wanglab/gogpt-training-data huggingface dataset:
Protein: EKC/KEOPS complex subunit CGI121 (CGI-121 homolog) (Q03705)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. CGI121 acts as an allosteric effector that regulates the t(6)A activity of the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. CGI121 is not required for tRNA modification.
Subcellular location: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000305}.
Interaction partners:
- EKC/KEOPS complex subunit PCC1
- tRNA N6-adenosine threonylcarbamoyltransferase
- EKC/KEOPS complex subunit GON7
- EKC/KEOPS complex subunit BUD32
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- Threonylcarbamoyl-AMP synthase
- Cell division control protein 13
Sequence:
MVVSIIPQFPDIKVSLALFEQVKNAKEIRSKMSELSTSFAFIDPRLVCSGEQMYSAIYKTLIEVKYNKMRTRNLNSECVLCLSPTSNISDAFLKFGIKDDSSQLICLKFHTNTDDVDKEQLRTIMTSIVKGQEIEFNDDNLSRFYDEALIRKIYKLSDDFKPQDVNGLSRALVDAIQLRGV
Protein: Pre-mRNA-splicing factor 38 (Q8MR43)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367025}.
Interaction partners:
Sequence:
MDEDYSASSSAGGGKKAGKQHNTLPFWGNESSMNLNALILANIQSSSYFKVHLFKLKTYHEVVDEIYYQVKHMEPWERGSRKTSGQTGMCGGVRGVGAGGIVSTAYCLLYKLYTLRLTRKQINGLLNHTDSAYIRALGFMYLRYTQPPGDLYDWYEDYLQDEEEIDVKAGGGQVLTIGQMVYQFMTKLDWFSTLFPRIPVPIQKQIEKRIEQYCREQGVTVHQLSTGRSTAGTGGGPGAAGQDADYQDYPEGGVERGSGGRGVDKLAPVPTPTHNRITTATIMTSVTTMLPRLARPTAVVAVAMRTTHRRRCHHRCLTASAKGRGIAIGIRIRITTATAASTRRSTTIDKARVAAAEAAAGVATAPSAMSASGTVVATSGAARAGTTNTMKSVSDVIGEDRFHPPKLASSSLSCSVTN
Protein: Transcription factor bHLH106 (Basic helix-loop-helix protein 106) (AtbHLH106) (bHLH 106) (Transcription factor EN 56) (bHLH transcription factor bHLH106) (O80674)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Probable transcription factor PosF21
- BZIP transcription factor, putative
- At5g56840
- Putative transcription factor bHLH041
- Protein PLANT CADMIUM RESISTANCE 4
- Protein PLANT CADMIUM RESISTANCE 11
- Protein PLANT CADMIUM RESISTANCE 9
- PLAC8 family protein
- Protein PLANT CADMIUM RESISTANCE 5
- Protein PLANT CADMIUM RESISTANCE 12
Sequence:
MQPETSDQMLYSFLAGNEVGGGGYCVSGDYMTTMQSLCGSSSSTSSYYPLAISGIGETMAQDRALAALRNHKEAERRRRERINSHLNKLRNVLSCNSKTDKATLLAKVVQRVRELKQQTLETSDSDQTLLPSETDEISVLHFGDYSNDGHIIFKASLCCEDRSDLLPDLMEILKSLNMKTLRAEMVTIGGRTRSVLVVAADKEMHGVESVHFLQNALKSLLERSSKSLMERSSGGGGGERSKRRRALDHIIMV
Protein: Unconventional myosin-Va (Dilute myosin heavy chain, non-muscle) (Myosin heavy chain 12) (Myosin-12) (Myoxin) (Q9Y4I1)
Organism: Homo sapiens (Human)
Function: Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.
Interaction partners:
- Ras-related protein Rab-27A
- Melanophilin
- Rab effector MyRIP
- Ras-related protein Rab-11A
- Protein spire homolog 2
- Ras-related protein Rab-10
- Exocyst complex component 4
- RILP-like protein 2
- Ras-related protein Rab-8A
- Melanoregulin
Sequence:
MAASELYTKFARVWIPDPEEVWKSAELLKDYKPGDKVLLLHLEEGKDLEYHLDPKTKELPHLRNPDILVGENDLTALSYLHEPAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRTPAKPTKGRPGQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKKYLRMRKAAITMQRYVRGYQARCYAKFLRRTKAATIIQKYWRMYVVRRRYKIRRAATIVLQSYLRGFLARNRYRKILREHKAVIIQKRVRGWLARTHYKRSMHAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDGELWLVYEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKKEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV
Protein: Thiohydroximate-O-sulfate sulfur/sulfate-lyase (nitrile-forming) NSP2 (EC 4.8.1.5) (Jacalin-related lectin 21) (Nitrile-specifier protein 2) (AtNSP2) (O49326)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.
Interaction partners:
- UPF0235 protein At5g63440
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- DELLA protein RGA
- Scarecrow-like protein 3
- Nuclear transcription factor Y subunit A-1
- Scarecrow-like protein 4
- Scarecrow-like protein 13
- Protein PAT1 homolog
- Scarecrow-like protein 27
- Scarecrow-like protein 21
Sequence:
MVQKVEARGGEIGDVWDDGAYDGVRKVYVGQGEDGIAFVKFEYVNGSQEVVGDERGKKTLLGAEEFEVDPDDYIVYVEGYHEKVFGVTTKEIISTLTFKTYKGKTSPPFGIVSGTKFVLQGGKIVGFHGRSTDVLHSLGAYISSPATPKLRGKWIKVEQKGEGPGPRCSHDIAQVGNKIFSFGGELTPNQPIDKHLYVFDLETRTWSISPATGDVPNLSCLGVRMVSIGSSLYVFGGRDASRKYNGFYSFDTTKNEWKLLTPVEQGPTPRSFHSMTADENNVYVFGGVSATVRLKTLDAYNIVDHKWVQCSTPGGSCSVRGGAGLEVVQGKVWVVYGFNGCEVDDVHCYDPAQDKWTQVETFGEKPCARSVFASAVVGKHILVFGGEIAMDPKAHEGPGQLSGGTFALDTETLKWEKLDKLGEEEETPSIRGWSASTTGTIDGKKGLVMFGGKAQTNDRFGDLFFYGVDSA
Protein: UPF0312 protein PA0423 (Q9I690)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Periplasm {ECO:0000255|HAMAP-Rule:MF_00780}.
Interaction partners:
- Cytochrome b561 bacterial/Ni-hydrogenase domain-containing protein
- Lipid/polyisoprenoid-binding YceI-like domain-containing protein
- DUF541 domain-containing protein
- Hemolysin
Sequence:
MLKKTLAALALGSALFTAGQAMAADYKIDKEGQHAFIEFRIKHLGYSWLYGRFNDFDGSFTFDEKNPSADKVKVTINTNSVDTNHAERDKHLRSGDFLNVSKNPTATFESTEVKANGDSADITGNLTLNGVTKPVTIKAKLIGQGDDPWGGYRAGFEGSATLKLKDFGIKMDLGPASQEVELLLSVEGIRQ
Protein: Histidine-containing phosphotransfer protein (F4J1I8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU369004}. Nucleus {ECO:0000256|RuleBase:RU369004}.
Interaction partners:
Sequence:
MQRQVALIKQSLFDQGYLDEQFMELEELQDDANPNFVEEVSALYFKDSARLINNIDQALERGSFDFNRLDSYMHQFKGSSTSIGASKVKAECTTFREYCRAGNAEGCLRTFQQLKKEHSTLRKKLEHYFQLARQAGPKETARRPK
Protein: Poly(A) RNA polymerase gld-2 (EC 2.7.7.19) (Defective in germ line development protein 2) (O17087)
Organism: Caenorhabditis elegans
Function: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. Acts as a regulator of mitosis/meiosis required for progression through meiotic prophase during oogenesis and spermatogenesis and for promotion of the entry into meiosis from the mitotic cell cycle. May act by regulating and activating gld-1 mRNA activity in germline.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12239571}.
Interaction partners:
- Defective in germ line development protein 3
- RRM domain-containing protein
- Poly
- Poly
- Poly
- Female germline-specific tumor suppressor gld-1
- DUF3453 domain-containing protein
- Poly
- Fem-3 mRNA-binding factor 2
- Cytoplasmic polyadenylation element-binding protein 3
Sequence:
MVMAQQQKNAERNDEHTRRNRSPSVDSVSRVQQQSGGFAFYNQQSNHQYQQSHPRRTSFSRDGNTGYYNNHSGNKRQTYNNQRGGRSYNHRGNSNYQQNGEYSGNQGCVPKYHQRNQNYPQLQPKYSYFQPHQRPIFNSTQGYGTYSVRRSSPPSPSALSSSTANSTSNRAPTQPPILLRHAEPASDKNHQGSDHEQNHDPKIHLYRSAGTAPGGYTQCPSPYKQPPPQPPSTPSSSDKRIEQQQAEDWPTRFQHPPPQFRRGQDPMPASIELQHKTANQTMPVDIVQTNQQKTVSSYERAAQFRASASELPTDSVDAKHPCFANERMQSALIGISPQLKTQQQSPGIPIQNEAEASAVMKAMRSFQFHNWPQMSHGSYYPMPYHLENQMRPMKSGDQLPLNQQNHNLSGFPAFVGKSSLVGSSLNTRNSSEADPEEMPRIMEKLDDEVTGADHDKTIDENRRRIHKSQEPRIGTEEKALNELPRKANRRNSSCSSISSVSESSSPSALDESTLTKILPTDNFRGGRGFASPSPPTSLLSEPLSRMDVLSEKIWDYHNKVSQTDEMLQRKLHLRDMLYTAISPVFPLSGLYVVGSSLNGFGNNSSDMDLCLMITNKDLDQKNDAVVVLNLILSTLQYEKFVESQKLILAKVPILRINFAAPFDDITVDLNANNSVAIRNTHLLCYYSSYDWRVRPLVSVVKEWAKRKGINDANKSSFTSYSLVLMVIHFLQCGPTKVLPNLQQSYPNRFSNKVDVRTLNVTMALEEVADDIDQSLSEKTTLGELLIGFLDYYANEFNYDRDAISIRQGRRVERAALAVRPKIHSNSEGDKETPPPSSSASTSSIHNGGTPGIPMHHSISNPHFWRSQWRCVCIEEPFTNSNTAHSIYDEMVFEAIKKAFREAHGELQHNHDLDKLMECEPIKASTTNTGAAVFAATYEGERPLAQQPNTIACASLRVLNSIPVSSGPGHYHYQQQSNQNLSRPQRPGSNQGYQMNNNRGFNGNNQQQHQNRRSFNNQSSSNPGNGSTGPRSSRSNENVRDSSRQQNSQKGSSGVSVSKENVASTTGVPVDKKQQNSNRKDDGNRTKRSPMVQSPEPAKTKSEKTPMASSNVSQ
Protein: Internal protein I (IpI) (P03718)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Internal protein I is one of four proteins in a complex that functions in bacteriophage head maturation.
Interaction partners:
Sequence:
MKTFKEFTSTTTPVSTITEATLTSEVIKANKGREGKPMISLVDGEEIKGTVYLGDGWSAKKDGATIVISPAEETALFKAKHISAAHLKIIAKNLL
Protein: 17S U2 SnRNP complex component HTATSF1 (HIV Tat-specific factor 1) (Tat-SF1) (O43719)
Organism: Homo sapiens (Human)
Function: Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation. In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus.
Subcellular location: Nucleus {ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:8849451}. Chromosome {ECO:0000269|PubMed:35597237}. Note=Recruited to DNA damage sites during S-phase following interaction with poly-ADP-ribosylated RPA1. {ECO:0000269|PubMed:35597237}.
Interaction partners:
- Splicing factor 3B subunit 1
- Splicing factor 3A subunit 2
- Probable ATP-dependent RNA helicase DDX46
- U2 small nuclear ribonucleoprotein A'
- Splicing factor 3B subunit 2
- Crooked neck-like protein 1
- U2 small nuclear ribonucleoprotein B''
- Splicing factor 3B subunit 6
- PHD finger-like domain-containing protein 5A
- Small nuclear ribonucleoprotein F
Sequence:
MSGTNLDGNDEFDEQLRMQELYGDGKDGDTQTDAGGEPDSLGQQPTDTPYEWDLDKKAWFPKITEDFIATYQANYGFSNDGASSSTANVEDVHARTAEEPPQEKAPEPTDARKKGEKRKAESGWFHVEEDRNTNVYVSGLPPDITVDEFIQLMSKFGIIMRDPQTEEFKVKLYKDNQGNLKGDGLCCYLKRESVELALKLLDEDEIRGYKLHVEVAKFQLKGEYDASKKKKKCKDYKKKLSMQQKQLDWRPERRAGPSRMRHERVVIIKNMFHPMDFEDDPLVLNEIREDLRVECSKFGQIRKLLLFDRHPDGVASVSFRDPEEADYCIQTLDGRWFGGRQITAQAWDGTTDYQVEETSREREERLRGWEAFLNAPEANRGLRRSDSVSASERAGPSRARHFSEHPSTSKMNAQETATGMAFEEPIDEKKFEKTEDGGEFEEGASENNAKESSPEKEAEEGCPEKESEEGCPKRGFEGSCSQKESEEGNPVRGSEEDSPKKESKKKTLKNDCEENGLAKESEDDLNKESEEEVGPTKESEEDDSEKESDEDCSEKQSEDGSEREFEENGLEKDLDEEGSEKELHENVLDKELEENDSENSEFEDDGSEKVLDEEGSEREFDEDSDEKEEEEDTYEKVFDDESDEKEDEEYADEKGLEAADKKAEEGDADEKLFEESDDKEDEDADGKEVEDADEKLFEDDDSNEKLFDEEEDSSEKLFDDSDERGTLGGFGSVEEGPLSTGSSFILSSDDDDDDI
Protein: Ribosomal RNA processing protein 1 homolog B (RRP1-like protein B) (Q91YK2)
Organism: Mus musculus (Mouse)
Function: Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (By similarity). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (By similarity). Involved in regulation of mRNA splicing. Inhibits SIPA1 GTPase activity. Involved in regulating expression of extracellular matrix genes. Associates with chromatin and may play a role in modulating chromatin structure (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q14684}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14684}. Chromosome {ECO:0000250|UniProtKB:Q14684}. Note=Predominantly located in the nucleolus with a small amount found in the nucleoplasm. Associates with the perichromatin region during metaphase and with cytoplasmic foci during telophase before reaccumulation in the nucleolus during G2. Associates with heterochromatin and euchromatin. {ECO:0000250|UniProtKB:Q14684}.
Interaction partners:
- Probable rRNA-processing protein EBP2
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- WD repeat-containing protein 74
- Ribosome biogenesis protein BRX1 homolog
- Protein MAK16 homolog
- Suppressor of SWI4 1 homolog
- Ribosome production factor 1
- mRNA turnover protein 4 homolog
- Pescadillo homolog
- Ribosome biogenesis protein WDR12
Sequence:
MALAMQSSEFQFAQRLASSEKGVRDRAVRKLRQYLSARTQSDTGSFSQEELLKIWKGLFYCMWVQDEPLLQEELANIISQLIHVVNSLEAQYLFIQTFWQTMNREWQGIDKLQLDKYYMLIRLVLRQSFEVLKRNAWEESQITLFLDILMKEILSPESQSPNGVRTHLIDVYLEELTTVGGAELLADQNLKLIDPFCRIAAKTKDHTLVQTVARGVFEVIVDQSACVPQESVEERKTKEDGSGFPTKALACRKAVSGKKAALDECLRDGVIGSRERDICAALKDSGSPLQFDYKAVADRLLEIANSKSTPPFNRKRLCRLVRKFQDLCEGNGAPLSSAEDNGQRRHKRKRKKLLESEKGDTVSPAAEEDSGGHIHKKKRKKRKRSHFQPDTQNLDAVAVPKVPDSESEPDTAQRQAPCGQACVTEPTAEAVSSIGENSSKPTPVMPIHNKRKRPRKKKLRAHKEICKSTTLPQEDMSKNDAVSGHSQSSAAHISSSEGVQAQKRKRKLGALPDSSSDLPVQKSGTPTSPVEGKDGQTTLPRCKRSQKKTASSTLDPCDPSSQKPAISKKKKKTMKLMSNGVLESNPGQIQALGSNRTLKKPLKTEDDFVKFDTRFLPKPLFFRKAKNSSATRPQGPAGQLNKTPSSSKKVTFGLNRNMTAEFKKTDKSILVSPTGLSRVAFNPEQRPLHGVLKTATSSPASTPLSPMRLPATTPKRRPRAADFF
Protein: CBTF122 protein (Interleukin enhancer-binding factor 3-A) (Q2TAV5)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRPMRIFLNDDRHVMAKHSVVYPTQEELEAVQNMVSHTERALKAVSDWIDQQEKDCSGEQEQPMAEETETTEEGKDSEMKTGENPTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCRDKPTISLLKRVADNLVLQFETVSEDKYEVIQNIREALIVVKSTKEPPLTLNIRLTSPLVREEMEKLSAGETLTVSDPPDVLDRHKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWEPLRGWPLELLCEKAIGTANRPMGAGEALRRVLECLSSGILMPDGSGLYDPCEKDASDALEHLERQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKTKVETPVIDYTVQIPPSTTYAMPPLKRPIEEDGDDKSPSKKKKKIQKKDEKSEPPQVMNALMRLNQLKPGLQYKLISQTGPVHAPVFTMSVEVDDKTFEASGPSKKTAKLHVAVKVLQDMGLPTGMEEKEEGTDESEQKPVVQTPAQPDDSAEVDSAALDQAESAKQQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGVKFQGSGSNKKVAKAYAALSALEKLFPDYTMYTEAPKKKRPPMMPRGGPKFAGKHNQGFGMMYSEVPPPQAMRGRGRGGMNRGRGRGRGGFGGGYMNSGGYGGGYGGNYNYQTSATAGYSQFYSNGGASGNAGGGGAGTGGYSSYYQGDSYSAPTPPKPFVNKKPPPPQQQQQQQPPPQHASNPPKPSYNQGYQGHQGGQQQQQQQQQQQTYNQNQYSNYGPPQKQKGGYNQGAQGAGSGGSYNYSNSYTGGTAPGYGSGEGAGGRGGSSYTAPSSGYNTGAHSGYGGASSTSTYQGYTQSNYNQGPPGQNYSGPPNNYQQPQGGAGSYSRNTEHNMSYQYR
Protein: Anaphase-promoting complex subunit 10 (20S cyclosome/APC complex protein apc10) (O42971)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Acts as a positive regulator of the anaphase promoting complex (APC)-cyclosome. Involved in G1 cell cycle arrest in response to nitrogen starvation. Required for ubiquitination and degradation of the mitotic B-type cyclin, cdc13.
Interaction partners:
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 4
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 11
- Mitotic spindle checkpoint component mad2
Sequence:
MAQIRQEALKKQKSETQKSTEGFVDIGNLAQWTCSSEKSGFPIRLVRDDNIDTYWQSDGSQPHTIHIKFVKRVSIKYVSMYLQYTLDESYTPSTLRISAGTGFQDLEIVTTVQVEEPTGWVHVPVGDFGRNGLLDVHLIQIKILANHQSGKDSHVRLIKIYAPEIEQPAIAVDEIPYTSLQFISRNQLR
Protein: Beaten path (FI23920p1) (Q94534)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRFPQNAYQTALTTILLALTLEMTAALRDVRVRVPHAVRRSEKAILKCFYDIEDDSLYSVKWYKGRREFYRYTPKETPPMKVFHFPGVKVRRVSSNESQVVLDAVTMATSGKYSCEVSADAPSFHTLIAAAELEVIETPHNAPFITGIRPRYRVGDILRGNCTSRHSRPAANLTWTVNNEEVNPALVRHHKILRDARNDMETAVVGIHFVVTDQHFDNGKLKLRCSAQLHDVYWKTTEKIILETDLFPKHGNGANGNHVNPDDFYDQYALHEDHLHNKKNSYLTQLQGEEDDGTEGGLGDGGAAWRGAGSSSSRLSPSSSQSCWMVGGSLMAVLSWTLARQLVSPLQAMMTKTGGATCNMSGRCASRRTRAHGMRVSATKQKQKQRQMQQEHRKSCLRVSKSSWKGRGYVCGCGFGRINSRCIRQLT
Protein: Mitochondrial import inner membrane translocase subunit tim23 (Q9USM7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit tim44
- Mitochondrial import inner membrane translocase subunit tim17
- Mitochondrial import inner membrane translocase subunit tim50
- Mitochondrial import inner membrane translocase subunit tim14
- Mitochondrial import inner membrane translocase subunit tim21
- Cytochrome c oxidase subunit 4, mitochondrial
- Mitochondrial import inner membrane translocase subunit tim16
- Mitochondrial import inner membrane translocase subunit tim22
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- Mitochondrial import inner membrane translocase subunit tim9
Sequence:
MSWLFTRNKEEEPTSKIDSSELQVPTEATASDILSGSEFDPAKLHPLADLDKPLDYLLIEEDALSTLPGDSMAIPSRGWQDDLCYGTGTSYLSGLAIGGLWGLNEGMKKTKDITSTRLRLNGILNGVTRRGPFVGNSLGVLALVYNGINSLIGYKRQKHGWENSVAAGALTGALYKSTRGLRAMAISSSLVATAAGIWTLAKRSFTKRLN
Protein: Post-GPI attachment to proteins factor 4 (Post-GPI attachment to proteins GalNAc transferase 4) (Transmembrane protein 246) (Q9BRR3)
Organism: Homo sapiens (Human)
Function: Golgi-resident glycosylphosphatidylinositol (GPI)-N-acetylgalactosamine transferase involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for the initial step of GPI-GalNAc biosynthesis, transfers GalNAc to GPI in the Golgi after fatty acid remodeling by PGAP2.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:29374258}; Multi-pass membrane protein {ECO:0000269|PubMed:29374258}.
Interaction partners:
Sequence:
MSTSTSPAAMLLRRLRRLSWGSTAVQLFILTVVTFGLLAPLACHRLLHSYFYLRHWHLNQMSQEFLQQSLKEGEAALHYFEELPSANGSVPIVWQATPRPWLVITIITVDRQPGFHYVLQVVSQFHRLLQQCGPQCEGHQLFLCNVERSVSHFDAKLLSKYVPVANRYEGTEDDYGDDPSTNSFEKEKQDYVYCLESSLQTYNPDYVLMVEDDAVPEEQIFPVLEHLLRARFSEPHLRDALYLKLYHPERLQHYINPEPMRILEWVGVGMLLGPLLTWIYMRFASRPGFSWPVMLFFSLYSMGLVELVGRHYFLELRRLSPSLYSVVPASQCCTPAMLFPAPAARRTLTYLSQVYCHKGFGKDMALYSLLRAKGERAYVVEPNLVKHIGLFSSLRYNFHPSLL
Protein: Farnesyltranstransferase (A0A1D8PNS6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Diphosphomevalonate decarboxylase
- Farnesyl pyrophosphate synthase
- Squalene synthase ERG9
- Isopentenyl-diphosphate delta-isomerase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- Trans-hexaprenyltranstransferase
- Alkyl transferase
- Alkyl transferase
- ditrans,polycis-polyprenyl diphosphate synthase [
Sequence:
MQLDINKLIQPTEAYVPESSDPIVQPYTYISETPSNNQNVRTRFLHAFNDLFYKISDESLLARISEIISVFHNSSLLIDDIEDDSKYRRGVPVAHVKYGIPTTINCGNLMYFVALQQAQQLSGPHGSMEVKFKSSQILIDELLNLHRGQGLDIYWRDYLKKLEKLPDVEEYLEMIKDKTGGLFRLAIKLLSLYSDVKENDQLISLANLMGILYQVRDDYLNLVDAKYSAMKGTTCEDLIEGKLSLPILHCLRTTKDSPVHKILYDYDSSSDRVSQNSLIDLSLSFMKNESKSLEYTLNLIKVLEKKLRQLILKYPESENSALLKIVERLCDL
Protein: Talanin (Q70YC4)
Organism: Homo sapiens (Human)
Function: May play a role in uric acid excretion.
Interaction partners:
Sequence:
MSALGQITITVSRCWNTERNQTDKNPCLHGAYLQLRETVKNKSTHLKKPLMKQAPPWKDHLTFQPLHPAERKTQVWRWQSGNSSDLETTSSASPWPTGSNRDVVLNTLAESCCGLSELITAPPYAGVSIQGFSQIWVLFPFCGGTFHHNEKDVLGLQDFERESVSTSQSRNISLLTLGQLQNCVIGKLTIIDLLTEHLLGVRHGVICFPWGLPSSS
Protein: S-adenosylmethionine synthase isoform type-2 (AdoMet synthase 2) (EC 2.5.1.6) (Methionine adenosyltransferase 2) (MAT 2) (Q3THS6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Interaction partners:
- Methionine adenosyltransferase 2 subunit beta
- Methionine synthase
- S-adenosylmethionine synthase isoform type-1
- Betaine--homocysteine S-methyltransferase 1
- S-adenosylmethionine decarboxylase proenzyme 1
- S-adenosylmethionine decarboxylase proenzyme 2
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- DNA
- DNA
- DNA
Sequence:
MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAIDYQKVVREAIKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
Protein: Candida glabrata strain CBS138 chromosome H complete sequence (Q6FS39)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Heat shock protein homolog SSE1
- Candida glabrata strain CBS138 chromosome H complete sequence
- Hsp70 nucleotide exchange factor FES1
- Candida glabrata strain CBS138 chromosome J complete sequence
- Peptidyl-prolyl cis-trans isomerase D
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Endoplasmic reticulum chaperone BiP
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MVKETKLYDLLGISPSANEQEIKKGYRKAALKYHPDKPTGDTEKFKEISEAFEILSDPQKREVYDQYGLEAARNGGPAFGGAGGFRGGGFSSAGGAHAFSNDDAFNIFSQFFGGSSPFGAADDGFSYSSFGGMPGGMGGMHGGMGGGMHGGMGGGMGGMGGMPGGFRSASSPQPEEEVVPVNLSVSLEDLYTGKKKTFMIGRKGPNGAPEKTQVDIQLKPGWKAGTKITYKNYGDYNPATGRRKTLQFIIQEKKHPFFTRDGNDLIYTLPLTFKESLLGFNKTIQTIDGRTLPVSRIQPIQPSEKSTYPGQGMPIPKTPGQRGDMIVNYKVDYPISLTDKQRQAIDENF
Protein: long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Q960I0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYTSGSTGTPKGVLLSHKNCIATMKGFVDMVPIYPDDVLIGFLPLAHVFELVAESVCLMTGVPIGYSTPLTLIDTSSKIKRGCKGDATVLKPTCMTSVPLILDRISKGINDKVNSGSAFKKSLFKFLYQYKVKWVQRGYKTPLIDKLVFKKVAKLMGGKVRIIMSGGAPLSADTHEQIKTCLCLELIQGYGLTETTSGATVMDYRDMTYGRTGGPLTVCDIRLVNWEEGNYRVTNKPYPQGEVLIGGECVSQGYYKLPGKTNEDFFEEDGQRWFKTGDIGEIQADGVLKIIDRKKDLVKLQAGEYVSLGKVESELKTCGIIENICVYGDPTKQYTVALVVPNQNHLEELAQKHGLGDKSFEELCSSPIIEKAILKEIAEHARKCKLQKYEVPAAITLCKEVWSPDMGLVTAAFKLKRKDIQDRYQHDINRMYAS
Protein: Response regulator 4 (Q9FRZ1)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MTVLDAESRFHVLAVDDSIIDRKLIEMLLKSSSYQVTTVESGNKALELLGLRDNGAEDASPPSSSSSSSSSSSPDHQEIDVSLIITDYCMPGMTGYDLLKRVKGSSSLKDIPVVIMSSENVPARISRCLQDGAEEFFLKPVKPADMKKLKSHLLKRKQPKQKNKPQAQAVESPEQQLDPHPQPVHELELEEAAADRNGVNKRKAAAMEEGLTVVVTAPESTKPRRLSTSSLTVET