wanglab/gogpt-training-data huggingface dataset:
Protein: Citrinin resistance protein, mitochondrial (Citrinin sensitive knockout protein 1) (Q06139)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial protein that is involved in citrinin resistance.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein RTA1
- Uncharacterized protein YKL070W
Sequence:
MQSISNCPIGLVSKNTINSASTIAEWVACPWKYINVVGSGRYVSNKPDKITRYDLLKAAQEAEMQELLTRNDMKGRHKRNKKSKIALETIAEENSSTESLF
Protein: Glucan endo-1,3-beta-D-glucosidase (Endo-1,3-beta-glucanase) (EC 3.2.1.39) (Laminarinase) (Q9KG76)
Organism: Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans)
Function: Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q47N06}.
Interaction partners:
- Endo-1,4-beta-xylanase A
Sequence:
MKGKNVQLLFALVVIILLFPTGASASPHAVSVGKGSYATEFPEIDFGGINDPGFRDQQGEPPATIYRSDRVTGPMQTNSWWGSLAVDRFSMNQYPHPFSVRHRAEGLHVFYDAPHNMVVHENREAGTWHIHGAIGTDFTIKHSGTANFEQAVVDDYNDWYVRGLLENGAHQMAITYGVGSPYIFVEYEDGSAVLDFDIAPDVWEMNGHVIGFSTHDHKHYAAFAPPGQNWSGIGSKTLTNNADYIAIAKLPEKDGNMLAKFEQYAYSVVRDAVADWTYDEATGTVTTTFEVTTEAKVQGAPDGTIFALYPHQYRHLASSSENQLLQNYQYEIIRGTMIGLEGKRFTTELTYPGVLPSLPDLGDYDRERLIGYLHDATSDYPTGSDTYELGKYIGKLATLAPIADQMGEYELAEQFRGELKDILEDWLQATNASGQLKGKNLFYYNENWGTILGYHAAHSSATRINDHHFHYGYFVKAAAEIARADQEWAKSENWGGMIDLLIRDFMADRDDDLFPYLRMFDPYSGNSWADGLATFDAGNNQESSSEAMHAWTNVILWAEATGNKALRDRAIYLYTTEMSAINEYFFDVHQEIFPEEYGPEIVTINWGGKMDHATWWNSGKVEKYAINWLPFHGGSLYLGHHPDYVDRAYEELRRDIGSTDWNLWSNLVWMYRAFTNPDDALQQMEASIDDYGLFDPGNEKIIERGSTKAQTYHWIHNLAELGRVDPTVTANHPIYAVFNKNGNRTYIVYNFSDSPITVQFSDGHSIQVEPHSFNIGNGDGPTNPDPSEPDLKNPYERIQAEAYDAMSGIQTEGTDDDGGGDNIGWINDGDWVKYERVHFERDASSIEVRVASDTPGGRIEIRTGSPTGTLLGDVQVPNTGGWQQWQTVTGNVQIQPGTYDVYLVFKGSPEYDLMNVNWFVFRANGQGNGDSHTHPDYTAGIRGITGNEVTIFFAPTTEARYVDVHLKVNNGQQLNYRMTERNGEWERVVENLSSGDVLEYSFTYEKLGPQYTTEWFTYSR
Protein: Phytoene synthase 3, chloroplastic (OsPSY3) (EC 2.5.1.32) (B6UV92)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the conversion of geranylgeranyl diphosphate to phytoene. Mediates the first committed step in carotenoid biosynthesis. May play a role in regulating carotenoid flux in response to abiotic stress in roots. May control flux to carotenoid precursors that are required for abiotic stress-induced abscisic acid (ABA) formation in roots.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:18326788}; Peripheral membrane protein {ECO:0000305}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:23023170}.
Interaction partners:
- aldehyde oxygenase
- 15-cis-phytoene desaturase, chloroplastic/chromoplastic
- Os07g0580900 protein
- prolycopene isomerase
- Os02g0668100 protein
- Probable solanesyl-diphosphate synthase 3, chloroplastic
- Solanesyl-diphosphate synthase 2, chloroplastic
- Phytoene synthase 2, chloroplastic
- Phytoene synthase 1, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
Sequence:
MMSTTTTSSAAGSPVCARRRQRVFVDVPRRRATSLARVEYAKMAPPPPPPCSVRAAGSNPIGCLEVAEPWSGAAPPPLPPLPGHLHVAAPAAEDDDDALAAAAAAVPSEQRVHDVVLKQAALAAAAPEMRRPAQLAERERVAGGLNAAFDRCGEVCKEYAKTFYLATQLMTPERRRAIWAIYVWCRRTDELVDGPNASHMSALALDRWESRLDDIFAGRPYDMLDAALSHTVATFPVDIQPFRDMIEGMRLDLTKSRYRSFDELYLYCYYVAGTVGLMTVPVMGISPDSRANTETVYKGALALGLANQLTNILRDVGEDARRGRIYLPMDELEMAGLSEDDIFDGRVTDRWRCFMRDQITRARAFFRQAEEGASELNQESRWPVWASLLLYRQILDEIEANDYNNFTKRAYVPKAKKIVALPKAYYRSLMLPSSVRHCSSLTSS
Protein: Protein REDUCED CHLOROPLAST COVERAGE 3 (F4HZK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as the scaffold of a protein complex, which sequesters key factors that are required for the G2 to M transition in meristematic tissues (By similarity). Together with REC2, REC3 and FMT/CLU, contributes to the establishment of the cellular volume devoted to the chloroplast compartment.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:F4HS99, ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:F4HS99}.
Interaction partners:
- CASC3/Barentsz eIF4AIII binding protein
- SEED MATURATION PROTEIN 1
- Pentatricopeptide repeat-containing protein At1g30610, chloroplastic
- Eukaryotic initiation factor 4A-III homolog
- Ethylene-responsive transcription factor ERF022
- Protein SUPPRESSOR OF NIM1 1
- Peptidyl-prolyl cis-trans isomerase CYP63
Sequence:
MAPRSSKGKSNNKGKGGDKKKRDDKLLAPSLVEITVTTPYETQVILKGVSTDKIIDVRRLLASHVETCHFTNYSLSHKVKGHKLNDNIQVLSLKPCFLRMIPEEYLEESQALTQVRRVIDIVACTTRFFSKSPNKSIVAGNANPTPAPDGLDMVAIHTTPKLSQFYEFFSIHHLSPPILHLKKVDGEEAGEKRDGDYFGLKVKICNGKVIHVIASVKGFFAVGKQLSHCHSIVDLLQNVSNAFAKAYESLMKAFTDRNKFGNLPFGLRSNTWLVPSPVSESASPLPTEDEHWGGNGGGQGRNGEYDHRPWAAEFSVLATLPCKTEEERVIRDKKAFLLHSQFIDTSVQRAVRAICNVMDTNQQTSGTTDLPAGSILLEDHVGDLSIVVKRDIASLDSKPEATFQNDAFVLSSEELAERNLLKGITADESVIVHDTPALGKVIVRQCGYTAVVNVKGQTQKAMSDFRDILIDDLPDGGANALNLNSLRVEFHRPHSVGTSVENQPTQLDWDDLESYRCIIQELVKINLTKLEETRVSSVRPIRWELGSTWVQHLQKKETDVCGKPATNDETELSVKGLGKQFKDLKSKSKKSENISAVNEKDTRLHELNEEDDLGQKSIDGLFTELKELLSEEAFSRLKETGTGLHLKSKEELTNMAYGYYDEIALPRLVADFGSLELSPVDGRTLTDFMHIRGLQMRSLGHVAKLAEKLPHIQSLCIHEMITRAFKHLLRAVIASVNNMAELPVAVAASLNFMLGRRELEGCDRIPGEEYCLRLQWLQKFLSRKFGWIQKDEFHHLKKFSILRGLCQKVGLELVSRDFDFDSPNPFMSSDIIGLVPVCKHVLCISSDGRTLLESSKLALDKGKLDDAVSYGTKALVKMIAVCGPYHRNTACAYSLLAVVLYHTGDFNQATIYQQKALDINERELGLDHPDTMKSYGDLSVFYYRLQHFELALKYVNRALFLLHFTCGLSHPNTAATYINVAMMEKEVGNDHLALRYLHEALKSNKRLLGADHIQTAASYHAIAVALSFMEAHSLSVQHEQTTLQILTAKLGADDLRTQDAAAWLEYFESRAIEQQEAGRNGIPKPDASIASKGHLSVSDLLDYISSDPDTKGNVAHRKHRRARILQVNDKVASADDDAHRVASQIDIVTWNNVAEADVTKSRSEVNDPDTVVDKTNIETGDIVVHRLNVDRQTVEESTLDEGWQEAYSKGRSGNGAGRKSRQRQPDLMKKRMLLNKHHNRNQDVQQQNIYSPLQKTSKGPSLSKSSPRRALKNAEIDVSTNTTKPQLKASGAAAVTSTTLASKSLSYKEVALAPPGTVLKPMLEKLELNLERTETQIYRTSSASSGEESKSDTVMLDLPIEGTELHCEKQESQESAESVENLTSESEGDLGSYRGKKTSDISRTKLSASAEPYNPGGFLVIDLQSSAATIGSYPIMVADPISWAVVSCGIHSPPYYSAIHSNGVGTPRSMNPDAPEFVPRRSLQNSSQHAGEDASVSVDSSSCLKAEKDAVDLKKRELASFIVKSSQKEVPAALSKTSPEAESGGTSEKDSAVTEIVYSREEENGANANETNGGEGFVIVAKKRRRKNKVRLTNVAAGLYHQPSSVCA
Protein: Membrane-associated phosphatidylinositol transfer protein 2 (Drosophila retinal degeneration B homolog 2) (RdgB2) (Phosphatidylinositol transfer protein, membrane-associated 2) (PITPnm 2) (Pyk2 N-terminal domain-interacting receptor 3) (NIR-3) (Q6ZPQ6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions (By similarity).
Subcellular location: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:10460238}. Note=May associate with the cytoskeleton.
Interaction partners:
Sequence:
MIIKEYRIPLPMTVDEYRIAQLYMIQKKSRNETHGQGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPGWFRSILPKAALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDTGENNNVFNLSPVEKSQLITDIIDIVKDPVPPSEYKTEEDPKLFQSVKTCRGPLSENWIQEYKKRLLPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLTMEKIRELEREVQLMLSRKMAQFSEEGPSELSKDSATKDQASGTTSDPGSKNGEPLGRGLKKQWSTSSKSSRSSKRGASPSRHSISEWRMQSIARDSDEGSEEEFFDAHENLYCTEEKQAKDMTKWNSNDLMDKMESPEPEESQDEIYQQSGSEFRVASSVEQLNIIEDEVSQPLAAPPSKIHVLLLVLHGGTILDTGAGDPSSKQGDTNTITNVFDTVMRVHYPSALGHLAIRLVPCPPICADAFALVSNLSPYGHDEGCLSSSQDHIPLAALPLLATSSPQYQEAVATVIQRANLAYGDFIKSQEGVTFNGQVCLIGDCVGGILAFDALCYSGQPVSESQSSSRRGSVVSMQDADLLSPGTLANAAHCSGGSGGGGSGGSSLESSRHLSRSNIDIPRSNGTEDSRRQLPRKRSDSSTYELDTIQQHQAFLSSLHASVLRNEPSSRRSSSSTMLDGAGALGKFDFEIADLFLFGCPLGLVLALRKTVIPSLDVFQLRPACQQVYNLFHPADPSASRLEPLLERRFHSLPPFSIPRYQRYPLGDGCSTLLADVLQTHNTVFQEHAAPSSPGTAPAGRGFRRASEISIASQVSGMAESYTASSIAQKGPSSLNHTPSIRRLSLLALPPPSPTTQGPRARARQVSPNLERAPCLPDLDIGEVAAKWWGQKRIDYALYCPDALTAFPTVALPHLFHASYWESTDVVSFLLRQVMRHDSSSILELDGKEVSVFTPSQPRERWQRKRTHVKLRNVAANHRINDAVANEDGPQVVTGRFMYGPLDMVTLTGEKVDVHIMTQPPSGEWLHLDTLVTNSSGRVSYTIPETHRLGVGVYPIKMVVRGDHTFADSYITVLPRGTEFVVFSIDGSFAASVSIMGSDPKVRAGAVDVVRHWQDLGYLIIYVTGRPDMQKQRVVAWLAQHNFPHGVVSFCDGLVHDPLRHKANFLKLLISELHLRAHAAYGSTKDVAVYNSISLSPMHIYIVGRPTKKLQQQCQFITDGYAAHLAQLKYNHRARPARNTATRMALRKGSFGLPGQSDFLRSRNHLLRTISAQPSGPSHRHDRTQTQMDSEQRGQRSMSVAASCWGRAMAGRLEPGAATGPK
Protein: GH16843p (Q8I941)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Golgin 104
- FI01459p
Sequence:
MSSEELAPINEQDFKDLKERMKLIVEADPKQYHNDFSLRRYLRAFKTTDDAFQAILKTNKWRETYGVDKLSEMDRSQLDKKARLLRHRDCIGRPVIYIPAKNHSSERDIDELTRFIVYNLEEACKKCFEEVTDRLCIVFDLAEFSTSCMDYQLVQNLIWLLGKHFPERLGVCLIINSPGLFSTIWPAIRVLLDDNTAKKVKFVADEAELCQYLIPDILPTDM
Protein: Cohesin subunit SA-1 (SCC3 homolog 1) (Stromal antigen 1) (Q8WVM7)
Organism: Homo sapiens (Human)
Function: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.
Subcellular location: Nucleus. Chromosome. Chromosome, centromere. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
Interaction partners:
- Wings apart-like protein homolog
- Structural maintenance of chromosomes protein 1A
- Double-strand-break repair protein rad21 homolog
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein PDS5 homolog A
- Structural maintenance of chromosomes protein 1B
- Nipped-B-like protein
- Cohesin subunit SA-2
- Meiotic recombination protein REC8 homolog
- Sister chromatid cohesion protein PDS5 homolog B
Sequence:
MITSELPVLQDSTNETTAHSDAGSELEETEVKGKRKRGRPGRPPSTNKKPRKSPGEKSRIEAGIRGAGRGRANGHPQQNGEGEPVTLFEVVKLGKSAMQSVVDDWIESYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRNMQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKMYSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSMTLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLVYSAHRPVAVAAGEFLHKKLFSRHDPQAEEALAKRRGRNSPNGNLIRMLVLFFLESELHEHAAYLVDSLWESSQELLKDWECMTELLLEEPVQGEEAMSDRQESALIELMVCTIRQAAEAHPPVGRGTGKRVLTAKERKTQIDDRNKLTEHFIITLPMLLSKYSADAEKVANLLQIPQYFDLEIYSTGRMEKHLDALLKQIKFVVEKHVESDVLEACSKTYSILCSEEYTIQNRVDIARSQLIDEFVDRFNHSVEDLLQEGEEADDDDIYNVLSTLKRLTSFHNAHDLTKWDLFGNCYRLLKTGIEHGAMPEQIVVQALQCSHYSILWQLVKITDGSPSKEDLLVLRKTVKSFLAVCQQCLSNVNTPVKEQAFMLLCDLLMIFSHQLMTGGREGLQPLVFNPDTGLQSELLSFVMDHVFIDQDEENQSMEGDEEDEANKIEALHKRRNLLAAFSKLIIYDIVDMHAAADIFKHYMKYYNDYGDIIKETLSKTRQIDKIQCAKTLILSLQQLFNELVQEQGPNLDRTSAHVSGIKELARRFALTFGLDQIKTREAVATLHKDGIEFAFKYQNQKGQEYPPPNLAFLEVLSEFSSKLLRQDKKTVHSYLEKFLTEQMMERREDVWLPLISYRNSLVTGGEDDRMSVNSGSSSSKTSSVRNKKGRPPLHKKRVEDESLDNTWLNRTDTMIQTPGPLPAPQLTSTVLRENSRPMGDQIQEPESEHGSEPDFLHNPQMQISWLGQPKLEDLNRKDRTGMNYMKVRTGVRHAVRGLMEEDAEPIFEDVMMSSRSQLEDMNEEFEDTMVIDLPPSRNRRERAELRPDFFDSAAIIEDDSGFGMPMF
Protein: Transcription factor atf1 (Protein sss1) (Transcription factor mts1) (P52890)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transcription factor required for sexual development and entry into stationary phase. Binds and activates CRE sites (cAMP-response elements, also known as M26 meiotic recombination hotspots).
Subcellular location: Nucleus.
Interaction partners:
- Mitogen-activated protein kinase sty1
- Transcription factor pcr1
- Transcriptional repressor tup11
- Transcriptional repressor tup12
- AP-1-like transcription factor
- General transcriptional corepressor ssn6
- Protein kinase wis1
- Mitogen-activated protein kinase spm1
- Catalase
- Chromatin-associated protein swi6
Sequence:
MSPSPVNTSTEPASVAAVSNGNATASSTQVPENNQSDSFAPPSNNSQQNQQSSTIAPNGGAGSVANANPADQSDGVTPSFVGSLKLDYEPNPFEHSFGSTASVGQGNPSLNRNPSLSNIPSGVPPAFARTLLPPVSSIASPDILSGAPGIASPLGYPAWSAFTRGTMHNPLSPAIYDATLRPDYLNNPSDASAAARFSSGTGFTPGVNEPFRSLLTPTGAGFPAPSPGTANLLGFHTFDSQFPDQYRFTPRDGKPPVVNGTNGDQSDYFGANAAVHGLCLLSQVPDQQQKLQQPISSENDQAASTTANNLLKQTQQQTFPDSIRPSFTQNTNPQAVTGTMNPQASRTQQQPMYFMGSQQFNGMPSVYGDTVNPADPSLTLRQTTDFSGQNAENGSTNLPQKTSNSDMPTANSMPVKLENGTDYSTSQEPSSNANNQSSPTSSINGKASSESANGTSYSKGSSRRNSKNETDEEKRKSFLERNRQAALKCRQRKKQWLSNLQAKVEFYGNENEILSAQVSALREEIVSLKTLLIAHKDCPVAKSNSAAVATSVIGSGDLAQRINLGY
Protein: WD repeat-containing protein 3 (Q9UNX4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:34516797}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 18 homolog
- U3 small nucleolar ribonucleoprotein protein MPP10
- WD repeat-containing protein 43
- Nucleolar protein 6
- Small subunit processome component 20 homolog
- Transducin beta-like protein 3
- WD repeat-containing protein 36
- Ribosome biogenesis protein BMS1 homolog
- Something about silencing protein 10
- Periodic tryptophan protein 2 homolog
Sequence:
MGLTKQYLRYVASAVFGVIGSQKGNIVFVTLRGEKGRYVAVPACEHVFIWDLRKGEKILILQGLKQEVTCLCPSPDGLHLAVGYEDGSIRIFSLLSGEGNVTFNGHKAAITTLKYDQLGGRLASGSKDTDIIVWDVINESGLYRLKGHKDAITQALFLREKNLLVTSGKDTMVKWWDLDTQHCFKTMVGHRTEVWGLVLLSEEKRLITGASDSELRVWDIAYLQEIEDPEEPDPKKIKGSSPGIQDTLEAEDGAFETDEAPEDRILSCRKAGSIMREGRDRVVNLAVDKTGRILACHGTDSVLELFCILSKKEIQKKMDKKMKKARKKAKLHSSKGEEEDPEVNVEMSLQDEIQRVTNIKTSAKIKSFDLIHSPHGELKAVFLLQNNLVELYSLNPSLPTPQPVRTSRITIGGHRSDVRTLSFSSDNIAVLSAAADSIKIWNRSTLQCIRTMTCEYALCSFFVPGDRQVVIGTKTGKLQLYDLASGNLLETIDAHDGALWSMSLSPDQRGFVTGGADKSVKFWDFELVKDENSTQKRLSVKQTRTLQLDEDVLCVSYSPNQKLLAVSLLDCTVKIFYVDTLKFFLSLYGHKLPVICMDISHDGALIATGSADRNVKIWGLDFGDCHKSLFAHDDSVMYLQFVPKSHLFFTAGKDHKIKQWDADKFEHIQTLEGHHQEIWCLAVSPSGDYVVSSSHDKSLRLWERTREPLILEEEREMEREAEYEESVAKEDQPAVPGETQGDSYFTGKKTIETVKAAERIMEAIELYREETAKMKEHKAICKAAGKEVPLPSNPILMAYGSISPSAYVLEIFKGIKSSELEESLLVLPFSYVPDILKLFNEFIQLGSDVELICRCLFFLLRIHFGQITSNQMLVPVIEKLRETTISKVSQVRDVIGFNMAGLDYLKRECEAKSEVMFFADATSHLEEKKRKRKKREKLILTLT
Protein: Exonuclease 1 (mExo1) (EC 3.1.-.-) (Exonuclease I) (Q9QZ11)
Organism: Mus musculus (Mouse)
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis.
Subcellular location: Nucleus {ECO:0000250}. Note=Colocalizes with PCNA to discrete nuclear foci in S-phase. {ECO:0000250}.
Interaction partners:
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- DNA replication ATP-dependent helicase/nuclease DNA2
- RecQ-like DNA helicase BLM
- DNA repair protein RAD51 homolog 1
- DNA mismatch repair protein Msh6
- DNA endonuclease RBBP8
- Double-strand break repair protein MRE11
- Mismatch repair endonuclease PMS2
- Serine/threonine-protein kinase Chk1
- DNA mismatch repair protein Msh2
Sequence:
MGIQGLLQFIQEASEPVNVKKYKGQAVAVDTYCWLHKGAIACAEKLAKGEPTDRYVGFCMKFVNMLLSYGVKPILIFDGCTLPSKKEVERSRRERRQSNLLKGKQLLREGKVSEARDCFARSINITHAMAHKVIKAARALGVDCLVAPYEADAQLAYLNKAGIVQAVITEDSDLLAFGCKKVILKMDQFGNGLEVDQARLGMCKQLGDVFTEEKFRYMCILSGCDYLASLRGIGLAKACKVLRLANNPDIVKVIKKIGHYLRMNITVPEDYITGFIRANNTFLYQLVFDPIQRKLVPLNAYGDDVNPETLTYAGQYVGDSVALQIALGNRDVNTFEQIDDYSPDTMPAHSRSHSWNEKAGQKPPGTNSIWHKNYCPRLEVNSVSHAPQLKEKPSTLGLKQVISTKGLNLPRKSCVLKRPRNEALAEDDLLSQYSSVSKKIKENGCGDGTSPNSSKMSKSCPDSGTAHKTDAHTPSKMRNKFATFLQRRNEESGAVVVPGTRSRFFCSSQDFDNFIPKKESGQPLNETVATGKATTSLLGALDCPDTEGHKPVDANGTHNLSSQIPGNAAVSPEDEAQSSETSKLLGAMSPPSLGTLRSCFSWSGTLREFSRTPSPSASTTLQQFRRKSDPPACLPEASAVVTDRCDSKSEMLGETSQPLHELGCSSRSQESMDSSCGLNTSSLSQPSSRDSGSEESDCNNKSLDNQGEQNSKQHLPHFSKKDGLRRNKVPGLCRSSSMDSFSTTKIKPLVPARVSGLSKKSGSMQTRKHHDVENKPGLQTKISELWKNFGFKKDSEKLPSCKKPLSPVKDNIQLTPETEDEIFNKPECVRAQRAIFH
Protein: Microtubule integrity protein mal3 (Q10113)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May play a role in regulating the integrity of microtubules possibly by influencing their stability. Involved in an anchoring mechanism to maintain tea2 and tip1 at growing microtubule ends. Strongly stimulates the ATPase activity of tea2.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15177031, ECO:0000269|PubMed:18256284}. Note=Associated with microtubules (PubMed:15177031, PubMed:18256284). During metaphase, localizes to astral microtubules, spindle microtubules, and intranuclear microtubules (INMs) (PubMed:18256284). {ECO:0000269|PubMed:15177031, ECO:0000269|PubMed:18256284}.
Interaction partners:
- Tip elongation protein 1
- Tubulin beta chain
- Phosphoprotein p93
- Kinesin-like protein tea2
- Tubulin alpha-1 chain
- Spindle pole body component alp14
- Tubulin alpha-2 chain
- Tip elongation aberrant protein 1
- Kinesin-like protein 2
- Protein peg1
Sequence:
MSESRQELLAWINQVTSLGLTRIEDCGKGYAMIQIFDSIYQDIPLKKVNFECNNEYQYINNWKVLQQVFLKKGIDKVVDPERLSRCKMQDNLEFVQWAKRFWDQYYPGGDYDALARRGNRGPANTRVMNSSAGATGPSRRRQVSSGSSTPSMTKSSANNNNVSSTANTAAVLRAKQAQQQITSLETQLYEVNETMFGLERERDFYFNKLREIEILVQTHLTTSPMSMENMLERIQAILYSTEDGFELPPDQPADLTTALTDHDTNNVAEEAQMTDLKDSETQRVPSAPDFVHARLQSLEVDDDENITF
Protein: Protein YibA (P0ADK6)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Protein RhsA
- Uncharacterized protein YkfM
Sequence:
MSNTYQKRKASKEYGLYNQCKKLNDDELFRLLDDHNSLKRISSARVLQLRGGQDAVRLAIEFCSDKNYIRRDIGAFILGQIKICKKCEDNVFNILNNMALNDKSACVRATAIESTAQRCKKNPIYSPKIVEQSQITAFDKSTNVRRATAFAISVINDKATIPLLINLLKDPNGDVRNWAAFAININKYDNSDIRDCFVEMLQDKNEEVRIEAIIGLSYRKDKRVLSVLCDELKKNTVYDDIIEAAGELGDKTLLPVLDTMLYKFDDNEIITSAIDKLKRS
Protein: At2g21530 (SMAD/FHA domain-containing protein) (Q8GWP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Zinc finger CCCH domain-containing protein 18
- Protein RADIALIS-like 6
- RNA polymerase sigma factor sigC
Sequence:
MEITISQLCSRVKFSSSSSSSSLFCFYGNSNRNNLNGAVSVNCLRENEQISNISFIAKKPRSHAPVVRTTRASLDENQSPTSGGERWLLKPVGDGDTRHIGYKVAMPAPFEISSGQVTIGRLPEKADVVIPVATVSGVHATINTNEKNLLVTDMNSTNGTFIEDKRLIPGVAAPAFPGTRITFGDTNLAIFRVFKLQDSEESIEKPTTE
Protein: Entomoglyceroporin 2, isoform C (A0A0C4DHF9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Aquaporin
Sequence:
MPVQQPQSAEIGHQMKMSSEEPPSGKQTCRSQSNCWLLQRRQLDSITTVLAEMIATAMLMFLGCMGSVENSVFTNSDFQSALNFGFVVLICIQCFGCVCGAHLNPAVTLATYVYNMISLPMALAYFVAQMVGAFIGYGLLKAVLPESAIYSAENPNGVCLTSLNSTLTPWQGLAVEFLITCVLISVCCGVWDPRNATKQDSLPVRFGLAIACLSLTAGQLTGASMNPVRSFAPAIWNGFWDDHWIYWVGPMAAALITSVIYKHAFRRELEESEVDETTMSTKRTSEAELA
Protein: MKIAA0311 protein (Q6ZQD9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
QSEKAHLEDPLLHGFYFDKKSCKPKHQTSESQPDAPLHEKILASAPHEMGRSSYKSSDIEKALTGIQNARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFSGQMSLDVASSINEDSPASLTELSSSDELSLCSEDIVLHKNKVPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLSREKKRPSVTDEIKVNKDGGSTERANPSDTLDIEALLNCSIKRLSENNGNGKNPPRTHDLGTKGENKKNTYDVTKDPHVADMENGNVESTPEREKEKPEIPEASANLASNVKKISESKHDEYEALMDGSDDSSVTGKEFGPPNDRHPPQIGADPQHPERGDCTSVQNSCSGLLLETGGGSRQDSDGLKSLSNDAPSVARNAAGCCLLEQNETEESASISSSTSCCNCKPDVFHQKDDEDCSVHDFVKEIIDMASTALKSKSQPESEVAAPTSLTQIKEKVLEHSHRPIHLRKGDFYSYLSLSSHDSDCGEVTNYIDEKSNTPLPPDTVDSGLDDKEDVDCFFEACVEDEPADEEARLSSALPNESEVQDEAAKPEQMTASSSVFRDETDTVPLSGLSPQKGADDAKEGDGASHTSQGCVESAEPTTPPGKAKREGSSRKQSVSGTPEENAASAKPKIQAFSLNAKQPKGKAALYPSPQTLTCKEKLVSFHEDRHSNMHR
Protein: Nicotinamide riboside kinase 2 (NRK 2) (NmR-K 2) (EC 2.7.1.22) (Integrin beta-1-binding protein 3) (Muscle integrin-binding protein) (MIBP) (Nicotinic acid riboside kinase 2) (EC 2.7.1.173) (Ribosylnicotinamide kinase 2) (RNK 2) (Ribosylnicotinic acid kinase 2) (Q9D7C9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). Reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. Involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. May play a role in the regulation of terminal myogenesis (By similarity).
Interaction partners:
- Nicotinate phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide phosphoribosyltransferase
- Purine nucleoside phosphorylase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Purine nucleoside phosphorylase
- Nicotinamide riboside kinase 1
- NAD-capped RNA hydrolase NUDT12
Sequence:
MKLIIGIGGVTNGGKTTLTNSLLKALPNCCVIHQDDFFKPQDQIAVGEDGFKQWDVLESLDMETMLSTVQAWVKDPHKFARAHGVSLQSGASDTHVLLLEGFLLYSYRPLVDLYSQRYFLTVPYEECKRRRRSRTYMVPDPPGLFDGHVWPMYQKYRREMEQDGVEVVYLDGMKSPEGLFHQVLEDIQNRLLNTS
Protein: EF-hand protein NUCB1 (O44117)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVQNVALLGLALIAISASIVALPVTQNKKDHKEAAESSTPATADVETALEYERYLREVVEALEADPEFRKKLDKAPEADIRSGKIAQELDYVNHHVRTKLDEIKRREVERLRELANQAYELSNDIDRKHLKVSQHLDHDNEHTFEIEDLRKLIQKTSDDLAEADRKRRGEFKEYEMQKEFEREAQKKEMDEESRKKFETELKEKEEKHKDHEKLHHPGNKAQLEDVWEKQDHMDKNDFDPKTFFSIHDVDSNGYWDEAEVKALFVKELDKVYQSDLPEDDMRERAEEMERMREHYFQETDMNHDGLISIDEFMVQTNKEEFQKDPEWETIDRQQQYTHEEYLEYERRRQEEVQRLIAQGQLPPHPNMPQGYYAAPPPGGVAYQQAPPGAQLHYQHPDQVHAQQQQQYAQQQQQYAQQYQQQQYGNGQQPVQLQPNQVYQHAGQIPQQQQPVYQNQPVYQQQQPVYQQQQPVQQQQKPVQQPVQQQPVQQQQQTAQQQPVAQQQIHNQSPPPVLNQQVPVQQQQKQHQESLNQQH
Protein: Amino acid--[acyl-carrier-protein] ligase (EC 6.2.1.n2) (Amino acid:[carrier-protein] ligase [AMP forming]) (aa:CP ligase) (Aminoacyl-[acyl-carrier-protein] synthetase) (L-alanine:[acyl-carrier-protein] ligase) (L-glycine:[acyl-carrier-protein] ligase) (L-serine:[acyl-carrier-protein] ligase) (Q7CWR3)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Catalyzes the ATP-dependent activation of L-alanine, and to a lesser extent of L-glycine and L-serine, and their transfer to the phosphopantetheine prosthetic group covalently attached to the vicinal carrier protein Atu2571 of yet unknown function. May participate in nonribosomal peptide synthesis or related processes. L-proline and L-glutamate are very poor substrates whereas D-amino acids are not substrates for ATP-dependent activation. Does not display tRNA aminoacylation activity.
Interaction partners:
- Aminoacyl carrier protein
- Acyl-CoA dehydrogenase
- Uncharacterized protein
- beta-mannosidase
- Serine aminopeptidase S33 domain-containing protein
- (S)-ureidoglycine aminohydrolase cupin domain-containing protein
Sequence:
MTVFSAIPPISCWFTGRTPASWDKTMDMQTSFLDRLFEEGLLIETGVDGLYGRSGQFEDVIAAFERLIDRTGGADGAEAIRFPPGINRAYFEKSGYMKSFPQLAGTVHSFCGCELDHVSLLKSMDEGGDWTKDQKATDIVLTPAACYPLYPTIAKRGALPAGGGLYDIQSYCFRHEPSKDPARQQLFRMREYVCMGTESDVTEFRQTWMDRGVEMMKAVGLDVTIDIANDPFFGRAGKMLANNQRDQNLKFELLIPVTSATNPTACMSFNYHQDAFGQKWGLNLENGDVAHTACVGFGLERIALALFAHHGLDVKKWPAKVVETLWG