wanglab/gogpt-training-data huggingface dataset:
Protein: Centrosomal protein cep57l1 (Centrosomal protein 57kDa-like protein 1) (Centrosomal protein of 57 kDa) (Cep57) (XCep57) (Cep57-related protein) (Cep57R) (Q5FWP9)
Organism: Xenopus laevis (African clawed frog)
Function: Required for spindle microtubule attachment to both kinetochores and centrosomes. Also functions to tether minus-ends of spindle microtubules to centrosomes. May act by forming ring-like structures around microtubules, or by serving as a cross-linker or scaffold at the attachment site.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17803911}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17803911}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17803911}. Note=Localizes to spindle microtubules.
Interaction partners:
Sequence:
MESVSKESYLPSFHQFPLCASLSEFESASSKETQSSALKNISPHPYDILQAPNSRALISALKTLQNKICRLESEKTHARDRLTNLSRAAGEHKKVLESEKRSAEWAAQEATSQKNDVAMQLNNAEQRCSLLEKQLDYMRKMMENADIQNNPIHQIPAQKEQKDMLEMQSKLQKLEVLENECLRLKATHKSSENKIQFLEEKLSVEEQERKALQDKAAQVQTSLEVNRILLSSASSQNSTQRKVKKKKQSKQKNAISKEPSSKEPLSKEPPSKCFFPKAGELPFVAGKSTTSSHSLSANVQNMLHMMKHQSPRVSQKDPKTVEHKPSILPGGSRSIPTRLMSSSTGDTLSDILLALQDELGQMSFEHQELLKHIDETKNTDMREDLERELDYLVKQMEIKSDQIIKLKRHQLNVAKLKKTAKKQPRPPSTTKPAEDEQNIGATDPCTPRNKGNLANGTGTPNSKASLELLKSVRKIQMTLKKDDIMWEK
Protein: F-box protein pof13 (O94334)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- F-box protein pof12
- F-box protein pof9
- F-box protein pof6
- La-related protein 7 homolog
Sequence:
MRPTHWSSNQCEVDFTAEALTTLSLSNRNHEEDPIQPVLKNSNLFLLNRDIWSLIINYLDAFDILRLMHSSRQFYYWLRKSAVDECCFNNNFLNLQPYQRTVPVASDLEWATEVDLYGNPPILKLQLRDSFVWSMLAKFQGLQTIALDGTGVTISSVTNILLNIPTVKTLSIRWCVGVCSLSLIEFLQNSKSRTFSLENLYVLGVKGLELLKPVLLDGSEDDTLTSNWHSRVILFQNALDALPTTHGNPVECDISRCPLNACKIAGQETELADLFSLQKVPACIYCLREWKKPICRYCIDLRSCLVCDSFVCPSCISLDFDLQIQAFARQHRVISTLGVVYPEREDSCFHKIKAAQWHQISPRSLLFQFQEQNHIHHKKIRRKLLAAGWKWPQSQI
Protein: NDR1/HIN1-like 25 (F4K5V1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Tubby-like F-box protein 11
- Receptor-like protein 53
Sequence:
MSDHQKIHPVSDPEAPPHPTAPLVPRGSSRSEHGDPTKTQQAAPLDPPREKKGSRSCWCRCVCYTLLVLFLLIVIVGAIVGILYLVFRPKFPDYNIDRLQLTRFQLNQDLSLSTAFNVTITAKNPNEKIGIYYEDGSKISVLYMQTRISNGSLPKFYQGHENTTIILVEMTGFTQNATSLMTTLQEQQRLTGSIPLRIRVTQPVRIKLGKLKLMKVRFLVRCGVSVDSLAANSVIRVRSSNCKYRFRL
Protein: Carboxypeptidase Q (EC 3.4.17.-) (Hematopoietic lineage switch 2) (Plasma glutamate carboxypeptidase) (Q9WVJ3)
Organism: Mus musculus (Mouse)
Function: Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Lysosome {ECO:0000250}. Secreted {ECO:0000250}. Note=Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin. {ECO:0000250}.
Interaction partners:
Sequence:
MRSLFFLFIVHLLALGSGKAVFKNGVSQRTFREIKEEIANYEDVAKAIINLAVYGKYQNRSYERLGLLVDTVGPRLSGSKNLEKAIQIMYQNLQQDGLENVHLEQVRIPHWERGEESAVMLEPRIHKMAILGLGSSIGTPPGGITAEVLVVASFDELQRRASEARGKIIVYNQPYTGYEKTVQYRVQGAVEAAKVGAVASLIQSVASFSIYSPHTGIQKYQDGVPKIPTACITVEDAEMMSRMASRGNKIVIHLEMGAKTYPDTDSFNTVAEITGSMYPEEVVLVSGHLDSWDVGQGALDDGGGAFISWEALSLVKDLGLRPKRTLRLVLWTAEEQGGIGASQYYELHKANISKYSLVMEADSGTFLPTGLQFTGSDKARAIMKEVMNLLQPLNVTKVFSNGEGTDINFWIQAGVPGASLRDDLYKYFFFHHSHGDTMTVMDPKQMNVAAAVWAVVAYVVADMDEMLPRS
Protein: Calmodulin-binding transcription activator, isoform G (E1JH18)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MENVPDISTSASSSSTSNSTSTLKLQSQITSKNVLIRSQSSGKLSSNEAKSAKPAATTSTTTTLRAAKLKIGAMQQQKQQHQQQHQATSGGNIILLRGTRNENGQIIIQNKQDILSLLSEQQQQQQQEKSHSSTAITLNQLPTATTVARKTIVQGSSGAGSSSSSSSSTISIVANSNNKEASSNTILLQTPINASQLESVLKAQERSKQANATQTKMVERPFMLKHATRSLSSESNCDSKSPFVLQTLKRLEKSQSILVIRNSTASTAATNTSMATSPPNGNSLATSSILSVTRTTKAAKGVAGALHKLKAAAATTATSGGASSAGATSSTATTILRLGKSATTVAINGASKLEATTSTTTAVPVPATATTSNKLSNAVTSEQQQQQQQQSTTTQTNVPLGNDGEPIKLPDNLESLPRADSFPSQRHRWNTNEEIAAILISFDKHGEWQSKEVRTRPKSGSLLLYSRKKVRYRRDGYCWKKRKDGKTTREDHMKLKVQGTECIYGCYVHSAILPTFHRRCYWLLQNPDIVLVHYLNVPYPDDNKMAVIAPSITLWGDKKEWTKEELVSQLKPMLSTINSDDDSDSGNDIEISTAETVESIVCQLMEKQRLSRQAALVKQLDCGCGDGGCVDGKTCTHPVMRRSAAMLKSSVQEKRLGEPFNGNTPNVVVASKLYSRWAERPRQHVDNHGQFHNVTQQLPQESAIKFQIIPPQQQQQQDGNYQQQQYRGGSQMLAARSNLVMQQQQQHQQQQQYHQQQQQQQQQQQQHQQQQQHLSLQRFVASQGQNSVHLNQQHRLQIANTTITATASDPATTLAAAAAVAAASGATPVALNIMDTELIENQNHMTANKITNSGSSNSSSSNASKQLAGQTNNKLNVVNNNDPGNNNFMYNQQQQLNASSNSNNSSQQQQQQQQQHYYKLQQTTATPTSGQPPPLAQVQPHSLAQPPVEAMCMSPEHRSSSQPTPATSSAGSIPSSVSVSISVSTSTPTPAPTSISTPTSGTSSTSSSLQSIIDGNQQQQITTTSTAATCDNLMSANALSEDSHTVNNQATEAPNRSQLQSQSQSLSLNQNGCATYSASSDNSSQISDESSSFGGNNQNSSNSSTSEEEPQVEALSFFNETLDLSQEDIQRTLIANMPYNTTAAGATAPSTTITTGNTKLELSQQETKEKPAMGTETATEIEDDETDDVFANLDAFDMLVEFPELDLDDKQALNNTALEQSSFLGESAPSQPRKVHNICDFSPEWSYTEGGVKVLVAGPWTSSNGGAYTVLFDAQPVPTQLVQEGVLRCYCPAHEAGFVTLQVACGGFLVSNSVMFEYKLSLLADAPFDATSSNDCLYKFTLLNRLSTIDEKLQVKTEHELTTDNTALYLEPNFEEKLVAYCHKLIKHAWSMPSTAASWTVGLRGMTLLHLAAALGYAKLVGAMLNWRSENPHIILETELDALSQDVYGFTPLAWACVRGHVECSLLLYKWNHNALKIKTQAQQTPLDLASMRGHKVLLAQMYRLEKERCRKPQLRGGLANLSMNMGVEAEAEEQHQSFSAFDLELQRKHDGVFLRPVAVHSNQSPPNGSSRYSKRSSIDSGINMDIRSKSGKPLARLHSNFESHDSYALGVDSPLDSLTGTNCLLSPLRKMDFALWDSDAKVLTLAEHIIAAMPERIKNEADEMMVLGSPLTEPLTSESSALTDSFMDPLLDSLPNTHFDSDFSFDFHDHSYRYHDVSTPCSSLSPASSGPLQSPASYSILGTDPSVSSPSPPPSTKQLTEFLHASSISSYPFEADFSKLTLTDTEQRELYEAAKCIQKAYRSYKGRQKLEEQNKERSAATVIQNYYRRYKQYAYYRQMTNAALVIQHGYRSYRRNKRFKKSGLCLSSSSDHGSVSSNSQCLSSFYDHYKQDQQQLHELGSQPSTPKETSPSGPLKRTYSQSTQNQAARKIQQFMRQSRIKLQKERAEKEKLVHQRRAEYLQNLQFQGQQEMLVYHENNISAPSSGNTNASNNNNLHQIQSNQ
Protein: E3 ubiquitin-protein ligase CCNB1IP1 (EC 2.3.2.27) (Cyclin-B1-interacting protein 1) (RING-type E3 ubiquitin transferase CCNB1IP1) (D3Z3K2)
Organism: Mus musculus (Mouse)
Function: Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over. Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:24390283}. Chromosome {ECO:0000269|PubMed:24390283}. Note=Associates to the synaptonemal complex.
Interaction partners:
- Probable E3 SUMO-protein ligase RNF212
- MutS protein homolog 4
- E3 ubiquitin-protein ligase RNF212B
- Fanconi anemia group M protein homolog
- Probable ATP-dependent DNA helicase HFM1
Sequence:
MSLCEDMLLCNYRKCRIKLSGYAWVTACSHIFCDQHGSGEFSRSPAICPACNSTLSGKLDIVRTELSPSEEYKAMVLAGLRPEVVLDISSRALAFWTYQVHQERLYQEYNFSKAENHLKQMEKMYMQQIQSKNIELTSMKGEVISMKKVLEEYKKKFSDISEKLMERNRQYQKLQGLYDSLRLRNITIASQEGSLEPGMIPQSGVFGFPPGNNSKFSLDHIPVGNQGGGDEDVQFRPFFVCSPTAPEPINNFFSFASPSHEAEQQVCSRAFKAKRI
Protein: Regulator of G-protein signaling 6 (RGS6) (P49801)
Organism: Rattus norvegicus (Rat)
Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P49758}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49758}. Membrane {ECO:0000250|UniProtKB:P49758}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49758}. Nucleus {ECO:0000250|UniProtKB:P49758}. Cell membrane {ECO:0000250|UniProtKB:Q9Z2H2}. Note=Interaction with GNB5 mediates translocation to the nucleus. {ECO:0000250|UniProtKB:P49758}.
Interaction partners:
Sequence:
LAVQDLKKQPLQDVAKRVEEIWQEFLAPGAPSAINLDSHSYEITSQNVKDGGRYTFEDAQEHIYKL
Protein: Possible cationic amino acid transport integral membrane protein (O05896)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protein Rv3254
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- Trehalose synthase/amylase TreS
- Probable alpha-glucosidase AglA
- Rubredoxin
Sequence:
MAGRRRMKSVEQSIADTDEPTTRLRKDLTWWDLVVFGVSVVIGAGIFTVTASTAGDITGPAIWISFLIAAATCALAALCYAEFASTLPVAGSAYTFSYATFGEFLAWVIGWNLVLELAMGAAVVAKGWSSYLGTVFGFGNGTGHLGSLQLDWGALVIVTLVATLIALGTKLSSRFSAVVTAIKVSVVVLVVVVGAFYIRAANYSPFIPEPEVQHHGGGLDQSVFSLLTGAQGSHYGWYGVLAGASIVFFAFIGFDIVATMAEETKRPQRDVPRGILASLGVVTLLYVAVSVVLSGMVPYTQLRTVPGRGPANLATAFQANGVYWASGIISVGALAGLTTVVMVLMLGQCRVLFAMARDGLVPRQLAKTGSRGTPVRVTVLVAVLVATTASVFPITKLEEMVNVGTLFAFILVSAGVVVLRRTRPDLQRGFTAPWVPLLPIAAVCACLWLMLNLTALTWIRFGIWLVAGTAIYVGYGRRHSAQGLRQARESATRRC
Protein: ATP synthase subunit gamma, mitochondrial (F-ATPase gamma subunit) (Q96250)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}. Mitochondrion inner membrane {ECO:0000305|PubMed:14671022}; Peripheral membrane protein {ECO:0000305|PubMed:14671022}.
Interaction partners:
- ATP synthase subunit O, mitochondrial
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit beta, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit delta, chloroplastic
- ATP synthase subunit beta-3, mitochondrial
- ATP synthase subunit beta-2, mitochondrial
- ATP synthase subunit delta', mitochondrial
Sequence:
MAMAVFRREGRRLLPSIAARPIAAIRSPLSSDQEEGLLGVRSISTQVVRNRMKSVKNIQKITKAMKMVAASKLRAVQGRAENSRGLWQPFTALLGDNPSIDVKKSVVVTLSSDKGLCGGINSTVVKVSRALYKLNAGPEKEVQFVIVGEKAKAIMFRDSKNDIVLSVTELNKNPLNYAQVSVLADDILKNVEFDALRIVYNKFHSVVAFLPTVSTVLSPEIIEKESEIGGKLGELDSYEIEGGETKGEILQNLAEFQFSCVMFNAVLENACSEMGARMSAMDSSSRNAGEMLDRLTLTYNRTRQASITTELIEIISGASALEAAK
Protein: COMM domain-containing protein 2 (Q86X83)
Organism: Homo sapiens (Human)
Function: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21778237}.
Interaction partners:
- COMM domain-containing protein 3
- COMM domain-containing protein 4
- COMM domain-containing protein 10
- Coiled-coil domain-containing protein 22
- COMM domain-containing protein 5
- COMM domain-containing protein 1
- COMM domain-containing protein 9
- COMM domain-containing protein 6
- COMM domain-containing protein 8
- COMM domain-containing protein 7
Sequence:
MLLELSEEHKEHLAFLPQVDSAVVAEFGRIAVEFLRRGANPKIYEGAARKLNVSSDTVQHGVEGLTYLLTESSKLMISELDFQDSVFVLGFSEELNKLLLQLYLDNRKEIRTILSELAPSLPSYHNLEWRLDVQLASRSLRQQIKPAVTIKLHLNQNGDHNTKVLQTDPATLLHLVQQLEQALEEMKTNHCRRVVRNIK
Protein: Transcription factor E2F8 (E2F-8) (A0AVK6)
Organism: Homo sapiens (Human)
Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene.
Subcellular location: Nucleus {ECO:0000269|PubMed:15897886}.
Interaction partners:
- Transcription factor E2F7
- Cell division control protein 6 homolog
- Transcription factor E2F1
- Transcription factor Dp family member 3
- Kinesin-like protein KIF11
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cyclin-A2
- DNA topoisomerase 2-alpha
- Ribonucleoside-diphosphate reductase subunit M2
- Centromere protein F
Sequence:
MENEKENLFCEPHKRGLMKTPLKESTTANIVLAEIQPDFGPLTTPTKPKEGSQGEPWTPTANLKMLISAVSPEIRNRDQKRGLFDNRSGLPEAKDCIHEHLSGDEFEKSQPSRKEKSLGLLCHKFLARYPNYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLNKTLGTLKSIGEENKYAEQIMMIKKKEYEQEFDFIKSYSIEDHIIKSNTGPNGHPDMCFVELPGVEFRAASVNSRKDKSLRVMSQKFVMLFLVSTPQIVSLEVAAKILIGEDHVEDLDKSKFKTKIRRLYDIANVLSSLDLIKKVHVTEERGRKPAFKWTGPEISPNTSGSSPVIHFTPSDLEVRRSSKENCAKNLFSTRGKPNFTRHPSLIKLVKSIESDRRKINSAPSSPIKTNKAESSQNSAPFPSKMAQLAAICKMQLEEQSSESRQKVKVQLARSGPCKPVAPLDPPVNAEMELTAPSLIQPLGMVPLIPSPLSSAVPLILPQAPSGPSYAIYLQPTQAHQSVTPPQGLSPTVCTTHSSKATGSKDSTDATTEKAANDTSKASASTRPGSLLPAPERQGAKSRTREPAGERGSKRASMLEDSGSKKKFKEDLKGLENVSATLFPSGYLIPLTQCSSLGAESILSGKENSSALSPNHRIYSSPIAGVIPVTSSELTAVNFPSFHVTPLKLMVSPTSVAAVPVGNSPALASSHPVPIQNPSSAIVNFTLQHLGLISPNVQLSASPGSGIVPVSPRIESVNVAPENAGTQQGRATNYDSPVPGQSQPNGQSVAVTGAQQPVPVTPKGSQLVAESFFRTPGGPTKPTSSSCMDFEGANKTSLGTLFVPQRKLEVSTEDVH
Protein: Breast carcinoma-amplified sequence 1 (Amplified and overexpressed in breast cancer) (Novel amplified in breast cancer 1) (O75363)
Organism: Homo sapiens (Human)
Function: Required for myelination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14567997}.
Interaction partners:
- KH domain-containing RNA-binding protein QKI
- Zinc finger protein 217
- Myelin proteolipid protein
Sequence:
MGNQMSVPQRVEDQENEPEAETYQDNASALNGVPVVVSTHTVQHLEEVDLGISVKTDNVATSSPETTEISAVADANGKNLGKEAKPEAPAAKSRFFLMLSRPVPGRTGDQAADSSLGSVKLDVSSNKAPANKDPSESWTLPVAAGPGQDTDKTPGHAPAQDKVLSAARDPTLLPPETGGAGGEAPSKPKDSSFFDKFFKLDKGQEKVPGDSQQEAKRAEHQDKVDEVPGLSGQSDDVPAGKDIVDGKEKEGQELGTADCSVPGDPEGLETAKDDSQAAAIAENNNSIMSFFKTLVSPNKAETKKDPEDTGAEKSPTTSADLKSDKANFTSQETQGAGKNSKGCNPSGHTQSVTTPEPAKEGTKEKSGPTSLPLGKLFWKKSVKEDSVPTGAEENVVCESPVEIIKSKEVESALQTVDLNEGDAAPEPTEAKLKREESKPRTSLMAFLRQMSVKGDGGITHSEEINGKDSSCQTSDSTEKTITPPEPEPTGAPQKGKEGSSKDKKSAAEMNKQKSNKQEAKEPAQCTEQATVDTNSLQNGDKLQKRPEKRQQSLGGFFKGLGPKRMLDAQVQTDPVSIGPVGKSK
Protein: Mekk1b (Q95YH6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRRKKVEYRVKQTPSRPVQMTRNRIGALEEDLPPEDELAAHYEAFGTTPPRTRLKIKNRDWERKQKVVNVTASADLPASVGGTPKKTRTARSRVLRRNTMDCALLNEMFVNDESKRTDKRLQSLLRDSEREMKNSLATTAVAAPRGNSFHETAHPLESLDQIMPLNSEAMAPIPLRIASKVVESCNRYRCVSSRPIGYRSSAPPLAFAAQLPAGMLRSDGRATPGLGKRKDFHETFANLIKLGSVDRQDAKLSQEEHTWQTELKDLIWLELQAWQADRTVEQQDKYLFEARQGVSDLLTHIINYKFQPRYRREPSLISLDSGTHSDSNSNASSPLPSKMCQGCMSLYCKDCMDHQKLALREVEGMLTRLEAAEALYPSSQAMGALHPIYKSQSFVGRIKSMCLWYNITKQNKLKLSILGKILARLQDEKFSWPVCTSSYIATDSGSSSASGVENDDSAVNSMDSSKPPSMAGSASRKGVTPCHKVQFMLNDATHVPGETSSSNESTSTEVSQWSSECSHSHMRKGSMHDINIFSVEPLGTCSSNGTGEQSTGLYRKFIENVLKSRGLAKSLAFLHKLHNVALYKAHIALEKPGAEDFDYESDAESIEEDVPRLDPEISREQVVELRTYGYWSEEAQSINLPSYIPTFVFLSGIPLQFMHEFLRMRLETRPVRPNPLSLEQLMKELREGLTLALTHRERYQRHITTALVENEAELGSYISILNHYDATVRKTFELYLEYIDQLVLVAVPEGNQKSVLEKEWMFTKLISPMIKGMHTLASQKFCGIISKLLRSISERLVKRTVELDQQIDGTADTDDNEEVKWQLLTICRETQSLLTVERERSIKVLFFAKTFCRDVETTDFHREHYEHDVANQQHDFICSDVKAAFKLLQQDVLQVRNKLTAIIEGVQKRCCLSNMRDLDEQDKQAVLSRTREILHQGYKFGFEYHKDVIRLFEQKIMDQKDSGAHTVDLALGIIAYAKMWMHFVMERCERGRGMRPRWASQGLEFLILACDPQITQHLDDDEFEALKQQMDRCISHVIGITSEPEKVAKKKASPRTRKTSSPATSRSRTPTRTPMSAGMVLNPNTPPLQSPPYNKLLHPQFSLKEDVSGTSYSPVDSSDYVDTPCQRSANGELRLLVPQTPPTPASPGKSSLESTPLALRQERVRDAVNRLDMDLEDGLRERRLIGQVKSLNSSDKVHIRARSVHFRWHRGIKIGQGRFGKVYTAVNNNTGELMAMKEIAIQPGETRALKNVAEELKILEGIKHKNLVRYYGIEVHREELLIFMELCSEGTLESLVELTGNLPEALTRRFTAQLLSGVSELHKHGIVHRDIKTANIFLVDGSNSLKLGDFGSAVKIQAHTTVPGELQGYVGTQAYMAPEVFTKTNSDGHGRAADIWSVGCVVVEMASGKRPWAQFDSNFQIMFKVGMGEKPQAPESLSQEGHDFIDHCLQHDPKRRLTAVELLEHNFCKYGRDECSSEQLQMQVRGSFRRNVATSSS
Protein: Large ribosomal subunit protein P2 (60S acidic ribosomal protein P2) (Acyl carrier protein) (Q96UQ7)
Organism: Rhodotorula glutinis (Yeast)
Function: Probable bifunctional protein. The phosphorylated protein plays an important role in the elongation step of protein synthesis (By similarity). The phosphopantetheinylated protein acts as an acyl carrier protein.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MKHVAAYLLLVSAGNTSPSAEDVKKVLAAADIQADEERLSVLIKELEGKDVNEVIAEGSKKLASVPSGGAAPAAAAGGAAAGGAAEEKAEDKPAEKDEESDDDMGFGLFD
Protein: Spinophilin, isoform E (M9NFI2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MEKPMHHAPAPVGKVSQIANIFQRKPIEIQPVEQLSAVAAAHAAAAAAAAAAHHAHVQGAPAVRTESHSARFNNARALFEKLGVESNSNVSSRLLRSGSREDNLCDGSDRSSSRSSDRSQSPPKRRTPFPSGVSLVHNNNNAAIVAQNGVPPEQRLSNSKFIVEPAAQVVPTSVVKYPQHNISRLKSEEPSPVPPPASGSVSALFASSGGDKPEKPERKFNSRELIEKQKKWTSHFTKTKTTRTHSDLNRCDIIRTVPGTGLIMDSEKVAKPAMEPPQPPPNASPNPPMRAQAPPEIKPRSGKIGSPVKSPPLPPIPAVKPKNVSPVKFNPDRLRQSPTKTADNSPPPPPAKSAAVLQRSLMQEQQELLRNSCDQGVAPIPPEKPRKKSVDLIEDTLPLTNCSTPSSCASPTSSYLMQPAKRGSLDGGSGNGQYPGNGLSGSTNSATSGSPVASASSGPSSPVHTEDEKQENESTEKSEMEYYHGGNYNSVPRRRRSENEGRKSVDESSPSANNSQQQQQHSIPGSAAGSPQRVANKRSSITVNMPAAGLGQRPPSIISTTSQDEGGFNESAPELKAKLQPAYDQTEEQPHSLNYVDVGYRLNPDGSESREVYGSEAELYDTAKVTDMQRKFHGANGFGQESSTVYAIIKPDVQESQPVAPSRSVLIQSPNSSSVEGSPLHRGSYSSPPVGVVSPIRRRNSSNQDQSVGGGGSAKTTPQCSPARSALVKGIAPIASIDAHEEEELDLVEEDEHLAVEYVEVLELQQDEEEEEAPVLPERRAPAQGSLELQDLEYADTSAGEDEEDIINHLKDGDVLDVELIDDVVDEVIKVHVNHSVATAPSIQAATPAAAIPREDSLPDDMTAAEAERLLSSSILENKIRQQSLLSDEQAKEVEQILNAAPSVGVAVATVVATATSPTSIKNLIEDLPGQSAVAASAANGEQDIQIAAVPAIVEEDEDEEEDFPEDDEEDHARADFDANGGDADGDSDDVEAVDIVGYGHASTALNATFVKADSTETETTTTTPSTATTATTRHDDDEPEWLRDVLEAPKRSLENLLITSATSSRAPGQREELENGYDLHEKHSDLNQTYITGGESLHESIVSVESTQSDATLNQTTTIDDSIISSKHNSTYSLADAEQATSSTVLSTGVTELDDSQYYIPEYPPVRSKEVLVEAGVHYFEDGNFWMEVPGLLDFDDDDCSYPPITVRKNPKVRFSSGPIHVYSTFSVNDYDRRNEDVDPVAASAEYELEKRVEKMHVFPVELMKGPEGLGLSIIGMGVGADAGLEKLGIFVKTITDNGAAARDGRIQVNDQIIEVDGKSLVGVTQAYAASVLRNTSGLVKFQIGRERDPENSEVAQLIRLSLQADREKEERLKRQQEEYLRRTLDYSEDSTQPVSANSSVCEGPSSPVQVEHPMEVEATHSQEVESLKRLLQESEMGCLVKEEIIQNLKRKLVKLETTGNENELLSERLRQSERELGNIRKEAANLQNMLQQSQGQYMALDKKYNKAKRLVREYQQRELDMCHREEFYQQLLQEKDTEYNALVKKLKDRVINLEHELQETQRKAGFPVGLPYDSATLKLTPQMMRKTPPKPLFHKLETELSDTEISDLSPDGDGVKTATVERKVPVKDELDAAVPQHELLDNSINKTKIDLVPWQQQHHQQIQQQPSAHTTGPPSPTSMSSGCSSPGYSPSRTLDLSGSSSSFSDRKAMAAGYTYKGGPVHEWTKDQVGHWLMGIELERYIPVFKENNVEGGALLTLDSKDFKTLGICGDDKHRLKKRLKDLKANIEKERKDMERERREREKAIRKAEKKAAKKK
Protein: Lysozyme-like protein 4 (Lysozyme-4) (Q96KX0)
Organism: Homo sapiens (Human)
Function: May be involved in fertilization (By similarity). Has no detectable bacteriolytic and lysozyme activities in vitro (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9D925}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q9D925}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9D925}. Note=Found in the principal piece of sperm tail. {ECO:0000250|UniProtKB:Q9D925}.
Interaction partners:
Sequence:
MKASVVLSLLGYLVVPSGAYILGRCTVAKKLHDGGLDYFEGYSLENWVCLAYFESKFNPMAIYENTREGYTGFGLFQMRGSDWCGDHGRNRCHMSCSALLNPNLEKTIKCAKTIVKGKEGMGAWPTWSRYCQYSDTLARWLDGCKL
Protein: Histone H2B (B2R4S9)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000451}.
Interaction partners:
Sequence:
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Threonine dehydratase, mitochondrial (EC 4.3.1.19) (Threonine deaminase) (P00927)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Acetolactate synthase catalytic subunit, mitochondrial
- Acetolactate synthase small subunit, mitochondrial
- Threonine synthase
- Tryptophan synthase
- Dihydroxy-acid dehydratase, mitochondrial
- Low specificity L-threonine aldolase
- SUMO-conjugating enzyme UBC9
- Cystathionine beta-synthase
- Branched-chain-amino-acid aminotransferase, cytosolic
- Branched-chain-amino-acid aminotransferase, mitochondrial
Sequence:
MSATLLKQPLCTVVRQGKQSKVSGLNLLRLKAHLHRQHLSPSLIKLHSELKLDELQTDNTPDYVRLVLRSSVYDVINESPISQGVGLSSRLNTNVILKREDLLPVFSFKLRGAYNMIAKLDDSQRNQGVIACSAGNHAQGVAFAAKHLKIPATIVMPVCTPSIKYQNVSRLGSQVVLYGNDFDEAKAECAKLAEERGLTNIPPFDHPYVIAGQGTVAMEILRQVRTANKIGAVFVPVGGGGLIAGIGAYLKRVAPHIKIIGVETYDAATLHNSLQRNQRTPLPVVGTFADGTSVRMIGEETFRVAQQVVDEVVLVNTDEICAAVKDIFEDTRSIVEPSGALSVAGMKKYISTVHPEIDHTKNTYVPILSGANMNFDRLRFVSERAVLGEGKEVFMLVTLPDVPGAFKKMQKIIHPRSVTEFSYRYNEHRHESSSEVPKAYIYTSFSVVDREKEIKQVMQQLNALGFEAVDISDNELAKSHGRYLVGGASKVPNERIISFEFPERPGALTRFLGGLSDSWNLTLFHYRNHGADIGKVLAGISVPPRENLTFQKFLEDLGYTYHDETDNTVYQKFLKY
Protein: Uncharacterized protein (Q382X9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVDELPPVLSGVGTTDSVPRVNEHEPTSPSVDFEGQEMLLEPGTSTINDESNSALFCGAGDPKELQAEPRDSRDRTGIVSRQLITPQQQQQLGISTCSRKSLEQKISILEATIATQKKEIILLQRQLQSRSTGATDHRLANALKEIAALKEALNHANGKAESEREPAALQMQATIERLSTERNELMNCLRKQNKLIEALKRQKVHLESATLLNIMEKEIEKYFELAR
Protein: Achintya, isoform C (Achintya, isoform D) (A1Z916)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Vismay, isoform B
- Mothers against decapentaplegic homolog
- LD38858p
Sequence:
MISPEQEEVNMVLDRHVRQNIQDMMHEAHVQASLLENEGRGRFHSDSSLDQDSLHADVIVEEDQSTEHGANQVQNYHDMMVDSEHHIDINGSLRKRRGNLPKTSVKILKRWLYEHRYNAYPSDAEKFTLSQEANLTVLQVCNWFINARRRILPEMIRREGNDPLHFTISRRGKKVSPNCSRSSALGANLTGPNPAHGSPASEVVVGATEEVDGAGEIHEGIANVLTNFEQYVQGPNGQMVKMEPEYEDSVIYSWQQAIANNPMGFQSLHSSLQATMIDKIKNYQMRKAAAIGGSAVGSGGAGGSSSNSSPATSILPYSLFGQLPPEFDDEEKPRPPKRVRTRTVAAKSPRENAKQAKQKTGNKQETMYCYKDSYGGIVVSPRSEGEESAQGYESCGPNSEEEVRFETSHDWQSVIKTVFGTEEVSTSAGNNPGTSGSKGSVQNTAIWNRNQTAKRDVNQQLTDFESELNRIQASEIQTIDPTNSNQQDIGDNLQADEVFTGAEAEAGQSQLSAMSQGTSPDERAKYKCLYYLVETAMAVRQNDDVQDDDFVYMGD