFVNCWEIALITLATGPFIVAAGGISNIFLHRLAENIQDAYAEAAGIAEQAISYIRTLYAFTNETLAKYSYATSLQATLRYGILISLVQGLGLGFTYGLAICSCALQLWIGRFFVHNGRANGGEIIAALFAVILSGLGLNQAATNFYSFDQGRIAAYRLFEMITRSSSVANQEGAVLASVQGNIEFRNVYFSYLSRPEIPILSGFYLTVPAKKAVALVGRNGSGKSSIIPLMERFYDPTLGEVLLDGENIKNLKLEWLRSQIGLVTQEPALLSLSIRENIAYGRDATLDQIEEAAKNAHAHTFISSLEKGYETQVGRAGLAMTEEQKIKLSIARAVLLNPTILLLDEVTGGLDFEAERIVQEALDLLMLGRSTIIIARRLSLIKNADYIAVMEEGQLVEMGTHDELINLGGLYAELLKCEEATKLPRRMPVRNYKESAVFEVERDSSAGCGVQEPSSPKMIKSPSLQRGSGVFRPQELCFDTEESPKAHSPASEKTGEDGMSLDCADKEPTIKRQDSFEMRLPHLPKVDVQCPQQKSNGSEPESPVSPLLTSDPKNERSHSQTFSRPLSSPDDTKANGKASKDAQHKESPSFWRLAQLSFPEWLYAVLGSLGAAIFGSFNPLLAYVIALVVTEYYKSKGGHLREEVDKWCLIIACMGIVTVVANFLQHFYFGIMGEKMTERVRRMMFSAMLRNEVGWFDDEENSPDTLSMRLANDATFVRAAFSNRLSIFIQDSFAVIVALLIGLLLGWRLALVALATLPILTLSAIAQKLWLAGFSKGIQEMHRKASLVLEDAVRNIYTVVAFCAGNKVMELYRMQLQRILRQSYLHGMAIGFAFGFSQFLLFACNALLLWCTALSVNRGYMKLSTAITEYMVFSFATFALVEPFGLAPYILKRRKSLISVFEIVDRVPTIEPDDNSALKPPNVYGSIELKNVDFCYPTRPEILVLSNFSLKISGGQTVAVVGVSGSGKSTIISLVERYYDPVAGQVLLDGRDLKLYNLRWLRSHMGLVQQEPIIFSTTIRENIIYARHNASEAEMKEAARIANAHHFISSLPHGYDTHIGMRGVELTPGQKQRIAIARVVLKNAPIILIDEASSSIESESSRVVQEALDTLIMGNKTTILIAHRAAMMRHVDNIVVLNGGRIVEEGTHDSLAAKNGLYVRLMQPHFGKGLRQHRLI
Protein: V-set and immunoglobulin domain-containing protein 2 (Cortical thymocyte-like protein) (CT-like protein) (Q96IQ7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Sterol 26-hydroxylase, mitochondrial
- Conserved oligomeric Golgi complex subunit 8
- Heat shock factor protein 4
- Conserved oligomeric Golgi complex subunit 3
Sequence:
MAELPGPFLCGALLGFLCLSGLAVEVKVPTEPLSTPLGKTAELTCTYSTSVGDSFALEWSFVQPGKPISESHPILYFTNGHLYPTGSKSKRVSLLQNPPTVGVATLKLTDVHPSDTGTYLCQVNNPPDFYTNGLGLINLTVLVPPSNPLCSQSGQTSVGGSTALRCSSSEGAPKPVYNWVRLGTFPTPSPGSMVQDEVSGQLILTNLSLTSSGTYRCVATNQMGSASCELTLSVTEPSQGRVAGALIGVLLGVLLLSVAAFCLVRFQKERGKKPKETYGGSDLREDAIAPGISEHTCMRADSSKGFLERPSSASTVTTTKSKLPMVV
Protein: Keratin, type I cytoskeletal 12 (Cytokeratin-12) (CK-12) (Keratin-12) (K12) (Q99456)
Organism: Homo sapiens (Human)
Function: Involved in corneal epithelium organization, integrity and corneal keratin expression.
Interaction partners:
- Paired box protein Pax-6
Sequence:
MDLSNNTMSLSVRTPGLSRRLSSQSVIGRPRGMSASSVGSGYGGSAFGFGASCGGGFSAASMFGSSSGFGGGSGSSMAGGLGAGYGRALGGGSFGGLGMGFGGSPGGGSLGILSGNDGGLLSGSEKETMQNLNDRLASYLDKVRALEEANTELENKIREWYETRGTGTADASQSDYSKYYPLIEDLRNKIISASIGNAQLLLQIDNARLAAEDFRMKYENELALRQGVEADINGLRRVLDELTLTRTDLEMQIESLNEELAYMKKNHEDELQSFRVGGPGEVSVEMDAAPGVDLTRLLNDMRAQYETIAEQNRKDAEAWFIEKSGELRKEISTNTEQLQSSKSEVTDLRRAFQNLEIELQSQLAMKKSLEDSLAEAEGDYCAQLSQVQQLISNLEAQLLQVRADAERQNVDHQRLLNVKARLELEIETYRRLLDGEAQGDGLEESLFVTDSKSQAQSTDSSKDPTKTRKIKTVVQEMVNGEVVSSQVQEIEELM
Protein: long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (A1Z7H3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDSFWVQSAIGAIKAIAFVYDIITLPVYLVLQKPWKRRQDSRRVKAKIVRNDDNELTYRTTDPPRDVHVKMLQENIDTLEKVFNYVAKTYTSKRCLGTRQILSEEDEVQQNGRVFKKYNLGDYKWKTFTEAERTAANFGRGLRELGQKPRENIVIFAETRAEWMIAAHGCFKQAMPIVTVYATLGDDGVAHCITETEVTTVITSHDLLPKFKTLLDKCPLVKTIIYIEDQLQKTETTGFKEGVKILPFNQVVKTGQDSKFEHVPPKGDDIAIIMYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLIDTSSKIKRGCKGDATVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFLYQYKVKWVQRGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPNQNHLEELAQKHGLGDKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQHDINRMYAS
Protein: Pericentriolar material 1 (H0YBA1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATGGGPFEDGMNDQDLPNWSNENVDDRLNNMDWGAQQKKANRSSEKNKKKFGVESDKRVTNDISPESSPGVGRRRTKTPHTFPHSRYMSQMSVPEQAELEKLKQRINFSDLDQRSIGSDSQGRATAANNKRQLSENRKPFNFLPMQINTNKSKDASTNPPNRETIGSAQCKELFASALSNDLLQNCQVSEEDGRGEPAMESSQIVSRLVQIRDYITKASSMREDLVEKNERSANVERLTHLIDHLKEQEKSYMKFLKKILARDPQQEPMEEIENLKKQHDLLKRMLQQQEQLRALQGRQAALLALQHKAEQAIAVMDDSVVAETAGSLSGVSITSELNEELNDLIQRFHNQLRDSQPPAVPDNRRQAESLSLTREVSQSRKPSASERLPDEKVELFSKMRVLQEKKQKMDKLLGELHTLRDQHLNNSSSSPQRSVDQRSTSAPSASVGLAPVVNGESNSLTSSVPYPTASLVSQNESENEGHLNPSEKLQKLNEVRKRLNELRELVHYYEQTSDMMTDAVNENRKDEETEESEYDSEHENSEPVTNIRNPQVASTWNEVNSHSNAQCVSNNRDGRTVNSNCEINNRSAANIRALNMPPSLDCRYNREGEQEIHVAQGEDDEEEEEEAEEEGVSGASLSSHRSSLVDEHPEDAEFEQKINRLMAAKQKLRQLQDLVAMVQDDDAAQGVISASASNLDDFYPAEEDTKQNSNNTRGNANKTQKDTGVNEKAREKFYEAKLQQQQRELKQLQEERKKLIDIQEKIQALQTACPDLQLSAASVGNCPTKKYMPAVTSTPTVNQHETSTSKSVFEPEDSSIVDNELWSEMRRHEMLREELRQRRKQLEALMAEHQRRQGLAETASPVAVSLRSDGSENLCTPQQSRTEKTMATWGGSTQCALDEEGDEDGYLSEGIVRTDEEEEEEQDASSNDNFSVCPSNSVNHNSYNGKETKNRWKNNCPFSADENYRPLAKTRQQNISMQRQENLRWVSELSYVEEKEQWQEQINQLKKQLDFSVSICQTLMQDQQTLSCLLQTLLTGPYSVMPSNVASPQVHFIMHQLNQCYTQLTWQQNNVQRLKQMLNELMRQQNQHPEKPGGKERGSSASHPPSPSLFCPFSFPTQPVNLFNIPGFTNFSSFAPGMNFSPLFPSNFGDFSQNISTPSEQQQPLAQNSSGKTEYMAFPKPFESSSSIGAEKPRNKKLPEEEVESSRTPWLYEQEGEVEKPFIKTGFSVSVEKSTSSNRKNQLDTNGRRRQFDEESLESFSSMPDPVDPTTVTKTFKTRKASAQASLASKDKTPKSKSKKRNSTQLKSRVKNIRYESASMSSTCEPCKSRNRHSAQTEEPVQAKVFSRKNHEQLEKIIKCNRSTEISSAHARRILQQSNRNACNEAPETGSDFSMFEALRDTIYSEVATLISQNESRPHFLIELFHELQLLNTDYLRQRALYALQDIVSRHISESHEKGENVKSVNSGTWIASNSELTPSESLATTDDETFEKNFERETHKISEQNDADNASVLSVSSNFEPFATDDLGNTVIHLDQALARMREYERMKTEAESNSNMRCTCRIIEDGDGAGAGTTVNNLEETPVIENRSSQQPVSEVSTIPCPRIDTQQLDRQIKAIMKEVIPFLKEHMDEVCSSQLLTSVRRMVLTLTQQNDESKEFVKFFHKQLGSILQDSLAKFAGRKLKDCGEDLLVEISEVLFNELAFFKLMQDLDNNSITVKQRCKRKIEATGVIQSCAKEAKRILEDHGSPAGEIDDEDKDKDETETVKQTQTSEVYDGPKNVRSDISDQEEDEESEGCPVSINLSKAETQALTNYGSGEDENEDEEMEEFEEGPVDVQTSLQANTEATEENEHDEQVLQRDFKKTAESKNVPLEREATSKNDQNNCPVKPCYLNILEDEQPLNSAAHKESPPTVDSTQQPNPLPLRLPEMEPLVPRVKEVKSAQETPESSLAGSPDTESPVLVNDYEAESGNISQKSDEEDFVKVEDLPLKLTIYSEADLRKKMVEEEQKNHLSGEICEMQTEELAGNSETLKEPETVGAQSI
Protein: CTLH domain-containing protein (Q9UAU3)
Organism: Caenorhabditis elegans
Interaction partners:
- B30.2/SPRY domain-containing protein
- CTLH domain-containing protein
- RING-Gid-type domain-containing protein
- E3 ubiquitin-protein transferase MAEA
- Fructose-1,6-bisphosphatase isozyme 2
Sequence:
MEHRDDDFEFGHQFGGDEEEEEEEEAIDVDSPDELDVDAEPDDDSDMEVYHMETNGAANGNGRQVIGETGDEEEDDDYDEEDAMTWDSMSTISEVEVEKDDDEWYPLMKRDNVFPNFALPTTTRAAFRIGPQPIASADPSSTPGSSEHHSDTEDVEFNDYKEVMRPDPTREELQQLVIDHFLHHGYSEVIETFSKEVNIVVPKKDIDNMNARNEVRRLICVGEMESAIEKMTTLCPTILEDDEINFIVRKQHLIEMVRQKLTKEPVEYFRAHLMKNGQRPCDEKMDIIERIFTMLVFNLEDDVEFNVYFQQSEREQTAKEVNSALLAMNGKLKSSRLDLLAKTIAFTGCSQMRSSSPSRKHATIAEFSEEHYSKPYGLAAETSSAFRGEVDLTQDMR
Protein: Collagen type XVIII, alpha (I) chain (Q9WUW5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
VLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRSSVPIVNLKDEVLSPSWDTLFSGSQGQLHSGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTEATGVTGQASSLLSGRLLEQKAESCHNSYIVLCIENSFM
Protein: Trans-enoyl reductase iccB (EC 1.-.-.-) (Ilicicolin H biosynthesis cluster protein B) (A0A482N9T9)
Organism: Talaromyces variabilis (Penicillium variabile)
Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IccB collaborates with the hybrid PKS-NRPS synthetase iccA to assemble the backbone of ilicicolin H. The PKS portion of iccA and trans-acting enoyl reductase iccB work together to construct an octaketide, and two methyl groups are introduced by the MT domain of iccA during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the iliA C domain, and the resulting PKS-NRPS hybrid is offloaded by the iliA RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB since iccA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iccD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. IccA to iccE are sufficient for ilicicolin H biosynthesis and the roles of the remaining enzymes, iccF, iccG and iccH within the pathway have still to be determined (Probable).
Interaction partners:
Sequence:
MDATLPSIHTALKILGPNNVSVSENTALPVIQPLDILVRVACISINHVDAKSADMSPSPGATSGTDFSGVVVAIGSDVPKESFRSTNGMKPVQIGDRVFGGVFGNNPLRRDNGAFAEYVAVPARLVWHIPGGMDFSTASTLGAAVATVGLSLFQYMQLPMPTTTSTASPDNGPFVLVYGGGTATGAMAIQVLKIAGFRPITTCSSASAGHATELGATATFDYRSPTCGAELREHTGDTLTLALDCITDTASMNICYEALGSSGGRYVALDSFPLRAHTRRSVVPDWVCTYSQFGHPIAWAAPYNLEARPEDLLTAEAWYVVAQKLIDQGLITPHPKEERLGGLAAIGEGMEAVRRGQIKGKKLVYPISNELCAAA
Protein: F-actin-capping protein subunit alpha (Q10434)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15743909, ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:15743909}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15743909}. Note=Localizes to the actomyosin contractile ring. Localizes to cell tips during interphase. {ECO:0000269|PubMed:15743909}.
Interaction partners:
- F-actin-capping protein subunit beta
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Fimbrin
- Actin-like protein arp10
- Centractin
- Uncharacterized WD repeat-containing protein C9G1.05
- Twinfilin
- Myosin-51
Sequence:
MEKEAIYKLIRESPPGEVNQVVHDIRDIGLSDEEAIHEQLKLYHEDYNSSVSISDDEKVIISADNRLEGNRYYDQVLQKSFTINYETMEAENVEDYTEAIKIPDEIVKQIKKVASDHYLSDVTFGIIKKSDEVESFTIVLVSSKYNPKNYWNGSWRCICNYNVSEKKLEGRSHIRVHYYEDGNVWLDASRPISATVEETSKLYEVLAQVENGIQQSFNVELSSLNDKKFKELRRQLPVTRQKINWENVSGIRMRNT
Protein: Small ribosomal subunit protein mS37 (28S ribosomal protein S37, mitochondrial) (MRP-S37) (Coiled-coil-helix-coiled-coil-helix domain-containing protein 1) (Nuclear protein C2360) (Q96BP2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23908630}. Nucleus {ECO:0000269|PubMed:15177562}.
Interaction partners:
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein bS21m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS3m
Sequence:
MATPSLRGRLARFGNPRKPVLKPNKPLILANRVGERRREKGEATCITEMSVMMACWKQNEFRDDACRKEIQGFLDCAARAQEARKMRSIQETLGESGSLLPNKLNKLLQRFPNKPYLS
Protein: Disease resistance protein (TIR-NBS class) (Putative disease resistance protein) (Q4PT31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MYSSSSSSSATPQKFDVFLSFRGKDTRRTFISFLYKELIEMGIRTFKDDVELQSGRRIASDLLAAIENSKIAVVIISKNYSASPWCLQELVMIMDVEKKGSIIVMPIFYNVEPAHVRRQIEQVAKQFRKHEGRENYETVVSWRQALTNLASISGHCSRDCEDDSKLLDEITKRISDMLFSVTPPSESINNQLGFDARMKELYPLLDLDSNEGVRVVGIWARGGNGRSALARYVYQKIFKKFQSHCFLENVKGIPHDCQMSNLRDEFLIRIQGGYSRMKTSGLIKKRLMSQKVLLVANNVDKLEQLDALAEYFNCFGPGSIVLITTQDKQLLVAFGIKVVYEVECLRCFEVRQLFRQIGFRERDLNVGSELSSPISGTESS
Protein: PPFIA binding protein 1 (F5GZP6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKKGKDGEYEELLNSSSISSLLDAQGFSDLEKSPSPTPVMGSPSCDPFNTSVPEEFHTTILQVSIPSLLPATVSMETSEKSKLTPKPETSFEENDGNIILGATVDTQLCDKLLTSSLQKSSSLGNLKKETSDGEKETIQKTSEDRAPAESRPFGTLPPRPPGQDTSMDDNPFGTRKVRSSFGRGFFKIKSNKRTASAPNLAETEKETAEHLDLAGASSRPKDSQRNSPFQIPPPSPDSKKKSRGIMKLFGKLRRSQSTTFNPDDMSEPEFKRGGTRATAGPRLGWSRDLGQSNSDLDMPFAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQALGSEEETNHGKLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRINNFEPNCLRRRPSDENTIAPSEVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLIGAEAQHQKRDAMELPDYVLLTATAKVKPKKLAFSNFGNL
Protein: Large structural phosphoprotein (150 kDa matrix phosphoprotein) (150 kDa phosphoprotein) (pp150) (Basic phosphoprotein) (BPP) (Phosphoprotein UL32) (Tegument protein UL32) (P08318)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Participates in the last steps of viral maturation and release. Associates with nuclear capsids prior to DNA encapsidation and later preserves the integrity of nucleocapsids through secondary envelopment at the assembly compartment. Interacts with host CCNA2 and thereby blocks the onset of lytic gene expression to promote establishment of a quiescent state of infection in undifferentiated cells.
Subcellular location: Virion tegument {ECO:0000269|PubMed:9049366}. Host cytoplasm {ECO:0000269|PubMed:21411515, ECO:0000269|PubMed:9049366}. Host nucleus {ECO:0000269|PubMed:9049366}. Note=Found initially localized in the host nucleus, associated either with the nuclear membrane or with viral assembly regions, and later in the host cytoplasm.
Interaction partners:
Sequence:
MSLQFIGLQRRDVVALVNFLRHLTQKPDVDLEAHPKILKKCGEKRLHRRTVLFNELMLWLGYYRELRFHNPDLSSVLEEFEVRCVAVARRGYTYPFGDRGKARDHLAVLDRTEFDTDVRHDAEIVERALVSAVILAKMSVRETLVTAIGQTEPIAFVHLKDTEVQRIEENLEGVRRNMFCVKPLDLNLDRHANTALVNAVNKLVYTGRLIMNVRRSWEELERKCLARIQERCKLLVKELRMCLSFDSNYCRNILKHAVENGDSADTLLELLIEDFDIYVDSFPQSAHTFLGARSPSLEFDDDANLLSLGGGSAFSSVPKKHVPTQPLDGWSWIASPWKGHKPFRFEAHGSLAPAAEAHAARSAAVGYYDEEEKRRERQKRVDDEVVQREKQQLKAWEERQQNLQQRQQQPPPPARKPSASRRLFGSSADEDDDDDDDEKNIFTPIKKPGTSGKGAASGGGVSSIFSGLLSSGSQKPTSGPLNIPQQQQRHAAFSLVSPQVTKASPGRVRRDSAWDVRPLTETRGDLFSGDEDSDSSDGYPPNRQDPRFTDTLVDITDTETSAKPPVTTAYKFEQPTLTFGAGVNVPAGAGAAILTPTPVNPSTAPAPAPTPTFAGTQTPVNGNSPWAPTAPLPGDMNPANWPRERAWALKNPHLAYNPFRMPTTSTASQNTVSTTPRRPSTPRAAVTQTASRDAADEVWALRDQTAESPVEDSEEEDDDSSDTGSVVSLGHTTPSSDYNNDVISPPSQTPEQSTPSRIRKAKLSSPMTTTSTSQKPVLGKRVATPHASARAQTVTSTPVQGRLEKQVSGTPSTVPATLLQPQPASSKTTSSRNVTSGAGTSSASSARQPSASASVLSPTEDDVVSPATSPLSMLSSASPSPAKSAPPSPVKGRGSRVGVPSLKPTLGGKAVVGRPPSVPVSGSAPGRLSGSSRAASTTPTYPAVTTVYPPSSTAKSSVSNAPPVASPSILKPGASAALQSRRSTGTAAVGSPVKSTTGMKTVAFDLSSPQKSGTGPQPGSAGMGGAKTPSDAVQNILQKIEKIKNTEE
Protein: Carboxypeptidase Y homolog A (EC 3.4.16.5) (Q2TYA1)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity).
Subcellular location: Vacuole {ECO:0000269|PubMed:12223187, ECO:0000269|PubMed:16085884, ECO:0000269|PubMed:20622126}. Note=Requires vps10 for correct vacuolar localization.
Interaction partners:
- Vacuolar protein sorting/targeting protein 10
Sequence:
MRVLPATLLVGAASAAVPPLQQVLGRPEEGMSFSKPLHAFQEQLKTLSEDARKLWDEVANYFPDSMDHSPIFSLPKKHTRRPDSHWDHIVRGSDVQKIWVNNADGEKEREIDGKLEAYDLRIKKADPSALGIDPNVKQYTGYLDDNGNDKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLTGLFMELGPSSIDENIKPVYNDFSWNSNASVIFLDQPVNVGYSYSGSAVSDTVAAGKDVYALLSLFFKQFPEYAEQDFHIAGESYAGHYIPVFASEILAHKNRNINLKSVLIGNGLTDGLTQYGYYRPMGCGEGGYKAVLDEATCESMDNALPRCRSMIESCYNSESAWVCVPASIYCNNALIGPYQRTGQNVYDVRSKCEDESNLCYKGMGYVSEYLNKAEVREAVGAEVGGYDSCNFDINRNFLFHGDWMKPYHRLVPGLLEQIPVLIYAGDADYICNWLGNKAWTEALEWPGQKEYASAELEDLKIEQNEHTGKKIGQVKSHGNFTFMRLYGGGHMVPMDQPEASLEFFNRWLGGEWF
Protein: Amelogenin, X isoform (Q99217)
Organism: Homo sapiens (Human)
Function: Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:25789606}.
Interaction partners:
- Enamelin
- Ameloblastin
- Putative serine/threonine-protein kinase PRKY
- Testis-specific Y-encoded protein 1
- Amelotin
- Protocadherin 11 Y-linked
- Tuftelin
- F-box-like/WD repeat-containing protein TBL1Y
- cAMP-dependent protein kinase catalytic subunit PRKX
- Matrix metalloproteinase-20
Sequence:
MGTWILFACLLGAAFAMPLPPHPGHPGYINFSYEVLTPLKWYQSIRPPYPSYGYEPMGGWLHHQIIPVLSQQHPPTHTLQPHHHIPVVPAQQPVIPQQPMMPVPGQHSMTPIQHHQPNLPPPAQQPYQPQPVQPQPHQPMQPQPPVHPMQPLPPQPPLPPMFPMQPLPPMLPDLTLEAWPSTDKTKREEVD
Protein: Dynein regulatory complex protein 10 (Flagellar associated protein 84) (A8J0N6)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}.
Interaction partners:
- Dynein regulatory complex protein 8
- Dynein regulatory complex subunit 6
- Dynein regulatory complex subunit 3
- Flagellar-associated protein 59
- Flagellar associated protein
Sequence:
MNSLEAGRVLSVLDEALEGIRLISYVTQDVLDTAEQLRDMLGEDLANALIKHRQLIQSAKSTLNNDQVQASTLELVRLLKKSPSAQRLQVLPYERTYGILQTLQYFEQLRQFAQKRLTTTVEEDSSNREFFEEVRDREERAVAEQEQLKQKLKLQRVELQKAAGTIQVSEDRARGEVSEVQSSTQQSRAAIEGSARAQSEADKSSFQSDLDQVTKELAAARAELARLRQEHKDNEALLRKARKRAEQDVEVQIGEYDADVGAKEEELGKARAEYEEVLRQLQEYNSGWSEMYQERLEYEERERRLADQRFQAALLAVRQNHAARVIQSYWRGFKKAREAAKKKAKKLEKAKAAKKK
Protein: Talin-A (Filopodin) (P0CE95)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Actin-binding protein that may be involved in the control of cell motility and chemotaxis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7698984}. Cytoplasm, cell cortex {ECO:0000269|PubMed:7698984}. Note=Rapidly assembles at the leading edge of cells in response to chemoattractant.
Interaction partners:
Sequence:
MSISLKINIVGANTVKTLRFAPDMCIQECCTHIFEKTNEGGPDHGLYQAHIEGKQSARWLAMEKTLQFYDINSDQQLDYKKKHRPQKFKLLDGTIKTQLVDESQNVSEIVNSICKKMGIKNPEEYSLMNSAGAWLNNTQILSEQGISENDITVLMKKFFFNDANIDRNDPVQLHLLFVQCRDGIIEGKYPTQREESLALSALQCQVQLGDYNPTKHEPGFLTLKDYLPLQWLKSKGVEKDIFKEHKKLVSMTEVNAKYRYVQLCRSLKTYGMTSFDVKIREYGKKKMVDHILGITREQMLLMLTETKEVIMTHPLKHIKRWAATDKSFTLDFGDHETEYLILQTPNPEQISQLIGGYIEIIMKARKDSSKVIEKEDTAMGVEEVMAVKKGSVANSSSYMGYGAGGGGANQLQPSQQIPITDLKSALRATDLLIGELGGFRSSTGATPQNFTRSFTTLTPQQFKHQLISHTNAMAIAAQGLFQDMTTPPPTGGIAAFQQAITKRAQIIMAELNTVGTAAKNAGYFPDMASFSDEIIGVATKLSESMARLLAIGSTIQGTDCDEKSQKAAQTEIFNVQSLVTLMMAACDNEYVTDSSSKLLIECAKNVSAAIADMLVVGNSKVEFIDDELLLGQIQNTLKSTSLTSDELLSTTENLASTSCHPESRKQITNITQSALNQSNALLTAFKSGEIPEQDYNLLNARVSDIIESVNLINYAMDCSEREYKISITSNGVEVGEGEILAGTNLTEEFATVANDLTNAIMTMRSNLKNPDTVMESYKMVAGHANRLITCTKAVASRADTQSQQRLFNSTNAVFESVANLSNHCRSYIKNPEQEAHTFQIVETAGHLQFLTQNMSTDAGKIACITSLRDYSKEMIAQVSSLISTSRTSSQYLPDANGITLLKGAKDVSDALSKLMVGIKKVVLDPKSEATQMELLTLAQKQSLPPMNLVSTCKRFAPKISDPNQKQRLIFSSDAAAQSVQKLMKAGEAYKRICGHIEIEEALEVFDSTIADLETTEIAIAGGFLDAVSGTTREGAAELLMVAIKDLNKVNNELVTDIRVNPARLGDLVKSATESASSVAISAKTLICATTGKQVQTKLMGITKQLMIDMEQLIRASRSVRSNPNDRRSELLLDRRSNDVSISTAALVGSTANVDCKELDEASADISNLLSLKMGSLESILSQPTEEFAFYVEEIASSTKALNAASQQVVAMARNKNLKGLGASAKITASALSTLVSHAQNAIVLTENEATKNAILASTVALGGQIIGLLDFSKARIANYKDPIYDQNLINQAKSVEDHLVKVGRSLGGDGNNTICDEAVDRIIEATRSLDKTILPDTSGLQTNAHLEMLHQQSLLAITQASKKLGSITSNLVNSKNNSDLVGSGSTDAERIIEMIEAAKHVVHCSISTYNPDILLPAKSILDASQMLTANQADVNHVLSHAATIAACTQQLLGITRERASQFNEQDEQQVQVRDGIVKSTQQLAHATSSLARAVKSVTSKEPGAKAMISQSLKDLESAINNLLITSSVPASERGIGIADFNKLMSTCRSVSTASSQLIISASSCSQKPKDIELSSILSENAVLMTNSLKDIIKVTSSMMPGVNFCEEAIEIAQRAISDLSSVALSVAVGSFDSSANNKEGLSHVESQERLVDVTKKIGTGINDLLKASRQSPEAIGISAKALSFIAPSLVNTTKPALATAPDADAQNDLVTESKNVGDSILKLCQASLIASSNPSKETYQIIVNKCVDASEAMSKLVAQISSGVNLYKELDESLDRIRKSVVQTSAKDAPKDSENRGYQEYKEELSNLTKNLALSLKTIVATDGNNLVSISTISKDIANYISDIAHVSSAILATTSDQKIRDSIITSSRQVIVSTGDIVNHIKVNSTDKANSSQAKVNDSYRATNDNITRFLQSLKQGAIGEILSDAAIDQIRKVISDLDGYSLFAAAGQLENDQSSQSTMNEVTKQQHLKNLQKDTITQAKLLIVSSSQLVGSSRGTQEHLGSATTKVANTVSSLVKTAKDIASVLADTTSQQDILSASKALSISSQQMVLATKDAQRFKKDATAFRSLGKSAEAVAEAVGQFLTSVYTAISDAGKGIKELEKSIVQVANYHEKPDTVLSNKDATAEIFAQSARDLAKSSIEIVTSYTSSQDSLVKSSQAVVSNVQSFISNSKGVIALLGNGNDDLKSKVLENVKQTTGDMLALLQCVKDQDKNGSTSIADATRSISDRVHSVVTLSKSLPGGQNIVVEEDNVLEDLEALAEDELSACARSIEEATAKLIAARPQSKSKNGKLDAEGVAATIVDASSAIAKAVAKLVNSAAVAQSKRREDQIASGSVYKADPTWSNGLISAAKGVGAATHRLVEAAMKSATGKAEEEELIATARSVAAATALLVSASRAKSGDDYQSQAAHSHLSTAARQVASATSDLVAAAKAATIFDEQQQEEEQEQFNFTGSKVKELEQQMKILKLEKELETARRQMLNSRKQNYNKN
Protein: Protein argonaute-2 (Q9XVI3)
Organism: Caenorhabditis elegans
Interaction partners:
- Endoribonuclease dcr-1
- DRBM domain-containing protein
Sequence:
MEDQWLLSAIYDDDLVEKLKVRSSTSSRSTSINVPSLENEFLSSSSGSRVSDDLYLHPIEENREPFKLIGKPLPSTTGRFLSLLANHFQITCNGSIIHQYYIRFDPDIPSKKLNRTILRTLQEQNPGLIECPLVFDGIHTVYSTELINVKEVNNSVINVAGVVNTKESPNLFKLYLTHVDSFLLDTKIITGNQDQNQKLRMMHAIDTVFRQTSTGNFHAVLQSFFSIAQNSAIEPSHGLGWGTVNLGVGREVCYGFYQNVVETFDTLTMNLDVATTTFYRPVALVEFLAEILEVPLATVTDGRSLSDVQKKKFNREVAGLKVETRHCSCPRRFRVARCTWKPTENISFHLSETAGNQDSKPLSLVEYYKRRYNIDLTYKHLPCIEVGRTRECILPLELCYVVSGQRCIKKLNEQQIANLIRATSRNATERQNAVMSLQNRLKMDNDVNAVKFGLKVEAQLLKIEGRVLPVPRLLYRSPNLKRQECVTVPNNGTWDMRGKNFYSGIQIREWAIVCFASPEIIGEASMRSFVRNLVNVASEIGMPFLEEHRFCRYAEPDQTVKLLEHLNEQYNLQLVLCIVPGKSVVYGELKRKGELLGLTTQCVRSQNVSKASPHTLSNLCMKINSKLGGINVILSSPPQSLNSEPVLFIGCHLTRSSLASSSDSTSSIAHCDSSIACLVGSMDGHPTQFSPIFRTQPRHQRTIVDMCEMTREAIINFRKSTGFKPHKIIIYRAGIADVTVDEIMQTELRAVRDACAMIEYGFQPGITFIGLDVTHHTRLFAANEKDRVGNSQNVPAGTLVETGITVNNLFEFYLVSHAGIQGTSRPTKYVVMWDDNSIPSADIHEMTYQLCHTQSRCTRSVSIPSPVYYAKLVAQRAKILMADENFDMERFRLCGIGRNDGMSFT
Protein: Dahlein-4.3 (P84266)
Organism: Ranoidea dahlii (Dahl's aquatic frog) (Litoria dahlii)
Function: Has no antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:11555873}.
Interaction partners:
Sequence:
GLWQLIKDKFKDAATGFVTGIQS
Protein: Cyclase-like protein 2 (Q94JT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function redundantly with CYCLASE1 for normal plant growth, development and viability.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q93V74}.
Interaction partners:
- p-hydroxybenzoic acid efflux pump subunit
- Purple acid phosphatase 8
Sequence:
MAVPPLFFLLTLLSLPSLLISAGASNAYPSIPGTAPIDGGFTDELKPIRREVYGNGKIYDISHRYTPEMPSWDSSEGIGRFLWLAASMKNGSLANNSEMKIPTHTGTHVDSPGHVYDKYYDAGFDVDSLDLQVLNGLALLVDVPKDKNITAEVMKSLHIPKGVSRVLFRTLNTDRRLMFKKEFDTSYVGFMKDGAQWLVDNTDIKLVGIDYLSVAAYDDLIPSHLVFLKDRETILVEGLKLDGVKAGLYSVHCLPLRLVGAEGSPIRCILID