wanglab/gogpt-training-data huggingface dataset:
Protein: Golgin subfamily A member 1 (Golgin-97) (Q92805)
Organism: Homo sapiens (Human)
Function: Involved in vesicular trafficking at the Golgi apparatus level. Involved in endosome-to-Golgi trafficking.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10209123, ECO:0000269|PubMed:10209125, ECO:0000269|PubMed:9324025}; Peripheral membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:29084197}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q9CW79}.
Interaction partners:
- Golgin subfamily A member 4
- Ras-related protein Rab-6A
- GRIP and coiled-coil domain-containing protein 1
- Trans-Golgi network integral membrane protein 2
- GRIP and coiled-coil domain-containing protein 2
- Golgin subfamily B member 1
- Vesicle transport through interaction with t-SNAREs homolog 1A
- ADP-ribosylation factor-like protein 1
- Golgin subfamily A member 2
- Syntaxin-6
Sequence:
MFAKLKKKIAEETAVAQRPGGATRIPRSVSKESVASMGADSGDDFASDGSSSREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQEDLLRLRGPLQAEALSVNESHVTSRAMQDPVFQLPTAGRTPNGEVGAMDLTQLQKEKQDLEQQLLEKNKTIKQMQQRMLELRKTLQKELKIRPDNELFEVREKPGPEMANMAPSVTNNTDLTDAREINFEYLKHVVLKFMSCRESEAFHLIKAVSVLLNFSQEEENMLKETLEYKMSWFGSKPAPKGSIRPSISNPRIPWS
Protein: NADP-reducing hydrogenase subunit HndA (EC 1.12.1.3) (Hydrogen dehydrogenase (NADP(+))) (Q46505)
Organism: Solidesulfovibrio fructosivorans (Desulfovibrio fructosivorans)
Function: Catalyzes the reduction of NADP in the presence of molecular H(2) to yield NADPH.
Interaction partners:
Sequence:
MQNSTCQAVGECRVPEHAVLPQPLYREVVQFIESLPQKEGHLVTVLHKAQSVFGYLPIEVQQFVADHMEVPLAQVYGVVSFYTFFTMVPKGKYPISVCMGTACFVKGADKVVHAFKEQLKIDIGDVTPDGRFSIDTLRCVGGCALAPIVMVGEKVYGNVTPGQVKKILAEY
Protein: GM13767p (Q9VPL0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-processing factor 6
- 116 kDa U5 small nuclear ribonucleoprotein component
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Probable ATP-dependent RNA helicase DDX23
- Pre-mRNA-processing factor 17
- Pre-mRNA-processing factor 19
- Cell division cycle 5, isoform A
- Thioredoxin-like protein
- Microfibrillar-associated protein 1
Sequence:
MGTKRPNNSVILAQEAKRSKNDLMAYTNRDKALLESGVRRTSNLQAPIMQLEGHEGEIFTAEFHPEGELLLSSGFDRQIYIWQVYEDCENVMAMSGHSGAVMEAHFTPDGSHIFTCSTDKTLAFWDIATGQRQRRFKGHGNFVNSVQGSRRGQQLLCSGSDDRTIKIWDARKKHAAHTLESPFQVTAVCFGDTGEQVISGGIDNEVKIWDIRKQAVLHHLRGHSDTITGMSLSPEGDFILTNAMDNTLRVWDVRPYAPGERCVKVFQGHQHNFEKNLLRCAWSPGSDKITSGSADRHVYIWDVNTRRILYKLPGHNGSVNAVDFSPKEPLILSGSSDKTLYLGEIDE
Protein: von Willebrand factor A domain-containing protein 1 (J3QQ16)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Serpin H1
- Lumican
- Collagen alpha-1
Sequence:
MRKHRHLPLVAVFSLLLSGIATTHAQQHGVMEVNKRDIVFLVDGSSSLGPSNFNAIRDFVTRVIQRLEIGQDLVQVSVAQYADTVKPEFYLNSYTNKRDAITAVRKMRALNGSALYTGSSLDFVRNNLFTSSAGHRAAEGVPKLLVLITGGKSLDEVSQPAQELKRGSIMALAVGSKAADEDELKEIAFDSSLVFIPAEFRPAPLQNMLPSLMAPLRTLTGTTEESKRDILFLFDGSVNVLGQFPAVRDFLYRIIEELDVKPDGTRVAIAQFSDDVRLESRFSEHQTKAEILNLVKKMKLKTGKALNLGYALDYALRNIFVRSAGSRIEDNVQQFLVLLVAGRSSDAVAGPASSLKQRGVVPFIFQAKNANPSELEQIVLSPAFILAAESLPKIGDLQSQIVSLLKAEQGSGPVSGEKDVVFLIDGSEGVRSGFPLLKDFVQRVVESLDVGPDRVRVALVQYSDRTRPEFYLNSHMDQQGVISAIRRLTLLGGPTPNTGAALEFVLRNILTSSTGSRIAEGVPQLLIVLTAEPSGDDVRGPSVVLKQGGAVPIGIGIGNADISEMQTISFIPDFAVAIPTFRELGTIQQVISERVIQLNREELSSLKPILTPSTGAGVGSKKDVVFLIDGSRNAGPEFQYIRTLIERIVEYLDIGFDTTRVAVIQFSEDSKMEFPLNAHFSKDEVQNAVRRLRPKGGSQVYIGNALEYVLKNIFQRPLGSRIEEGVPQFLVLISSGKSDDEVDDSAVELKQFGVAPLTIARHTDQEELVKISLSPEYVYSVSTFRELPRLEQKLLTPITTLTSQQIHQILASTRYPPSVVESDAADIVFLIDSSDAVKPDGIAHIRDFVSRIVRRLNIGPSKVRIGVVQFSNDVFPEFYLKTHKSQSSVLEAIRRLRFKGGSPLNTGRALEFVARNLFVKSAGSRIEDGVPQHLVLFLGGKSQDDVARHAQVISSSGIVSLGIGDRNIDRTDLQTITNDPRLVFTVREFRELPNIEERVMLSFGPSGATPQPPGVDLPSPSRPEKKKADIVFLLDGSINFRRDSFQEVLRFASEIVDTVYEDGDSIRVGLVQYNSDPTDEFFLRDFSTKRQIIDAINKVVYKGGRHANTRVGIEHLLRNHFVPEAGSRLDERVPQIAFVITGGKSVEDAQDVSLALTQKGVKVFAVGVRNIDSEEVGKIASNSATAFRVGSVQELSELSETVLETLHDAMHETLCPGVTDVSKACNLEVILGFDGSRDQNVFVSQKGLESKVDIILNRISQIQRISCSGNQLPTVRVSVMANTPSGPVEAFDFAEYQPELFEKFRNMRSQRPYVLTADTLKLYQNKFRQSSPDTVKVVIHFTDGADGDMADLYRASEELRQAGAQALILVGLERVANLERLMHLEFGRGFMYDRPLRLNLLDLDYELAEQLDNIAEKACCGVPCKCSGERGDRGPIGSIGPKGISGEDGYRGYPGDEGGPGERGPPGVNGTQGFQGCPGQRGVKGSRGFPGEKGELGEIGLDGLDGEEGDKGLPGSSGEKGSPGRRGDKGPKGDKGERGDVGIRGDPGDSGRDSQQRGPKGETGDIGPMGLPGRDGIPGSPGDPGKDGGSGRRGPAGAKGNRGGPGQPGFEGEQGTRGSQGPPGPIGPPGLIGEQGIPGPRGGGGTAGAPGERGRTGPLGRKGEPGEPGPKGSIGNRGPRGETGDDGRDGVGSEGRRGKKGERGFPGYPGPKGTPGEPGADGPPGPKGIRGRRGNSGPPGATGQKGDPGYPGPSGHKGNRGDSVDQCALIQSIRDKCPCCYGPLECPVFPTELAFALDTSEGVTQDTFSRMREVLLGIVGDLTIAESNCPRGARVAVVTYNNEVTTEIRFADSKKKSALLDSIQNLQVALTSKQQSLETAMSFVARNTFKRVRSGFLMRKVAVFFSNKPTRASPQLREAVLKLSDAGITPLFLTSQEDRQLINALQINNTAVGHALVLPARRDLTDFLKNVLTCHVCLDICNIDPSCGFGSWRPSFRDRRAAGSDVDIDLAFILDSSEATTLFQFNEMKKYIGYVIRQLDLSPDPKASQHFARVAVVQQSTYESVDNASVPPVKVEFSLTDYGAKEKLLDFLSRRMTQLQGTMGLGNAIEYTIENIFESAPNPRDLKIMVLMLTGDMQRQQLEEAQRAILQAKCKGYFFVVLGIGRKVNIKEVYSFASEPNDVFFKFVDKSTELNEEPLMRFGRLLPSFVSSENAFYLPPDLRKQCDWFQGDQPVKNGVKFGHKQINPPHTANSSLTSKVVTTMKPVTTTKPTAIVNLPPAKPAPARPAPAQPVLAKPDPAKPAQARPAPAKPASAKLVPPQPVHVQPAPAQTASVRPAPAKPAPPQPAAAKPVPAKPAVPAQPAPPQPAAAKPVPAKPAVPAQPAPPQPAAAKPVPAKPAVPAQPAAAQPMPAQPVLTKSAAVKPASANKPVAAKPVATNTATATARPALAAKPAAAKPAATRPLAAAIRPVATKPEAPRQQAKPAATKPATTKPLARVSREVQVSEVTENSARLHWERPEPSSSFFYDLTVTSAHDQSLVLRQNLTVTDRVIGGLLAGQLYHVVVVSYLQSQVRAIYQGSFNTKKTQPPPLQAAHRASSSTINLMVNTEPLFLTKTDICKLSRDAGTCVDFKLLWHYDLESKSCKRFWYGGCGGNENRFHSQEECEKMCSPELTV
Protein: 1-aminocyclopropane-1-carboxylate synthase 6 (ACC synthase 6) (EC 4.4.1.14) (S-adenosyl-L-methionine methylthioadenosine-lyase 6) (Q9SAR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene. Involved in bacterial flagellin-induced ethylene production.
Interaction partners:
- Mitogen-activated protein kinase 6
- Mitogen-activated protein kinase 3
- 1-aminocyclopropane-1-carboxylate oxidase 4
- 1-aminocyclopropane-1-carboxylate synthase-like protein 1
- Mitogen-activated protein kinase 10
- 1-aminocyclopropane-1-carboxylate synthase 2
- Probable WRKY transcription factor 33
- 5'-methylthioadenosine nucleosidase
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- Ethylene-responsive transcription factor ERF104
Sequence:
MVAFATEKKQDLNLLSKIASGDGHGENSSYFDGWKAYEENPFHPIDRPDGVIQMGLAENQLCGDLMRKWVLKHPEASICTSEGVNQFSDIAIFQDYHGLPEFRQAVAKFMEKTRNNKVKFDPDRIVMSGGATGAHETVAFCLANPGDGFLVPTPYYPGFDRDLRWRTGVNLVPVTCHSSNGFKITVEALEAAYENARKSNIPVKGLLVTNPSNPLGTTLDRECLKSLVNFTNDKGIHLIADEIYAATTFGQSEFISVAEVIEEIEDCNRDLIHIVYSLSKDMGLPGLRVGIVYSYNDRVVQIARKMSSFGLVSSQTQHLIAKMLSDEEFVDEFIRESKLRLAARHAEITTGLDGLGIGWLKAKAGLFLWMDLRNLLKTATFDSETELWRVIVHQVKLNVSPGGSFHCHEPGWFRVCFANMDHKTMETALERIRVFTSQLEEETKPMAATTMMAKKKKKCWQSNLRLSFSDTRRFDDGFFSPHSPVPPSPLVRAQT
Protein: Rickets (Q7KTA0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Bursicon
- Partner of bursicon
Sequence:
MAARCRWSWRLALCPLLLQLLLQLLLLPPSAMGHDETKENPAPDMQNSQEQEPYVHLQHLQQQQQQNPQTVQQLSQITVNRTSKSASVTPTGIRENVMLPSADPEKEAQILYEKSLQEYHGSQLSTASTATDVIAGKRTLHSICERWLQKHCHCTGSLEVLRLSCRGIGILAVPVNLPNEVVVLDLGNNNLTKLEANSFFMAPNLEELTLSDNSIINMDPNAFYGLAKLKRLSLQNCGLKSLPPQSFQGLAQLTSLQLNGNALVSLDGDCLGHLQKLRTLRLEGNLFYRIPTNALAGLRTLEALNLGSNLLTIINDEDFPRMPNLIVLLLKRNQIMKISAGALKNLTALKVLELDDNLISSLPEGLSKLSQLQELSITSNRLRWINDTELPRSMQMLDMRANPLSTISPGAFRGMSKLRKLILSDVRTLRSFPELEACHALEILKLDRAGIQEVPANLCRQTPRLKSLELKTNSLKRIPNLSSCRDLRLLDLSSNQIEKIQGKPFNGLKQLNDLLLSYNRIKALPQDAFQGIPKLQLLDLEGNEISYIHKEAFSGFTALEDLNLGNNIFPELPESGLRALLHLKTFNNPKLREFPPPDTFPRIQTLILSYAYHCCAFLPLVAMSSQKKTSQVQEAVLFPSDAEFDMTLWNNSMMNIWPQMHNLSKQLGASMHDPWETAINFNEEQLQTQTGGQIATSYMEEYFEEHDVSGPATGYGFGTGLFSGMSTEDFQPGSVQCLPMPGPFLPCADLFDWWTLRCGVWVVFLLSLLGNGTVVFVLLCSRSKMDVPRFLVCNLAAADFFMGIYLGILAIVDAATLGEFRMFAIPWQMSVLCQLSGFLAVLSSELSVYTLAVITLERNYAITHAIHLNKRLSLKQAGYIMSVGWVFALIMALMPLVGVSDYRKFAVCLPFETTTGPASLTYVISLMFINGCAFLTLMGCYLKMYWAIRGSQAWNTNDSRIAKRMALLVFTDFLCWSPIAFFSITAIFGLQLISLEQAKIFTVFVLPLNSCCNPFLYAIMTKQFKKDCVTLCKHFEESRVVGGGGPGGRGAVARTKRGDLPPPLLPAAAVAHPPGCRCLRMLPSEMPNWHKMEQTPSMWQRLRTFCCGENRRRRKQRRQPQQRRQRAYTAAAANPYQYQFAELRQQRQNRASSISSENFCSSRSSSWRHGPPSSAPVPPGNCSMPLKMLEPHAHPHGHGRRRHSAWLITRKTSQDSNLSSSRNDSSASATTASTSTFRLSRSSAGSSTPLPSIIAHNGKAQLDAVKPRLVRQEAVQEEEDSSPPRLGVRFLPTIPSAADSSVVMEDGDSANTGVASFLGMPLPGASSGFLIAPTTAATTSPPPVVLQPAKPPPDPNDAPL
Protein: Inhibitor of growth protein 1 (Q9UK53)
Organism: Homo sapiens (Human)
Function: Cooperates with p53/TP53 in the negative regulatory pathway of cell growth by modulating p53-dependent transcriptional activation. Implicated as a tumor suppressor gene.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone deacetylase 1
- Paired amphipathic helix protein Sin3a
- Sin3 histone deacetylase corepressor complex component SDS3
- Histone-binding protein RBBP4
- Histone deacetylase complex subunit SAP30
- Histone deacetylase 2
- Histone H3.3C
- Histone H3.2
- Histone H3-7
- AT-rich interactive domain-containing protein 4A
Sequence:
MSFVECPYHSPAERLVAEADEGGPSAITGMGLCFRCLLFSFSGRSGVEGGRVDLNVFGSLGLQPWIGSSRCWGGPCSSALRCGWFSSWPPPSKSAIPIGGGSRGAGRVSRWPPPHWLEAWRVSPLPLSPLSPATFGRGFIAVAVIPGLWARGRGCSSDRLPRPAGPARRQFQAASLLTRGWGRAWPWKQILKELDECYERFSRETDGAQKRRMLHCVQRALIRSQELGDEKIQIVSQMVELVENRTRQVDSHVELFEAQQELGDTAGNSGKAGADRPKGEAAAQADKPNSKRSRRQRNNENRENASSNHDHDDGASGTPKEKKAKTSKKKKRSKAKAEREASPADLPIDPNEPTYCLCNQVSYGEMIGCDNDECPIEWFHFSCVGLNHKPKGKWYCPKCRGENEKTMDKALEKSKKERAYNR
Protein: Actin, cytoplasmic 1 (EC 3.6.4.-) (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed] (Q6QAQ1)
Organism: Sus scrofa (Pig)
Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60709}. Nucleus {ECO:0000250|UniProtKB:P60709}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P60709}.
Interaction partners:
- Caspase-3
- Profilin
- Peroxisome proliferator-activated receptor gamma
- Cofilin-1
- Ras homolog family member A
- Cofilin-2
- Ezrin
- Cell division control protein 42 homolog
- Caspase-3
- Uncharacterized protein.
Sequence:
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Negative elongation factor A (Q86NP2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. Has an essential role in postembryonic development.
Subcellular location: Nucleus {ECO:0000269|PubMed:15741180}. Chromosome {ECO:0000269|PubMed:15741180}. Note=Associates with polytene chromosomes. Associates with the hsp70 promoter when it is inactive, but not when it is activated.
Interaction partners:
- Negative elongation factor B
- Negative elongation factor D
- Negative elongation factor E
- Transcription elongation factor SPT5
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB1
- Transcription elongation factor SPT4
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB9
Sequence:
MANVRDSDTSLWLHNKLGTSNDSWINGSICSQLNKEVLRNIKECFPDLQTQVKLKLLLSFLHIPRRLVEEWKAELEEVIEVAGLDSELWVSMLAETMKTFPATSSLNTEISDYEDTRPIFIDMVNDLRKLVTKHSDLGMLPLECQYLNKNALISVVGQQPAPVKHFTLKRKPKSAQLRTELLHKSADAQSSLKKASAPTIPLRSRGMPRKMTDTTPLKGIPSRMPTTGFRSATVPGNAAQRPNLSRTPAGRKDGGIKLIEFTEQPLGYAAAKKRKREQQLEEQQKKQEQKQQQAAAAAAAAATAAASNAGDSSPTDAATASGGETPVTPTSANNSFEIKMEPQQLNQSAGSLEEPQDDEMSGKANMECDIETPEYATATLDFAQATSTSVADGQPGKPAVETKLKTPRTPKSAAKLNNNNNNNNNNSFNHTPKRIKQEIEIKSEEIIVPASIKLEKIETSPSTQRVSIQQQPPSLVQRTPHLLIRSSPQKRQNNGATTSAGTTTTTVGNTTIKMEKLDIKPMIRATGVSPSTSAGTTTTLLTPQQLRQAANPLANLPNNISVKITSAKAKAAAAAAATSSGSQTQSQQPQTLQVQQAPQQSHPPLLINSSTPVILASSPSAQRAKALALPSSSTSATTTTTIPSQAIKTMPLSQLKTATNSGPVIISQTIIQPAKRAQQQAGTSSAAAASQQQQQQQSQQQLLHQQIQQQTQQQAQLPQQPQQQQTQYILATPQQQPQQIQQQQQQQQPILPTLTSFSHSRPMPQTTTLYQATTPSGSGQTPTKILLKTSGSSSVVMTPLRQAQPQQATAVVSSNPPPLVATSAAVVSPGQTTLNIQNVQLPNRPVTIQPASQAAQQQHMQAQLQQQQPHPQHTIVANTTATQQPKLSQVLMQPTAAVGTSGVSALNVSPTSGKNKTIILTQKGVILRNIGGDMYQQIPISNVGNMQGLGGTTLMTTTAGPPSLVKTTPSSGVQLQQQQSGKQILPTLIPTSSLGGQHVIVQQQQPTNVIGNSQQQTIIRPVMTNVGGGLTTLPQGLTLIQRPGQQPQLVQVQAAPGSTQRTIITQSNTAAAASQQQPRQQQQQILVQHKPAPTLQQRLVTSTTSGGQGQQGNPNAGLPRTVQVQVQAQQQQQPQQQQATQQQSQQAPQRRGLSLSNEHVHKAHEMFRKANRVSRPDKALILGFMAGLRENPRPNNENVLVIKLGETEEKVQQDNGHTALCLVESHIRLDYNTGEWKTFQNYRLQDQSAAS
Protein: Atypical chemokine receptor 2 (V9GZ70)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAATASPQPLATEDADSENSSFYYYDYLDEVAFMLCRKDAVVSFGKVFLPVFYSLIFVLGLSGNLLLLMVLLRYVPRRRMVEIYLLNLAISNLLFLVTLPFWGISVAWHWVFGSFLCKMVSTLYTINFYSGIFFISCMSLDK
Protein: UBX domain-containing protein 5 (Q06682)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cell division control protein 48
- Ubiquitin fusion degradation protein 1
- Nuclear protein localization protein 4
- UBX domain-containing protein 4
- Proteasome subunit beta type-4
- UBX domain-containing protein 7
- UBX domain-containing protein 6
- UBX domain-containing protein 1
- Cullin-3
- UBX domain-containing protein 3
Sequence:
MSEGKVDEFMAITGADDAAIATQFIEMADGNLNTAISLFFENGGAALLSSNNTPTPSNSTPMAPTSVDSDADAQLAERLQREAYQQQQPDQDYVRPPDEARHEVLTETSGFPISYGGIGGRFEPLHRVNDMFDEGRPESIFNQRLDDTNTNTYINDNSSDSLDSEEENDDDEYEYVEEPVIELDEDGNIKEYTKLVRKPKTISKEQKLALLFRPPFSIMSKLDLDAAKQKARAKQKWIMINIQDSGIFQCQALNRDLWSSRPVKTIIKENFVFLQYQYESRNAQPYLQFYHLNNKDDLPHIAILDPITGERVKQWNRVVPIPEQFISEINEFLASFSLDPKVPNPTVNEPLPKVDPTTLTEEQQMELAIKESLNNNSSKSNQEEVPSTGEEQKRVQEPDPFSTIEARVHPEPPNKPGITTRIQIRTGDGSRLVRRFNALEDTVRTIYEVIKTEMDGFADSRFTLNDHQREDLIDKLNMTIADAGLKNSSLLLEKLDPEIE
Protein: Probable ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (Q8I2Z8)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- transketolase
- Phosphotransferase
- Enolase
- riboflavin kinase
- pyruvate kinase
- Pyruvate kinase
- Phosphoglycerate kinase
- Phosphoglycerate mutase
Sequence:
MDTKSGDKNAANKGGADGLVKTVSVLLRDNKCQFNIDENYDHNDKEKLECEVGKRDSGMINCLMEKLTSKKFLEEKESKNSFYLVDNENMKIKKLKEHGHSASLNDDLSPLQYERTKYIPSLPKALASEYQILDENYGDEFINKNDYEDVKRFLKNLHNLPMLNVKDSNNNESFKGGNILKIGIILSGGPAPGGHNVISGIYDYAKRYNEQSQVIGFLGGIDGLYSKNYVTITDSMMNRFRNLGGFNMLWSGRGKVKNKDDLIAIENIVAKLKLNGLVIIGGDGSNSNAALMAEYFAERQIPISIIGVPKTIDGDLKSEAIEISFGFDTATRTYSEIIGNLCTDVKTGHNVYHVVRVMGRSASHVVLECALQTRPNVVLIGEEVEQLNLSLKDIVKNIVNIILKRKSLNKNYGVILLPEGLIEFVPEMKILISELNVILKDGPFDASKLQKSKEVWDFLPPIIRDQLLMDRESTGYIQVGKIATERLIIVLVESELAKLNDKNLNIQFMSHYLGYEGRCAIPSNFDCNYCYALGYNAALLIDHKKTGYMSIIRNLEDSYTNWIPAAIPFLRIMHVIKDNTGNEFPAVKRYLVDLNSPLFNVLKEVRSLWSLYDLYRSPGPIQFNGHLGNARCYTVKTPTKDNLLCQNADDLELIINLTNKNMYENNGDNNHNISDDKARDGGSSPTSSAKKTKYNLSDDNNNNNNNNINNVSTNYNNTSDGSTFGNTTLLNTAYNVNGDGMNTLNCQKSNTSDVLSSEPVNQGFYEQHASSYKSLGCMSELQTSRLYNKLELPELCSDLKAKVRAGKQYISNDPYTQKQILSNYPHMSYENKFQIQEIFHDKYASPISFEIRIGIVFLSRQAPGAMNVLCGLYRRLKLLKGVCIAFYGLYGLLHNKYIIIDDDNIAKYVNQGGLELTGNSPEHSLFDKENRNKVCETVTKLQLNGLVMPGSNITITEAALLSEYFLEKKIPTSVVGIPLTGSNNLIHELIETCVGFDSSTKVYASLIGNVLTDAVSMPKYWHFIRLMGRSPSHEVLECALQTHPNVVIISEEYGAADKTLWRVVQDIADVVCARADVGKNYGTVLIPDALLMHLPHMKILLSEISDILNEASEKGQLLEARNDLVNLSGVDHGHLTSEWVSKLTPWSLALLKTFPQFIIKELLQVDLRSMRFEQLETEQLLLQMVKEELQDRKQKGKYSGSFMGLTHFFGYQGRSSLPSEFDCKLAYAYGHAASIVIESGLTGYIVSIRGLCGNVKDWKLFAIPFISLMKILPKGQGSKYLKSASKGDLPVIPSAPVDLNGKAYRSLKIALQKWQMEDRFCNPGPIQFEGNASNYYNRILFEEQSEYFEMLRYVECYANILKDTCRFGVSADYLKNVFVQLCGMLVLAYKPNDILSNMPYIGSIEDYYDWENQRKRMN
Protein: Guanylate kinase, putative (EC 2.7.4.8) (Q389H1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- GMP synthase
- Pyruvate kinase
- Ribonucleoside-diphosphate reductase
- Nucleoside diphosphate kinase, putative
- Nucleoside diphosphate kinase, putative
- Nucleoside diphosphate kinase
- Hypoxanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
Sequence:
MGAYPNRFGFSVSHTTRAPREGEVHGREYFFSTRESMLTMEKEGKFIELCDVHGNLYGTSIDAVKEVQSTGKVCVIDMDVKGAQKLRASGYLKNVLYLFVTVPSIDVLRARIQKRGALSEEVLQRRIATAEVELHFLGENPTFFSHVITNEELEVSYKKLCEIVGSEFLKYGMEGLNK
Protein: Brevinin-1Pa (P82841)
Organism: Lithobates pipiens (Northern leopard frog) (Rana pipiens)
Function: Antibacterial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli. Has activity against C.albicans.
Subcellular location: Secreted.
Interaction partners:
Sequence:
FLPIIAGVAAKVFPKIFCAISKKC
Protein: Fucolectin (Q7SIC1)
Organism: Anguilla anguilla (European freshwater eel) (Muraena anguilla)
Function: Acts as a defensive agent. Recognizes blood group fucosylated oligosaccharides including A, B, H and Lewis B-type antigens. Does not recognize Lewis A antigen and has low affinity for monovalent haptens.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
VIPEGYTQENVAVRGKATQSAQLRGEHAANSEASNAIDGNRDSNFYHGSCTHSSGQANPWWRVDLLQVYTITSVTITNRGDCCGERISGAEINIGQHLASNGVNNPECSVIGSMATGETKTFHCPAPMIGRYVVTYLPTSESLHLCEVEVNVDKPAAA
Protein: Protein Rex (Rev homolog) (Rex-2) (Q85601)
Organism: Human T-cell leukemia virus 2 (HTLV-2)
Function: Rex escorts unspliced gag-pro-pol and singly spliced env mRNAs out of the nucleus of infected cells. These mRNAs carry a recognition sequence called Rex responsive element (RxRE or XRE) located at the 3' region of the long terminal repeat (LTR). This function is essential since most HTLV proteins are translated from unspliced or partially spliced pre-mRNAs that cannot exit the nucleus by the pathway used by fully processed cellular mRNAs (By similarity).
Subcellular location: Host nucleus, host nucleolus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=The presence of both nuclear import (NLS) and nuclear export (NES) signals leads to continuous shuttling between the nucleus and cytoplasm. {ECO:0000250}.
Interaction partners:
Sequence:
MPKTRRQRTRRARRNRPPTPWPISQDLDRASYMDTPSTCLAIVYRPIGVPSQVVYVPPAYIDMPSWPPVQSTNSPGTPSMDALSALLSNTLSLASPPSPPREPQGPSRSLPLPPLLSPPRFHLPSFNQCESTPPTEMDAWNQPSGISSPPSPSPNLASVPKTSTPPGEKP
Protein: Heterogeneous nuclear ribonucleoprotein C (G3V2Q1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSVTEHPSPSPLLSSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSKSGKLKGDDLQAIKKELTQIKQKVDSLLENLEKIEKEQSKQAEMKNDKSEEEQSSSSVKKDETNVKMESEGGADDSAEEGDLLDDDDNEDRGDDQLELIKDDEKEAEEGEDDRDSANGEDDS
Protein: Vacuolar protein sorting-associated protein 4 (Q8IKQ5)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1, putative
- Vacuolar protein sorting-associated protein 46, putative
- Vacuolar-sorting protein SNF7, putative
- Vacuolar protein sorting-associated protein 2, putative
- Putative vacuolar protein sorting-associated protein 60
Sequence:
MDSEETINLAVKYAKEAVVEDEKKNYKEALNLYIQSLQYFNFFCKYEKNSNIRDLILKKMEVYMTRAENLKEMLNKKDSIENKEKITNTEETKENMKKQIKQFILNKNNNIKWSDVCGLETAKEVLKEAIIFPLKFPKLFNSSTLPYKGILLYGPPGTGKTFLALACSNECNMNFFNVSSSDLVSKYQGESEKYIKCLFETAKEHSPAIIFIDEIDSLCGSRTDGENESTRRIKTEFLINMSGLTNYKNNIIVMGATNTPWSLDSGFRRRFEKRIYIPLPNIYARAKIFEKYINQNENNNISKEDIKQFATLTENYTGADIDILCRDAVYMPVKKCLLSKFFKQVKKNNKICYTPCSPGDSDPTKVEKNVMSLSENELSLPPLTVQDFKTAISNAKPSLSVDDIKKYEEWTHQYGMNGT
Protein: Metallothionein-like protein (Q2VWA6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MSCCGGNCGCGSGCKCGGGGGCGCGGCKMYPEMNFAEQTTTETLVLGVAPRKVNFDGAEMETGAENGCKCGDNCTCNPCNCK
Protein: Chromosome 11 open reading frame 71 (Up-regulated in lung cancer 7) (A0A0A8K8C2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALNNVSLSSGDQRSRVAYRSSHGDLRPRASALAMVSGDGFLVSRPEAIHLGPRQAVRPSVRAESRRVDGGGRSPREPDGRGRSRQARFSPYPIPAVEPDLLRSVLQQRLIALGGVIAARISV
Protein: DNA replication licensing factor mcm6 (EC 3.6.4.12) (Minichromosome maintenance protein 6) (P49731)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA replication complex GINS protein sld5
- DNA replication licensing factor mcm10
- Cell division cycle protein cdt1
- DNA replication complex GINS protein psf2
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm3
- DNA replication complex GINS protein psf3
- Cell division control protein 18
- DNA replication licensing factor mcm4
- Cell division control protein 45 homolog
Sequence:
MSSLASQGNNASTPAYRYGFQTSEVGDRPTVSMPSQPESSAMLEDDGMVKRKPFAAIGEAIPKVIDTTGESVREAFEEFLLSFSDDRVAGGDALPSASQEKYYVQQIHGLAMYEIHTVYVDYKHLTSYNDVLALAIVEQYYRFSPFLLRALQKLIEKFEPEYYRSSLSRENASLSPNFKASDKTFALAFYNLPFRSTIRDLRTDRIGRLTTITGTVTRTSEVRPELAQGTFICEECHTVVSNVEQAFRYTEPTQCPNELCANKRSWRLNISQSSFQDWQKVRIQENSNEIPTGSMPRTLDVILRGDIVERAKAGDKCAFTGILIAVPDVSQLGIPGVKPEAYRDSRNFGGRDADGVTGLKSLGVRDLTYKLSFLACMVQPDDANDKSGADVRGDGSQGIEEQDEFLQSLSQEEIDDLRAMVHSDHIYSRLTNSLAPSVYGHEIIKKGILLQLMGGVHKLTPEGINLRGDLNICIVGDPSTSKSQFLKYVCNFLPRAIYTSGKASSAAGLTAAVVKDEETGDFTIEAGALMLADNGICAIDEFDKMDLSDQVAIHEAMEQQTISIAKAGIQATLNARTSILAAANPIGGRYNRKTTLRNNINMSAPIMSRFDLFFVVLDECNESVDRHLAKHIVDIHRLRDDAMQPEFSTEQLQRYIRYARTFKPKLNTESCAEIVKKYKQLRMDDAQGAGKNSYRITVRQLESMIRLSEAIARANCVDDITPAFVNEAYSLLRQSIIHVERDDIEVEEDDAEAQELENDNTNTTNGNDNVSSEEALQKPKVKITYDKYVSIMNGILQVLRQRSTEGVDGVPAGDLVQSYLELREDQFHTEEDIIYEVGLVRKVLTRLVHESIIMEIQNLTDSAVRLPFEERVFSIHPNCDIDALLSNGDVPN