wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphoserine phosphatase (PSP) (PSPase) (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) (Q99LS3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L-serine to L-serine. L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator. May also act on O-phospho-D-serine.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78330}.
Interaction partners:
- Phosphoserine aminotransferase
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Cystathionine beta-synthase
- Alanine--glyoxylate aminotransferase
- L-serine dehydratase/L-threonine deaminase
- Serine racemase
- D-3-phosphoglycerate dehydrogenase
- Serine dehydratase-like
- Transcription termination factor 2
Sequence:
MVSHSELRKLFCSADAVCFDVDSTVIREEGIDELAKFCGVEAAVSEMTRRAMGGALPFKDALTQRLALIQPSRDQVQRLLAEHPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVAAKLNIPTTNVFANRLKFYFNGEYAGFDEMQPTAESGGKGKVIRFLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
Protein: Uncharacterized protein (O25214)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Quinone-reactive Ni/Fe hydrogenase, large subunit
- Co-chaperone DjlA N-terminal domain-containing protein
- Conserved hypothetical integral membrane protein
- Uncharacterized protein
- Oligoendopeptidase F
- Fumarate reductase flavoprotein subunit
- LUD domain-containing protein
- Fumarate reductase iron-sulfur subunit
- DUF115 domain-containing protein
Sequence:
MSVLKLHVKVFRFETNKDYNPAYESYFLEYQEDQYLLDLLKQLKGVSYNENIALKINQIAVFEDAKVSDLVAFFSKEWVLDPLSKRYALKDLMIDEKAVLKNYEDFFKQIPYITKGEKEELEKFIQINFINPQTNPKYLGDGFFLYVKWLMKRYPTERNRLLEMISQPESGVMNFLSVVHYLYKNDDNIDHEIYELQEILTNSKIKPWKDFSKNLLSLFQYPSNSPKTPNPPKTCALFNAYAKHLDVQSLLKSAKLYLEKMGQKIIDLPFCYDGGYYGKIISTHDFLTASAYNLALAKANGVSLIFCEEDAYLNILHAKEVLDNNPEIINSVNEKLKKYQLVYEKGVEVVYLNEWVNEFLAWELKSPFDAFLGAEFSRIKRSDHFFNKIHLKAPHFLESFQNYAPLLEVNEVSGLLQCAHLRYLGIDLGADFLIVHSLGLFHAFENLSLKASKVYKRDNDNTPTLFLPQIALMAMGEKNTQALGLDAHYHKVTFI
Protein: Chromatin structure-remodeling complex subunit rsc58 (RSC complex subunit rsc58) (Q10412)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Chromatin structure-remodeling complex subunit rsc4
- SWI/SNF and RSC complexes subunit ssr3
- Chromatin structure-remodeling complex subunit rsc9
- SWI/SNF and RSC complexes subunit ssr2
- Chromatin structure-remodeling complex subunit rsc1
- Chromatin structure-remodeling complex subunit sfh1
- Chromatin structure-remodeling complex subunit rsc7
- SWI/SNF and RSC complexes subunit ssr1
- Chromatin structure-remodeling complex subunit snf21
- SWI/SNF and RSC complexes subunit arp42
Sequence:
MNAESCSLILSYISSAPAGNLVLNCTATTNKQTLEANLKSAVYQRYPEFLEDWTNVCVHIIHSYFPKDADYWNVDKLYTSVNRITTLEQSKVVGKEIKNGFTFDAENSTASLENDLQPQFRSHALFMVGSAGPLFSSTARTSRLDSRLPDGGIIAKPVALLPTPSVANSQEYTLDKLSPPSTAKPPASVIEFNPSLAKLPTVKYLQSGPFSSIAPYKNSSSSVIPDSSFHSVACYRASSHYKEAPVEKSIDIDIIQNNLSLLEEDSWTSVPIQGELVELNKLLQHLQLLQNQRITSHNVLSDEERQISVQVQNLILKLAKDYDMSPEDFLMDDFTLSLTQYGAFYRGTLPLSAQPLELPSQQLLRSQSNAALRSNSLSMNGSLSPSSTNVPLQSYRRTTKSRR
Protein: Knockout (O18363)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGTKSPGGPQRCRLILQRCLAIQLIKPGHTPEDFWMYDSGYMIFQNFLAANAQCWWNGPLTAATRALKYAGHVAPGMLLVTAEPCALEVLRGAFARSVLKPPATYVISSVGDIDDCIVTPTVQGQFTPLPEALCDVIMDLTAEGQSATIEHVRSKLGSRFPHMTTPATEVIYDSLAQLMQEQKIYQTSKGYFIFTPERRRSRSRPRSNHHQLNGSLAYGHLAEEEQQHGDDVVPQEARTMLMSNSEALHSLYGEISTERDGDLTHQCIQTNLADVICGGNPNDKIIYPRAAKRRSASFPTPRSLERRHSLRLFGSSKRLQRCASTRSLSKTYAQTLNTTDSSSSEYQSTDSSSPKKGSLLSRLFRRSGRAKQRQIETYSAQFPPAEWFNTRAVHLHSVGTQTAEHDMPVAHTLSNSTFYDGSELSQRSSTLPRRHRRHMSSESTFLISSRDCSPIRRRSPVYCSSSLPRSTQSIPATTAKTNHSSRLSHGHGGSVTPTPPKTAQKSVIGKHIFESSPSRSATLKATAAKRHTDGLIINSCLDNKATYRSLQSSGPSSLESCKTTSMLASGPSSIDSGKVSFSQKTSGHSSLDSQCSTNTAVIAPPSNSNNGSSRSILLLNGSPRGTPRHQAMRARVAEAQAQRQRASTPSRIMEEIYPAGGSNGVPTSNSNNSITLQVTTSNGNQSIPSTKIFVQNSPVRSVITLENGKMLENSNVFIINNETMTNEKGEIIKKTLSKQTSAAPAATSTPVKPETVSEQPLSETEANSETCDSISFISECSPESTCAVEPETPVYDGGKYAKNTNNDATMNNSRKLCLQLANGIAYKNNVLKNESQPNSPSADAPLKMAALAKQDFEIAGSVGNLNFYERVRRMWVPHRATT
Protein: BOS complex subunit NOMO1 (Nodal modulator 1) (pM5 protein) (Q15155)
Organism: Homo sapiens (Human)
Function: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17261586, ECO:0000269|PubMed:36261522}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- BOS complex subunit NCLN
- Pyridoxal-dependent decarboxylase domain-containing protein 1
- Bifunctional apoptosis regulator
Sequence:
MLVGQGAGPLGPAVVTAAVVLLLSGVGPAHGSEDIVVGCGGFVKSDVEINYSLIEIKLYTKHGTLKYQTDCAPNNGYFMIPLYDKGDFILKIEPPLGWSFEPTTVELHVDGVSDICTKGGDINFVFTGFSVNGKVLSKGQPLGPAGVQVSLRNTGTEAKIQSTVTQPGGKFAFFKVLPGDYEILATHPTWALKEASTTVRVTNSNANAASPLIVAGYNVSGSVRSDGEPMKGVKFLLFSSLVTKEDVLGCNVSPVPGFQPQDESLVYLCYTVSREDGSFSFYSLPSGGYTVIPFYRGERITFDVAPSRLDFTVEHDSLKIEPVFHVMGFSVTGRVLNGPEGDGVPEAVVTLNNQIKVKTKADGSFRLENITTGTYTIHAQKEHLYFETVTIKIAPNTPQLADIIATGFSVCGQISIIRFPDTVKQMNKYKVVLSSQDKDKSLVTVETDAHGSFCFKAKPGTYKVQVMVPEAETRAGLTLKPQTFPLTVTNRPMMDVAFVQFLASVSGKVSCLDTCGDLLVTLQSLSRQGEKRSLQLSGKVNAMTFTFDNVLPGKYKISIMHEDWCWKNKSLEVEVLEDDMSAVEFRQTGYMLRCSLSHAITLEFYQDGNGRENVGIYNLSKGVNRFCLSKPGVYKVTPRSCHRFEQAFYTYDTSSPSILTLTAIRHHVLGTITTDKMMDVTVTIKSSIDSEPALVLGPLKSVQELRREQQLAEIEARRQEREKNGNEEGEERMTKPPVQEMVDELQGPFSYDFSYWARSGEKITVTPSSKELLFYPPSMEAVVSGESCPGKLIEIHGKAGLFLEGQIHPELEGVEIVISEKGASSPLITVFTDDKGAYSVGPLHSDLEYTVTSQKEGYVLTAVEGTIGDFKAYALAGVSFEIKAEDDQPLPGVLLSLSGGLFRSNLLTQDNGILTFSNLSPGQYYFKPMMKEFRFEPSSQMIEVQEGQNLKITITGYRTAYSCYGTVSSLNGEPEQGVAMEAVGQNDCSIYGEDTVTDEEGKFRLRGLLPGCVYHVQLKAEGNDHIERALPHHRVIEVGNNDIDDVNIIVFRQINQFDLSGNVITSSEYLPTLWVKLYKSENLDNPIQTVSLGQSLFFHFPPLLRDGENYVVLLDSTLPRSQYDYILPQVSFTAVGYHKHITLIFNPTRKLPEQDIAQGSYIALPLTLLVLLAGYNHDKLIPLLLQLTSRLQGVRALGQAASDNSGPEDAKRQAKKQKTRRT
Protein: E3 ubiquitin-protein ligase BRE1-like 2 (EC 2.3.2.27) (Protein HISTONE MONOUBIQUITINATION 2) (AtHUB2) (RING-type E3 ubiquitin transferase BRE1-like 2) (Q9C895)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that monoubiquitinates H2B to form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and maybe H3K79me. It thereby plays a central role in histone code and gene regulation. Forms a ubiquitin ligase complex in cooperation with the E2 enzyme UBC2/RAD6.
Subcellular location: Nucleus {ECO:0000269|PubMed:17329563}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 1
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin-conjugating enzyme E2 3
- Histone H2B.6
- Histone H2B.8
- Histone H2B.5
- Histone H2B.9
- Histone H2B.3
- Histone H2B.4
- Histone H2B.1
Sequence:
MENQESDEPMQKKPHLLDSVSPNSMARNSSPSHPIAKSVSFFDCDFSLLCLRLVDYEIDVDATVLQLQNQKLVQQLDLQKKQLYDVESKIQELQLNQTSYDDELISVNQLWNQLVDDLILLGVRAGANQEALNYLDIVDKKRVPPCAADETFLCRLLQVDSLDTSKSDEVVRKVEEALALRHSSTMELMGLFENTIDTQKTKAESISQSLHAVKSTEDATIQLSSINDLMKEESKNLREMIDALHVRHKEHSEQIQAYISSHSTDQSELKHLKGQLEEIKAELEENRRKLITLKMQKDAACEGHVTSPAIANGSLSPEKPVDKTKLRELKDSIDEIKIMAEGRLSELQASQEYNLSLSRQCQDIENELKDDQYIYSSRLYSLINDRIHHWNAELDRYKILTEAIQAERSFVMRRDKELNLRAESLEAANHKTTTVGSRIEVLEKKLQSCIIEKNGLELETEEAIQDSERQDIKSEFIAMASTLSKEMEMMEAQLKRWKDTAQDALYLREQAQSLRVSLSNKADEQKGLEDKCAKQMAEIKSLKALIEKLLKEKLQLQNLASICTRECNDDRGLAEIKDSQRKAQAQAEELKNVLDEHFLELRVKAAHETESACQERLATAKAEIAELRTQLDLSEREVLELKEGIKVKEQEAEASIAEMETIGQAYEDMQTQNQHLLQQVAERDDYNIKLVSESVKTKHAYNTHLSEKQVMEKQLHQVNASVENFKARIAHNEEQMKGCFSEAYKLIQEDRHLVISLETTKWEVADADKEFRWLKSAVSSSEKEYEQISRRTDDIKLELDDERREKKKLEEELMELNKELEELGSESVEAAIVRLQEEVKNCKNILKCGVCFDRPKEVVIVKCYHLFCQQCIQRSLEIRHRKCPGCGTAFGQNDVRLVKM
Protein: Platelet-derived growth factor C (PDGF-C) (Fallotein) (Spinal cord-derived growth factor) (SCDGF) (VEGF-E) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)] (Q9NRA1)
Organism: Homo sapiens (Human)
Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16443219}. Secreted {ECO:0000269|PubMed:10806482, ECO:0000269|PubMed:10858496, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:15061151, ECO:0000269|PubMed:15372073, ECO:0000269|PubMed:15911618}. Nucleus {ECO:0000269|PubMed:16443219}. Cytoplasmic granule {ECO:0000269|PubMed:15061151}. Cell membrane {ECO:0000269|PubMed:16443219}. Note=Sumoylated form is predominant in the nucleus (PubMed:15247255). Stored in alpha granules in platelets (PubMed:15061151). {ECO:0000269|PubMed:16443219}.
Interaction partners:
- Platelet-derived growth factor receptor alpha
- Platelet-derived growth factor receptor beta
- Vascular endothelial growth factor receptor 2
- Platelet-derived growth factor subunit B
- Platelet-derived growth factor subunit A
- Vascular endothelial growth factor receptor 3
- Vascular endothelial growth factor receptor 1
- Platelet-derived growth factor D
- Epidermal growth factor receptor
- Insulin-like growth factor 1
Sequence:
MSLFGLLLLTSALAGQRQGTQAESNLSSKFQFSSNKEQNGVQDPQHERIITVSTNGSIHSPRFPHTYPRNTVLVWRLVAVEENVWIQLTFDERFGLEDPEDDICKYDFVEVEEPSDGTILGRWCGSGTVPGKQISKGNQIRIRFVSDEYFPSEPGFCIHYNIVMPQFTEAVSPSVLPPSALPLDLLNNAITAFSTLEDLIRYLEPERWQLDLEDLYRPTWQLLGKAFVFGRKSRVVDLNLLTEEVRLYSCTPRNFSVSIREELKRTDTIFWPGCLLVKRCGGNCACCLHNCNECQCVPSKVTKKYHEVLQLRPKTGVRGLHKSLTDVALEHHEECDCVCRGSTGG
Protein: Guanine nucleotide-binding protein alpha-1 subunit (GP-alpha-1) (P18064)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits a fast rate of basal nucleotide exchange. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Together with GCR1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate (IP(3)) as a second messenger. Promotes abscisic acid (ABA) responses in guard cells. Involved in the blue light (BL) signaling. Together with GCR1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Modulates root architecture (e.g. lateral root formation). Negatively regulated by RGS1. In collaboration with CAND2/PMTR1, regulates the melatonin-mediated stomatal closure involving H(2)O(2) and Ca(2+) signals.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14500984, ECO:0000269|PubMed:17158913}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- Guanine nucleotide-binding protein subunit gamma 1
- Guanine nucleotide-binding protein subunit gamma 2
- Regulator of G-protein signaling 1
- Guanine nucleotide-binding protein subunit gamma 3
- G-protein coupled receptor 1
- Phospholipase D alpha 1
- Pirin-1
- Protein THYLAKOID FORMATION 1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
Sequence:
MGLLCSRSRHHTEDTDENTQAAEIERRIEQEAKAEKHIRKLLLLGAGESGKSTIFKQIKLLFQTGFDEGELKSYVPVIHANVYQTIKLLHDGTKEFAQNETDSAKYMLSSESIAIGEKLSEIGGRLDYPRLTKDIAEGIETLWKDPAIQETCARGNELQVPDCTKYLMENLKRLSDINYIPTKEDVLYARVRTTGVVEIQFSPVGENKKSGEVYRLFDVGGQRNERRKWIHLFEGVTAVIFCAAISEYDQTLFEDEQKNRMMETKELFDWVLKQPCFEKTSFMLFLNKFDIFEKKVLDVPLNVCEWFRDYQPVSSGKQEIEHAYEFVKKKFEELYYQNTAPDRVDRVFKIYRTTALDQKLVKKTFKLVDETLRRRNLLEAGLL
Protein: Shuttling pre-60S factor ECM1 (Extracellular mutant protein 1) (Protein SIM1) (P39715)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Pre-ribosomal factor involved in 60S ribosomal protein subunit export from the nucleus.
Subcellular location: Nucleus, nucleolus. Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm and is re-imported by the KAP123 karyopherin.
Interaction partners:
- Probable metalloprotease ARX1
- Bud site selection protein 20
- Nucleolar GTP-binding protein 2
- Ribosome assembly factor MRT4
- Ribosome biogenesis protein RLP24
- Nucleolar GTP-binding protein 1
- Cytoplasmic 60S subunit biogenesis factor REI1
- Ribosome biogenesis protein NSA2
- Ribosomal RNA-processing protein 1
- Ribosome biogenesis protein 15
Sequence:
MWEQRRQKVVFSLTILVRYRLKQSMAKKISKNSRAARQSDALEPEVKDLSELPRAEKTDLTNILIRTAAKNEALLEAKISKKANKSKRGKKLNKKALEDKLANSISSMDRDRLVKALNFTNRLDGKIAKSISRAKYIQNTRKAGWDSTNETIKKELAFLNGGLSVQAKSASEGNAEKEDEEIPEVFDSLAEDNTVQKTPTNRFGVLPDDVEE
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (B3DKP1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000311}.
Interaction partners:
- Vascular endothelial growth factor A-A
- Vascular endothelial growth factor C
- C-fos induced growth factor
- Placenta growth factor
- Neuropilin-1a
- Protein tyrosine kinase 2ab
- Angiopoietin 2b.
- Vascular endothelial growth factor Ab
- Platelet-derived growth factor beta polypeptide a
- Angiopoietin 1.
Sequence:
MFDILFVMIFGLSGRVLTKDTDTKGRFSSPVLDVTEKQLVIERNQTLQLSCRGRWELQWVLPSGVPKLYPDTHIVNTQCGKKSNQYCSRLTLSPALTQHTGSYRCRYRQKERKQTSVYIYITDSQRPFVKVQSEIPDVVYMKEGEPLVFPCRVTNPDAKVSLVKFPLHRITPDHRNIIWNSRQGFIIRSPTFFYIGLFSCETIVDGVKYTNKFLTHRPVNKILDVYLNSTGLVHTLQGEMLALNCTVTAEWNSRVSISWTYPQKANGSAIISKRISRSRSNMLFYSVLTIPSLSKADKGLYKCQVTSGPSKRETNTTVIVYDQPFIRLKHRNGPVVQAFAGQKSFRLTPKLKAFPAPEIIWLKDGMVAAERCSRYHVDGFSLVIRDVAEEDAGIYTILTGIQQYGLFQNLTITLVVNVKPQIGEKSVSSQQPGTVQRGSRQALHCTSHGVPPPQIQWLWHPCPPKGLCEKPPPSSWTAVRKKTGVTSTHNPILTISHRQEVLEGKNKTVGVLTVGEALVSGIYRCVTSNILGRDELDIPFYVTDVKEGLVASLVEEPREGGDLRLLCIANRHLYSDLSWSRITSQITVWDEASGLDGELTEGQFSHTLHFGLKNLTARDSGTYRCSATHLLTGEHIHLDTAVEVTVLQAPVLLGNLSDHTVNVSNSITLHCPARGVPQPHITWYKNQRKLQQVSGIMLFPEEGTLHIDRITVEDQGFYTCQATNQRGSVESSAYIWVQNSSESLSLEIPTLACTCVVATLFWLLLTLLIRKLKHPNSDNGKAEYLPIILHPGEEPLVEHCDRLQYDPAKWEFPRDRLKLEKPLGRGAFGRVMQASAVGIGNSASCTTVAVKMLKDGATPSEHKALMTELKILNHIGHHINVVNLLGACTKSGGPLMVIVEYCQFGNLSAYLKSKREVFLLNRVNKEEEGVMKEGCKGRLTSVSSRQSNASSGFSEERGEISEEDSDCLSELSDPLLLEDLISYSFQVARGMEFLASRKCIHRDLAARNILLSNNNVVKICDFGLARDLYKDPDYVRNGDARLPLKWMAPESIFDKVFTTQSDVWSYGVLLWEIFSLGASPYPGLNMDEEFCRRLKHGTRMCSPQYSTPEIYSIMCACWENNPEDRPSFTTLVEILGDLLQTCVQQDGKDYIPLNAFKSGEGHTITTHLNQRDISQKALGNSSYISPGKIKAMSTFEDLHKEIPDDEQSDSGMVLPSEELIQVKWTDRFKTKNITKFFSRGQSQPRLSSAPCCSDQTALPPPHYEGDLLYPSF
Protein: DNA-directed RNA polymerase III subunit RPC10 (RNA polymerase III subunit C10) (DNA-directed RNA polymerases III 12.5 kDa polypeptide) (RNA polymerase III subunit C11) (O13896)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P32529}.
Interaction partners:
- DNA-directed RNA polymerase III subunit rpc5
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase III subunit rpc4
- DNA-directed RNA polymerase III subunit rpc1
- DNA-directed RNA polymerase III subunit rpc9
- DNA-directed RNA polymerase III subunit RPC2
- Probable DNA-directed RNA polymerase III subunit rpc6
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I and III subunit RPAC2
Sequence:
MQFCPTCGNHLIVAVDEEGRNAFDCRTCPYHFPISTFLYSRHEFAQKEVDDVLGGEEAFESNQQTEVTCENTKCDNNRAYFFQLQIRSADEPMSTFYRCTKCKFQWREN
Protein: Single-stranded TG1-3 DNA-binding protein (Meiotically up-regulated gene 187 protein) (Q9HEQ9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds single-stranded telomeric sequences of the type (TG[1-3])n in vitro. Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Chromosome, telomere {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MMSAEETVTQNAPNTVQDQVEASVDAAVHASAEQSNTPAQQADDFRVFVGRLSTSTKKSEIRSLFETVGTVRKVTIPFRRVRRGTRLVPSGIAFVTFNNQEDVDKAIETLNGKTLDDREIVVQKARPVQEQPIKDRKKSKNKNGEEPETSTSVENAESAKGSSDENEANTATAPSSNEANGVDKKQNEIKGKGGSGKNKAKPLPPNSIYVSGLSVTLTNEGLKEMFDAYNPTRARIAVRSLPPYIIRRIKLRGEQRRGRGFGFVSFANAEDQSRAIEEMNGKQVGDLTLVVKSAVFREDKQNDENEKNENEPIEASESAPTNVSDSTEPKASEVDSEEKSGVTASAITA
Protein: Cleavage stimulation factor 50 kDa subunit (Q387U0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Suppressor of forked domain-containing protein
- Cleavage and polyadenylation specificity factor subunit, putative
- RNA-binding protein, putative
- RNA-binding protein, putative
- C3H1-type domain-containing protein
- Uncharacterized protein
- Cleavage and polyadenylation specificity factor-like protein, putative
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Sequence:
MSGENLNKSMSAERVAGSLSVGHGVDHGSRKRARSICLKQNFSRLLYQMVIRQLHHDGFLAAASAVADATNVVVPRLEENADRLSKVVSWGLAVEESSVVEIENFFKFEVVERYLSASRVYMPLHLSESARVGSMAYRMRERFITSSLGGVVRRLAFSSDGSLIACGGTDGLCAIFSLNTIEDLSALEEVRQEQHFNGLDGSNPSNIGVGNASNKITELAEARRFHEHTHSVEAISFHPTKQLLVTGGFEGDLYIRDYSQPDNHVVHKLRDAFPVRSAVFHPSGEYVLYATDHTTPRLLNLRSGSVVAPVAHSDNAAATCVTAMAGGKGVARGASQRKGCDAGHAAALCDVDFSPDGRTFASCGLDGSLIVYDGVSSRIVAKVNNAHSSVPVTSVKFSRTGNILLTAGMDSVARLWDLRRGDGGWGCTEVMSFGEPGKCNHRSFRASFSCNESHVLSQDTSLFAIHAHCVYTGDTSYTLTVPNHMQRGFAPAPFSNVVVSGGDDSRMRLWTPAWTTA
Protein: DNA polymerase alpha subunit B (DNA polymerase I subunit B) (DNA polymerase alpha:primase complex p86 subunit) (Pol alpha-primase complex p86 subunit) (DNA polymerase-primase complex p74 subunit) (P38121)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of DNA polymerase alpha, which in a complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL12 may play an essential role at the early stage of chromosomal DNA replication by coupling DNA polymerase alpha to the cellular replication machinery (By similarity). Interacts with MCM10.
Subcellular location: Nucleus.
Interaction partners:
- DNA polymerase alpha catalytic subunit A
- DNA primase small subunit
- DNA primase large subunit
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon subunit B
- DNA polymerase delta small subunit
- DNA polymerase zeta catalytic subunit
- DNA polymerase epsilon subunit D
- Replication factor A protein 2
Sequence:
MSGSIDVITHFGPDADKPEIITALENLTKLHALSVEDLYIKWEQFSNQRRQTHTDLTSKNIDEFKQFLQLQMEKRANQISSSSKVNTSTKKPVIKKSLNSSPLFGLSIPKTPTLKKRKLHGPFSLSDSKQTYNVGSEAETNEKGNSSLKLEFTPGMAEDAVGDSAPLSHAKSSDAKTPGSSTFQTPTTNTPTTSRQNVPAGEILDSLNPENIEISSGNPNVGLLSTEEPSYNQVKVEPFYDAKKYKFRTMRQNLQEASDVLDDQIESFTKIIQNHYKLSPNDFADPTIQSQSEIYAVGRIVPDSPTYDKFLNPESLSLETSRMGGVGRRVRLDLSQVNELSFFLGQIVAFKGKNANGDYFTVNSILPLPYPNSPVSTSQELQEFQANLEGSSLKVIVTCGPYFANDNFSLELLQEFIDSINNEVKPHVLIMFGPFIDITHPLIASGKLPNFPQFKTQPKTLDELFLKLFTPILKTISPHIQTVLIPSTKDAISNHAAYPQASLIRKALQLPKRNFKCMANPSSFQINEIYFGCSNVDTFKDLKEVIKGGTTSSRYRLDRVSEHILQQRRYYPIFPGSIRTRIKPKDVSTKKETNDMESKEEKVYEHISGADLDVSYLGLTEFVGGFSPDIMIIPSELQHFARVVQNVVVINPGRFIRATGNRGSYAQITVQCPDLEDGKLTLVEGEEPVYLHNVWKRARVDLIAS
Protein: Testis-specific protein TSX (P70675)
Organism: Mus musculus (Mouse)
Function: May have an RNA/DNA binding role.
Interaction partners:
- Cleavage stimulation factor subunit 3
- pre-mRNA 3' end processing protein WDR33
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 2
- E3 ubiquitin-protein ligase RBBP6
- WD repeat-containing protein 82
- Cleavage and polyadenylation specificity factor subunit 5
- Cleavage stimulation factor subunit 2 tau variant
Sequence:
MSEKQSPKTSEAECSAMDLPEFEDEENWLFKVLGFQPGPSSALDDDTDDQADEPLSAAEFLHLQDILQEDRVSSTDDEDTCQAGCTEDDETSHSDRDIDNNVKVITGNIKASPSMYMEMFTDQNPQADQDLEETESDGAMNPTD
Protein: Tau-tubulin kinase homolog Asator (EC 2.7.11.1) (Q8IMC6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable serine/threonine protein kinase.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19890914}. Cytoplasm {ECO:0000269|PubMed:19890914}. Note=Found in the cytoplasm during interphase. Localizes to the mitotic spindle in dividing cells. {ECO:0000269|PubMed:19890914}.
Interaction partners:
- Nucleoprotein TPR
Sequence:
MFWHLLCVPNDENASAPDDGNQSCQPSSKQDQYLSPNRNCQKNLLRLYPPPPSKPPPLVGAILQTRLLHQISPSAIADADADLNAVGELLYPNVLQRSATLPAKHNRLGVRSRVTFKVPSSNLPAQDSYSHQPRNQVAVAAKDGILVDVKAKESVKMTSEDLLQPGHVVKERWKVVRKIGGGGFGEIYEGQDLITREQVALKVESARQPKQVLKMEVAVLKKLQGKEHVCRFIGCGRNDRFNYVVMQLQGKNLAELRRAQPRGAFSLSTTLRLGLQILKAIESIHSVGFLHRDIKPSNFSVGRLPYNCRRVYMLDFGLARQYTTGTGEVRCPRAAAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVNGQLPWRKIKDKEQVGLTKEKYDHRILLKHLPSDLKQFLEHIQSLTYGDRPDYAMLIGLFERCMKRRGVKESDPYDWEKVDSTAIGNISATGNPSIPIKSDYMHGNITQMTVAASNASGTEYIRKRAEIETAHITATDPLNIKEKVDKNCNATSLAQPAKGSGEPMVQHGNAANNQNITSKGLQQQSTLTNSQVAIANIQSAPSMIEREDVQYTKLEEGAPTKFITMKPNGECDNVDIAAKCIFEQKHVEANDDIVGRASLSGVEQHYKSQIKKHNSPEIANKQIQRTGTVTNDKTSEVNRSTEEQKSTFGRLRVLTAPPMSVHDLPSGGGHSHQVSDLSGKQDPYAATSNAAPIGINSSSTKFGSQHGQIFGLAAMPPINRRSATSTNLRPSSSASQRINSGSTIGGAVGNGSNTARSSVAGDHSVTQFALIDDENVSALQQVTKGGALTLASQWKSQFDDSEDTTDNEWNREHQLQPNLEQLIKLDISLPLNEAKPFPQHGVAGTGKLINPPGEAKGRPKRYTLNITGIENYEALRISIPNCWSEPAMGNVLRKGLEPPAVQQAAFDDTVYRMDIARNVCVRETYSEITHLARPSTSSVLRNRLPSPFKKDSALQLNSTNDSLDKSRHRNSLPNVSVNDIFDDLQMKLNLDLGSAIQENNCCISGRLEIRVIPKDTSHPDDSVYYDAMGAVKNTPTANEGHDHSDQAVNNCDEMEATSAVIAFPNKSISKIMSPPGRDATEERTGASLCSLYSAGVNKLKLNGNTAPRTQFKKGSTDGFGENESEFDFPLLNPSKIPVRQSKCASWAGADFISASKPLESAEVPQEIPYHPQSDTTYSVIDSIPVRKTTYSIALECPPNISDLTPGLSYFYCNIVVPLRLFSILLTES