wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear factor of activated T-cells 2 (A0A8I6A3G2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDAPEPQSDPDGGDGPGHEPGGSSQDELDFSILFDYDYLNPIEEEPIAHKAISSPSGLAYPDDVLDYGLKPCNPLASLSGEPPGRFGESDSIGFQNFLSPAKPAGASGPSPRIEITPSHELMQAGGALRGRDAGLSPEQPALALAGMAASPRFTLPVPGFEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNAGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVAPLPAASPQRSRSPSPQPSPHVAPQDDGIPAGYPPTAGSAVLMDALNSLATDSPCGIPSKIWKTSPDPTPVSTAPSKAGLARHIYPAVEFLGPCEQEERRNSAPESILLVPPTWPKQLVPAIPICSIPVTASLPPLEWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPEPSGRIVSLQAASNPIECSQRSAHELPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPSDEYEPSLICSPAHGGLGSQPYYPQHPMLAESPSCLVATMAPCQQFRSGLSSPDARYQQQSPAAALYQRSKSLSPGLLGYQQPSLLAAPLGLADAHRSVLVHAGSQGQGQGQGSTLPHTSSASQQASPVIHYSPTNQQLRGGGHQEFQHIMYCENFGPSSVRPGLPPVNQGQRLSPGSYPTVIQQQTAPSQRAAKNGPPVSDQKEALPSGVTVKQEQNLDQTYLDDGKKEFWPPGCPLRS
Protein: E3 ubiquitin-protein ligase Topors (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Topors) (SUMO1-protein E3 ligase Topors) (Topoisomerase I-binding RING finger protein) (Topoisomerase I-binding arginine/serine-rich protein) (dTopors) (Q9V8P9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions as a ubiquitin-protein E3 ligase. Negatively regulates the transcriptional repressor h/hairy by promoting its ubiquitination and subsequent degradation. Also directs the nuclear organization of the gypsy chromatin insulator. Chromatin insulators are regulatory elements which establish independent domains of transcriptional activity within eukaryotic genomes. Insulators have two defining properties; they can block the communication between an enhancer and a promoter when placed between them, and can also buffer transgenes from position effect variegation (PEV). Insulators are proposed to structure the chromatin fiber into independent domains of differing transcriptional potential by promoting the formation of distinct chromatin loops. This chromatin looping may require the formation of insulator bodies, where homotypic interactions between individual subunits of the insulator complex could promote the clustering of widely spaced insulators at the nuclear periphery. Within the gypsy insulator complex, this protein may promote formation of nuclear insulator bodies by recruiting individual insulator complexes to the nuclear lamina.
Subcellular location: Nucleus {ECO:0000269|PubMed:16209949}. Chromosome {ECO:0000269|PubMed:16209949}. Note=Colocalizes with the gypsy chromatin insulator complex on polytene chromosomes and to nuclear insulator bodies. Also localizes to the nuclear lamina.
Interaction partners:
- Modifier of mdg4
- Zinc finger protein su
- Centrosome-associated zinc finger protein Cp190
- Ubiquitin carboxyl-terminal hydrolase 16/45
- DNA topoisomerase 1
Sequence:
MAEENPGALAANVPYLGVDELGASVIVEPGLEGSNAGGRTLPAAAIKFADLTESGSESGDNEAEEPVSAGPDNANAIGEPGTSASAAEENGTVERNSPPPNCAICLSRCRRKCFTDSCMHQFCFKCLCEWSKIKPECPLCKQPFRTIIHNVRTLDDYDRYPVQTTSPVPTENPSLRYHIVRRPRYTPLVQNQAVIVNDIEAAIAAGAAGEDVLSAAEVAAGRRSYSRFEPYRSELMNYYQHDQDASTSGSLSQLWRRYVYDRKLYALPVSDSVTGHFREWSARFYRNNPAQIHRLMPWIHRDIMCLLRNAAHSVNTVMTLMSDLLPMTSLLGPTFRRRLSPYLGERTSHFIHELFNFARSPYDINGYDHVVQYSARVAEEVEVDLLDMVETQSSNGDDLNLEVGDSDADAINAGFSPDWSPPRVRPSTSVIVTNPGATHSFSVTMASDGSELPGISIRRTTNVGSQTVAINLSMRRPAAVASEEPEVIEIDDGDAAANAEVAAINDGSNTSRRHAGATLPVTAHIELESSSSSGDEDECVFVLELKPPHMRTPEQVSLDSNSDSDVVFVNEQHEAAPDAIAENRSTQSPLDLASRDQGLFMGPSTSGAAANRGKNWKLVMAQTRRLDQLRTLRSIRSKKSRRSSMPARSDSGSSPSSCSSSSFHFSSSSDEDSSDSSTTNSEPPKKKSRKRVANNKRSKKESIGKRTSRKRKAKDQNMEMLEQQQISQKKPQRQPESSSDSPSSSDDESGGDSSESSGQPNTNNNKSSSDSDDDSAVNMQLSALRATLKAEATLEDRKPVKLELQLPDDDQAGPLHSRMTPSPREDNEPGCSAPKRRRSCSHSNQSSQSASLASSSTATSSSAPLSSFAWGAAGFSGDPLMRGHPAMEEHDIANSLIELSTLTQPVNIGLFNEHYNSAENSMGMLSNTLCDSPQTLAADDANLENYFDTDADPEASRERDAYSLEAAIDVVGESELQIAEDTATATEEQDEEDEEDEDQEEDDQEEEKAAEEEEEEEEDDDDSDNHDENDENQGLLPY
Protein: Homogentisate 1,2-dioxygenase (EC 1.13.11.5) (Homogentisate oxygenase) (Homogentisic acid oxidase) (Homogentisicase) (Q9Y041)
Organism: Caenorhabditis elegans
Function: Plays a role in the tyrosine degradation pathway.
Interaction partners:
- 4-hydroxyphenylpyruvate dioxygenase
- Putative protein C31H2.4
- Fumarylacetoacetase
- Probable maleylacetoacetate isomerase
- maleylacetoacetate isomerase
- maleylacetoacetate isomerase
- Oxaloacetate tautomerase fahd-1, mitochondrial
- Tyrosine aminotransferase
- Kynureninase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
Sequence:
MSEFDELKYLTGFGNEHATSDPRVPDALPVGQNSPQKCSHGLYAEQLSGTAFTAPRSQNQRSWLYRIRPSVIHRPFEAMKENDQHWTNNFSSIPPNPNQYRWNPFPLPTKEGVTFVDNLYTVCGGGDVISRTGLAIHQFSCNASMEHTAMYNSDGDFLIVPQQGALEITTEFGRLLVNPQEIAVIPQGIRFSVAVRGPSRGYILEVYGTHFQLPDLGPIGANGLANPRDFEAPVAWFEDLDVEFTIINKYQGSWFQAKQGHSPFDVVGWHGNYVPYKYDLKKFMVINTVSFDHCDPSIFTVLTAPSVKHGTAIADFVIFPPRWGCADNTFRPPYYHRNCMSEYMGLITGCYEAKEGGFKPGGGSLHSMMTPHGPDFNCFEMASNADLKPQRVAEGTMSFMFESSLNMAITNWAVYQNVDKDYYKDWQPLKKHFTMPK
Protein: Tetratricopeptide repeat protein 8 (Bardet-Biedl syndrome 8 protein homolog) (Q23049)
Organism: Caenorhabditis elegans
Function: Component of the BBSome complex (By similarity). The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function (By similarity). Required for proper BBSome complex assembly and its ciliary localization. Required for cilia biogenesis and both the assembly and movement of intraflagellar transport proteins along the ciliary axoneme. Plays a role in guanylyl cyclase localization in the ring-like structures at the base of the finger compartment in AFD sensory neurons.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:15231740, ECO:0000269|PubMed:25335890}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15231740}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:15231740}. Note=Localized at the ciliary base and also in ring-like structures between the base of the AFD sensory neuron finger compartment and the dendritic membrane. {ECO:0000269|PubMed:25335890}.
Interaction partners:
- BBSome complex member BBS1
- Protein pthb1 homolog
- BBSome complex member bbs-4
- BBSome complex member bbs-7
- BBSome complex member bbs-2
- BBSome complex member bbs-5
- BBSome-interacting protein 1
- Very long-chain fatty acid transport protein
- long-chain-fatty-acid--CoA ligase
Sequence:
MSGESVIEFTGFIKACRLFRENRLAEAEAVCTNLLRKNPLDQATWALKMQCLSDSTYVDELENEDMGLAETFLDQNVIAPNARPGTSFARPKTSAKGVNPILRPTTNAGRPLSGVVRPQSSFKSGSMDQAVRTARTAKTARAVSSTSARNMRLGTASMAAGADGEFVNLARLNIDKYAADPQVNRQLFEYVFYYLNDIRVAHQIAGTASKAAGFEDYYWKNQLAKCYLRLGMLQDATKQLQSSLEQKKLIETFALLSKAYNRVDQPMAALKTYSAGLEVFPENVTMLTGMARVQEALGEYDESVKLYKRVLDAESNNIEAIACVATTYYYGGKPELAMRYYRRILQMGVSSPELFLNIGLCCMAAQQFDFALSSILRAQSTMTDDVAADVWYNIGQILVDIGDLVSAARSFRIALSHDPDHSESLVNLGILKHREGKIDEARSLYSSATSKNPYMFEGNYNLGLVSFTQGKYHECRELIEKALAAFPEHEHCKKILNHLKPLYESI
Protein: Protocadherin gamma subfamily C, 3 (Q9BR81)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVPEAWRSGLQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Coiled-coil domain-containing protein 158 (Q5M9N0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MESKAWESNNEDLLSSSGVTSNGGSSSSFFVSSIRGTIIENTSSAGTLTQVPFFPKYEVELDSPRKIIPSPGKEHFERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLKDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKICEHDSMSTLHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQMEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKTEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDNRNMEVQRLEALLKALKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTISDLTTSLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMTEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRMELKELKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRSELNNLSEEYEVLKRNFRNKSEEMEMTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKSKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVTNMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDIKELQGPGYTSNSSLKPRLLQPASVTRSHSNVPSSQSTASFLSHHSTKANTLKEDPTRDLKQLLQELRSVINEEPAVSLSKTEEDGRTSLGALEDRVRDCITESSLRSDMCHRSNNSLRDSTEGSKSSETLSREPVTLHAGDREDPSGCFTFTSAASPSVKNSASRSFNSSPKKSPVHSLLTSSVEGSIGSTSQYRSAKPIHSSDSVKDSQSPPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQEKMLLK
Protein: UDP-N-acetylgalactosamine-undecaprenyl-phosphate N-acetylgalactosaminephosphotransferase (EC 2.7.8.40) (B3FN88)
Organism: Aeromonas hydrophila
Function: Transfers N-acetyl-galactosamine (GalNAc) to undecaprenyl phosphate, a step in the assembly of the repeating-unit of the O-antigen. Shows no activity with UDP-N-acetyl-alpha-D-glucosamine.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSYQRRHSRWYERVLFSPPSLFFLGAMLAVCLPALERWGWGFWEYFDAVRVNTLGGAFVAFLLTGIVLYRFLRYPGASPVAYMIPTVTTLYGSLVGALFFLRLPYSRQVLFESYVVALLCCWVVYFIGRRYRTPKYALLPFGDYQPLMHHTCVEWRLLDKPDLGAVRYDAVVADLRDDDLAGEWERFLARCALAHIPVYHIKQISETLTGRVKIDHLHENQLGSLLPSPIYAFIKRGMDILAAVIAIPLFSPLMLATAVLIKLESPGPVMFLQNRVGKGNRDFRIYKFRSMCQNSEQHGAQFAQDGDMRVTRVGKVIRKLRIDELPQFFNVLKGDMSLIGPRPEQRTFVDQFDREIPFYMYRHIVRPGISGWAQVVHGYAADADDTRIKIEHDFYYIKNFSLWLDVLIVFKTIRTILTGFGAR
Protein: E74-like factor 2 (Ets domain transcription factor), isoform CRA_b (cDNA FLJ53930, highly similar to ETS-related transcription factor Elf-2) (cDNA, FLJ79354, highly similar to ETS-related transcription factor Elf-2) (B7Z720)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MATSLHEGPTNQLDLLIRAVEASVHSSNAHCTDKTIEAAEALLHMESPTCLRDSRSPEFIHAAMRPDVITETVVEVSTEESEPMDTSPIPTSPDSHEPMKKKKVGRKPKTQQSPISNGSPELGIKKKPREGKGNTTYLWEFLLDLLQDKNTCPRYIKWTQREKGIFKLVDSKAVSKLWGKHKNKPDMNYETMGRALRYYYQRGILAKVEGQRLVYQFKDMPKNIVVIDDDKSETCNEDLAGTTDEKSLERVSLSAESLLKAASSVRSGKNSSPINCSRAEKGVARVVNITSPGHDASSRSPTTTASVSATAAPRTVRVAMQVPVVMTSLGQKISTVAVQSVNAGAPLITSTSPTTATSPKVVIQTIPTVMPASTENGDKITMQPAKIITIPATQLAQCQLQTKSNLTGSGSINIVGTPLAVRALTPVSIAHGTPVMRLSMPTQQASGQTPPRVISAVIKGPEVKSEAVAKKQEHDVKTLQLVEEKPADGNKTVTHVVVVSAPSAIALPVTMKTEGLVTCEK
Protein: Delta-like protein 4 (Drosophila Delta homolog 4) (Delta4) (Q9JI71)
Organism: Mus musculus (Mouse)
Function: Involved in the Notch signaling pathway as Notch ligand. Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting (By similarity). Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types. During spinal cord neurogenesis, inhibits V2a interneuron fate (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 4
- Delta-like protein 1
- Delta-like protein 3
- Recombining binding protein suppressor of hairless
- Ephrin-B2
- Hairy/enhancer-of-split related with YRPW motif protein 1
- Cadherin-5
Sequence:
MTPASRSACRWALLLLAVLWPQQRAAGSGIFQLRLQEFVNQRGMLANGQSCEPGCRTFFRICLKHFQATFSEGPCTFGNVSTPVLGTNSFVVRDKNSGSGRNPLQLPFNFTWPGTFSLNIQAWHTPGDDLRPETSPGNSLISQIIIQGSLAVGKIWRTDEQNDTLTRLSYSYRVICSDNYYGESCSRLCKKRDDHFGHYECQPDGSLSCLPGWTGKYCDQPICLSGCHEQNGYCSKPDECICRPGWQGRLCNECIPHNGCRHGTCSIPWQCACDEGWGGLFCDQDLNYCTHHSPCKNGSTCSNSGPKGYTCTCLPGYTGEHCELGLSKCASNPCRNGGSCKDQENSYHCLCPPGYYGQHCEHSTLTCADSPCFNGGSCRERNQGSSYACECPPNFTGSNCEKKVDRCTSNPCANGGQCQNRGPSRTCRCRPGFTGTHCELHISDCARSPCAHGGTCHDLENGPVCTCPAGFSGRRCEVRITHDACASGPCFNGATCYTGLSPNNFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLVVLLVLLVMVVVAVRQLRLRRPDDESREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKLQNHTLDYNLAPGLLGRGGMPGKYPHSDKSLGEKVPLRLHSEKPECRISAICSPRDSMYQSVCLISEERNECVIATEV
Protein: BK channel (A0A2R8QRZ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLAVADGNGSYGSSSSRMSNNINFNKNPDSSVSISKMDVIIPFTPDVPCDNNGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCNIKNKEAQKVNNPITIQADGTTKTGNEKEEAPASEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALGIYFIDSSDPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLCSIFISTWLTAAGFIHLVENSGDPWENFQNSQPLSYWECVYLLMVTMSTVGYGDVYARTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVNGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKAGFIAQSCLAQGLSTMLANLFSMRSYIKIEEDTWQKYYLEGVANEMYTEYLSSAFVGLSFPTVCELCYVKLKLLLIAIEYKSEQRESSILINPGNHVKMQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRIEDEHPSTLSPKKKQRNGGMRNSPNCSPKMMRHDPLLIPGNEQIESMDANVKRYDSTGMFHWCPSKEIEKVILTRSEASMTVLSGHVVVCIFGDVTSALVGLRNLVMPLRASNFHYHELKPIVFVGSLDYLRREWETLHNFPKVFILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDASLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGLVRQASVTTGSNIPIITELAKPGKLLPLVSFSQEKNSGTNIQMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALLAEENALRGGYSTPQTLANRDRCRVAQLALYDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLGAPSQCTKRYVITNPPYEFEMVPTDLIFCLMQFDHNAGQSRASLSHSSHSSHSSSKKSSSVHSIPATNRQNRSSKAREARDKQNATRMNRMGPEKRWFTDEAENAYPRNIQIKPMSTHMANQVNQYKSTSSLIPPIREVEDEC
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A1ZBL5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSTAMRTTLQSVPEALPADSVSNGTASNVAAPAAPVSSATNAVPPLAAVSSTTATYATNSISTSSHSVKDQQQQQQQQQHDSANANIVSLPPTTTPVANTNTMMPIVTSSNSATSNSTAATPTPASGAAATGGVGSVSQGPATVSASAANTNHSHQHSHQHHHHVANNMTTDGARLSSNNSAVVASSAINHHHHHTPGSGVAPTVNKNVLSTHSAHPSAIKQRTSSAKGSPNMQMRSSAPMRWRATEEHIGKYKLIKTIGKGNFAKVKLAKHLPTGKEVAIKIIDKTQLNPGSLQKLFREVRIMKMLDHPNIVKLFQVIETEKTLYLIMEYASGGEVFDYLVLHGRMKEKEARVKFRQIVSAVQYCHQKRIIHRDLKAENLLLDSELNIKIADFGFSNEFTPGSKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGSTLRELRERVLRGKYRIPFYMSTDCENLLRKFLVLNPAKRASLETIMGDKWMNMGFEEDELKPYIEPKADLADPKRIGKTEALVAMGYNRSEIEASLSQVRYDDVFATYLLLGRKSTDPESDGSRSGSSLSLRNISGNDAGANAGSASVQSPTHRGVHRSISASSTKPSRRASSGAETLRVGPTNAAATVAAATGAVGAVNPSNNYNAAGSAADRASVGSNFKRQNTIDSATIKENTARLAAQNQRPASATQKMLTTADTTLNSPAKPRTATKYDPTNGNRTVSGTSGIIPRRSTTLYEKTSSTEKTNVIPAETNSGSAAPAGKGHTKSASVSSPRPSTDGCVSVSNDPLGTRARNNTALEYSGTSGASGDSSHPGRMSFFSKLSSRFSKRPTIADEAAKPRVLRFTWSMKTTSPLMPDQIMQKIREVLDQNNCDYEQRERFVLWCVHGDPNTDSLVQWEIEVCKLPRLSLNGVRFKRISGTSIGFKNIASRIAFDLKL
Protein: RCC1 and BTB domain-containing protein 1 isoform X1 (Regulator of chromosome condensation (RCC1) and BTB (POZ) domain-containing protein 1) (B8A4R1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Zinc finger protein 408
- ATP-dependent RNA helicase DDX55
- DNA excision repair protein ERCC-6-like
- SURP and G patch domain-containing 1.
- SKA complex subunit 2
- RNA helicase
Sequence:
MVDVSKWPLFTLLSAQELSSIRQACIFGASANEAIYITHDDEVYVLGLNCSNCLGTGDSQSTIAPKKLDCLSGKKLISLSYGSGPHVLLVTEDGELYAWGHNGYSQLGNGTTNQGVSPILVSTNLQGKRVTEVSCGSHHSLALTHEGEVFAWGYNNCGQVGSGSTANQPTPRKVSNCLQNKVIVNIACGQTSSMAVTDNGEVYGWGYNGNGQLGLGNNGNQLTPCRLIALQGFCVLQIASGYAHSLALTDEGLLYAWGANTYGQLGTGNKSNQLSPVQVMTEKERIVEIAACHSTHTSAAKTQSGQVYMWGQCRGQAIVLPHLTHFASTDDVFACFATPSVMWRMLSMEHDDFLTVAQSLKKEFDNPETSDLKFSIDGKYIHVHKAVLKIRCEHFRSMFQSHWNEDMKEVIEIDQFSYPVYRSFLEFLYTDSVDLPPEDAIGLLDLATSYCENRLKKLCQHIIKRGITVENAFSLLSAAIRYDAEDLEEFCFKFCVNHLTEVTQTAAFWQIDGNMLKEFICRASHCGAFKN
Protein: Enhancer of split m6 protein (E(spl)m6) (O97179)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ocho, isoform B
- Enhancer of split M2 protein
Sequence:
MSKVKNLLAKMLQRFGKNSSQADSQRYDSLEEIAQNQANERMLRATQVGLEEHLVICLETEAGSFYWHSQ
Protein: DnaJ heat shock protein family (Hsp40) member B4 (C9JUL4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKDYYCILGIEKGASDEDIKKAYRKQALKFHPDKNKSPQAEEKFKEVAEAYEVLSDPKKREIYDQFGEEGLKGGAGGTDGQGGTFRYTFHGDPHATFAAFFGGSNPFEIFFGRRMGGGRDSEEMEIDGDPFSAFGFSMNGYPRDRNSVGPSRLKQDPPVIHELRVSLEEIY
Protein: Nucleoporin 62 (M0R302)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGFNFGGTGAPTGGFTFGTAKTATTTPATGFSFSTSGTGGFNFGAPFQPATSTPSTGLFSLATQTPATQTTGFTFGTATLASGGTGFSLGIGASKLNLSNTAATPAMANPSGFGLGSSNLTNAISSTVTSSQGTAP
Protein: ATP synthase subunit d, mitochondrial (P30902)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit 4
- ATP synthase subunit g, mitochondrial
- ATP synthase subunit J, mitochondrial
- ATP synthase subunit a
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit f
- ATP synthase subunit alpha
- ATP synthase subunit H
Sequence:
MSLAKSAANKLDWAKVISSLRITGSTATQLSSFKKRNDEARRQLLELQSQPTEVDFSHYRSVLKNTSVIDKIESYVKQYKPVKIDASKQLQVIESFEKHAMTNAKETESLVSKELKDLQSTLDNIQSARPFDELTVDDLTKIKPEIDAKVEEMVKKGKWDVPGYKDRFGNLNVM
Protein: RNA polymerase principal sigma factor HrdB (RNA polymerase sigma factor SigA) (P18183)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. Its activity is stimulated by RbpA.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- RNA polymerase-binding protein RbpA
- RNA polymerase-binding transcription factor CarD
- MerR-family transcriptional regulator
- MerR-family transcriptional regulator
- AraC-family transcriptional regulator
- Zinc uptake regulation protein
Sequence:
MSASTSRTLPPEIAESVSVMALIERGKAEGQIAGDDVRRAFEADQIPATQWKNVLRSLNQILEEEGVTLMVSAAEPKRTRKSVAAKSPAKRTATKAVAAKPVTSRKATAPAAPAAPATEPAAVEEEAPAKKAAAKKTTAKKATAKKTTAKKAAAKKTTAKKEDGELLEDEATEEPKAATEEPEGTENAGFVLSDEDEDDAPAQQVAAAGATADPVKDYLKQIGKVPLLNAEQEVELAKRIEAGLFAEDKLANSDKLAPKLKRELEIIAEDGRRAKNHLLEANLRLVVSLAKRYTGRGMLFLDLIQEGNLGLIRAVEKFDYTKGYKFSTYATWWIRQAITRAMADQARTIRIPVHMVEVINKLARVQRQMLQDLGREPTPEELAKELDMTPEKVIEVQKYGREPISLHTPLGEDGDSEFGDLIEDSEAVVPADAVSFTLLQEQLHSVLDTLSEREAGVVSMRFGLTDGQPKTLDEIGKVYGVTRERIRQIESKTMSKLRHPSRSQVLRDYLD
Protein: RNA recognition motif (RRM)-containing protein (F4J5A7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Polyadenylate-binding protein-interacting protein 13
Sequence:
MASDRGSAASGGKPIWMKHAEDAKIKDEGEKDAAAKAAFEATFKGVDQTTHLIEPVAPVPESAPESDSDSDDDDDDESDYLSRKPIGPVDPSKSTASGAGIGGGTACVPSTFVVVTKDSDGRKVPNGGALIRVKVSPGVGVGGTDQEGVVKDVGDGSYAVTYVVPKRGNYMVNIECNGNAIMGSPFPVFFSQGSSSTGLMGSAPASYSNLINQTMPNMPNYTGSVSGAFPGLLGMVPGIASGPSGGAILPGVGASLGEVCREYLNGRCVNSMCKLNHPPQNLLMTAIAATTSMGNLSQVPMAPSAAAMAAAQAIVAAQALQAHASQMQAQAQSNKGSLGSPEKGENGDLKKFLQVSNLSPSLTTEQLRQLFSFCGTVVDCSITDSKHIAYIEYSNSEEATAALALNNTEVFGRALNVEIAKSLPHKPSSNNSSSSLPLMMQQAVAMQQMQFQQAILMQQAVATQQAANRAATMKSATELAAARAAEISRKLRPDGVGNDEKEADQKSRSPSKSPARSRSKSKSPISYRRRRRSPTYSPPFRRPRSHRSRSPLRYQRRSTYEGRRRSYRDSRDISESRRYGRSDEHHSSSSRRSRSVSPKKRKSGQEDSELSRLRRDSSSRGEKKSSRAGSRSPRRRKEVKSTPRDDEENKVKRRTRSRSRSVEDSADIKDKSRDEELKHHKKRSRSRSREDRSKTRDTSRNSDEAKQKHRQRSRSRSLENDNGSHENVDVAQDNDLNSRHSKRRSKSLDEDYDMKERRGRSRSRSLETKNRSSRKNKLDEDRNTGSRRRRSRSKSVEGKRSYNKETRSRDKKSKRRSGRRSRSPSSEGKQGRDIRSSPGYSDEKKSRHKRHSRSRSIEKKNSSRDKRSKRHERLRSSSPGRDKRRGDRSLSPVSSEDHKIKKRHSGSKSVKEKPHSDYEKVDDGDANSDSSQQERNLEGHLLSLDSMSSQDVEKSKENPPSSSSVERGDANDDEKFKIEEKRIILKS
Protein: DNA repair protein rad16 (EC 3.1.-.-) (P36617)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Endonuclease that specifically degrades single-stranded DNA and which is involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Required for double strand break-induced interchromosomal gene conversion.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mating-type switching protein swi10
- DNA repair protein rad14
- DNA repair protein rad13
- Crossover junction endonuclease mus81
- Replication factor A protein 1
- DNA mismatch repair protein msh2
- ATP-dependent helicase rhp16
- Probable asparagine--tRNA ligase, cytoplasmic
- DNA topoisomerase 3
- DNA repair protein rhp7
Sequence:
METKVHLPLAYQQQVFNELIEEDGLCVIAPGLSLLQIAANVLSYFAVPGSLLLLVGANVDDIELIQHEMESHLEKKLITVNTETMSVDKREKSYLEGGIFAITSRILVMDLLTKIIPTEKITGIVLLHADRVVSTGTVAFIMRLYRETNKTGFIKAFSDDPEQFLMGINALSHCLRCLFLRHVFIYPRFHVVVAESLEKSPANVVELNVNLSDSQKTIQSCLLTCIESTMRELRRLNSAYLDMEDWNIESALHRSFDVIVRRQLDSVWHRVSPKTKQLVGDLSTLKFLLSALVCYDCVSFLKLLDTLVLSVNVSSYPSNAQPSPWLMLDAANKMIRVARDRVYKESEGPNMDAIPILEEQPKWSVLQDVLNEVCHETMLADTDAETSNNSIMIMCADERTCLQLRDYLSTVTYDNKDSLKNMNSKLVDYFQWREQYRKMSKSIKKPEPSKEREASNTTSRKGVPPSKRRRVRGGNNATSRTTSDNTDANDSFSRDLRLEKILLSHLSKRYEPEVGNDAFEVIDDFNSIYIYSYNGERDELVLNNLRPRYVIMFDSDPNFIRRVEVYKATYPKRSLRVYFMYYGGSIEEQKYLFSVRREKDSFSRLIKERSNMAIVLTADSERFESQESKFLRNVNTRIAGGGQLSITNEKPRVIVDLREFRSSLPSILHGNNFSVIPCQLLVGDYILSPKICVERKSIRDLIQSLSNGRLYSQCEAMTEYYEIPVLLIEFEQHQSFTSPPFSDLSSEIGKNDVQSKLVLLTLSFPNLRIVWSSSAYVTSIIFQDLKAMEQEPDPASAASIGLEAGQDSTNTYNQAPLDLLMGLPYITMKNYRNVFYGGVKDIQEASETSERKWSELIGPEAGRRLYSFFRKQLKDYE
Protein: Hyaluronan and proteoglycan link protein 1 (Cartilage-linking protein 1) (Cartilage-link protein) (Proteoglycan link protein) (P10915)
Organism: Homo sapiens (Human)
Function: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Aggrecan core protein
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Sodium- and chloride-dependent creatine transporter 1
- EGF-like repeat and discoidin I-like domain-containing protein 3
- Cartilage oligomeric matrix protein
- Collagen alpha-2
Sequence:
MKSLLLLVLISICWADHLSDNYTLDHDRAIHIQAENGPHLLVEAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDYLKEVDVFVSMGYHKKTYGGYQGRVFLKGGSDSDASLVITDLTLEDYGRYKCEVIEGLEDDTVVVALDLQGVVFPYFPRLGRYNLNFHEAQQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNYGFWDKDKSRYDVFCFTSNFNGRFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKILGYDRCDAGWLADGSVRYPISRPRRRCSPTEAAVRFVGFPDKKHKLYGVYCFRAYN