wanglab/gogpt-training-data huggingface dataset:
Protein: Tubulin gamma-2 chain (Gamma-2-tubulin) (Q9NRH3)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000305}.
Interaction partners:
- Gamma-tubulin complex component 2
- Gamma-tubulin complex component 3
- Gamma-tubulin complex component 5
- Tubulin gamma-1 chain
- Gamma-tubulin complex component 6
- Gamma-tubulin complex component 4
- Mitotic spindle organizing protein 2B
- Mitotic-spindle organizing protein 2A
- Mitotic-spindle organizing protein 1
- Nucleoside diphosphate kinase homolog 7
Sequence:
MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSPYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPYQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQFDKLRKRDAFLEQFRKEDMFKDNFDEMDRSREVVQELIDEYHAATQPDYISWGTQEQ
Protein: Growth arrest-specific 6 (Growth arrest-specific protein 6 precursor) (Q7T3H4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRELVWSFCLVLLCSGFCSPVSVSSRQAHQFLRRTRRANQVFEETKQGHLERECVEEKCTKEEAREVFENDPETEYFYPKYQACMERFGDSEKKKQDLITCVHNIPDQCSPNPCYHYGTVRCEDKKGEFRCHCFTGWSGATCQNDVDECISGNGGCEHVCNNTMGSYKCSCEDGYRLSGHHSCLDVDECVETPDVCGSAHCSNLIGGLECLCDEGFIYDNISRSCVDVDECETHVCEEECVNTPGSFRCFCDGRLGKRLSSDMRSCESIGLDRPLDMRRNSRSLYLGRMFSGIPVVRLRFRRRVQTGFTAEFDLRTFDPEGVIFFAGGHLNSSWIVLLVHHGKLELQLKYGVVSRVTSSGPQVNDGQWHKISVEEQGRSLVIKIDREAVMKIAVNGDLFTLNKNMHELNLTVGGVPFRDDGLVSRVNPRLDGCMKDWRWLTGEDTSIQETIRHNERMQCYAVEDHSAFYPGHGFAYFNHSHGDNQTLSVHVTLRAASSMGVLFALVRQDRVPFSISLSDYHPGTLQWTKHVLVSLGDVVVGSVPVNLSDGQTHTVNVTMSGNDSVLEVDAQLAQMEMMEGVDSLDLTSSYSTFIGGIPDVSLVSSPVSAFFTGCMDVRVNGQLLDVDEAQHKHNDIRSHSCPLVDTLQ
Protein: Retinoblastoma family protein (Q24472)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions in cell cycle regulation. Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of developmentally controlled E2F target genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:8675008}.
Interaction partners:
- Transcription factor E2F2
- Transcription factor E2f1
- Lin-52, isoform A
- Transcription factor Dp
- Chromatin assembly factor 1 p55 subunit
- LD07342p
- LD06557p
- Protein lin-54 homolog
- Cyclin D, isoform D
- G1/S-specific cyclin-E
Sequence:
MSEPDPQELGAEVVSGLVATSDDRLEMINAEYTNLCRDLNMDRQTELQGYETYLEVSQRCSMEGTASHWMCCAIYTACRRTSTPTVTGQNAVVKGNCVSLNNLLRCCKMSIYEFKTKIKQWCDMANLPQEFVNEIEDLDRKFSITFMLHKRFRIIMDMIFSCPPNEKKHSKYISLHGNHAHGKCSYIKLDDICWRLFLCAKNQKPSNTVDLVTSYNLMICCIDLIYNNVLAEKRTDLINPKFEGLPSNWTELDFRHNPHCILSNFCDMTEEAKAMKATTFRQIMSSFFQASTIYGNKDTMLGLLANENFERNLKSLNISYEQYVLSVGEFDERILSAYDAGEHTALNDQSLRPPVTPLTRKQDLPAQPAMAGDKFEPVRNATNNVKQLSAFGRITEPTDFVKQAGEEVIAKLLSIIEEIEQKFLAKYPSTEAKSRFQLAKSFFFYLLDQILQAEIRNKPDIDLKRLLVQKVSLVIFNITLMACCVELVLEAYKTELKFPWVLDCFSISAFEFQKIIEIVVRHGSHEGCLNRSLIKHLNSIEETCLERLAWARNSTVWEMIASAQLPLPTWLMVNLDRAAGPLQIFLRKVYLLGWLRIQKLCSELSLCEKTPESIWHIFEHSITHETELMKDRHLDQNIMCAIYIYIRVKRMEDPKFSDIMRAYRNQPQAVNSVYREVFIDINEDGEPKVKDIIHFYNHTYVPLMRQFVIDYLNVTPDVSGRASDLQLSPHPKERAAQPKKVTQSHSLFVSQMSKNEIQQSPNQMVYSFCRSPAKDLQAMNEKVRGGKRMLSFGDEPGLGTMAETKRSKISQVKAVMDDPELQSAEQQTAVTTEGCVGGEGGEHET
Protein: Golgin A2 (A0A087WYC0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
EKKECHQKQGALREQLQVHIQTIGILVSEKAELQTALAHTQHAARQKEGESEDLASRLQYSRRRVGELERALSAVSTQQKKADRYNKELTKERDALRLELYKNTQSNEDLKQEKSELEEKLRVLVTEKAGMQLNLEELQKKLEMTELLLQQFSSRCEAPDANQQLQQAMEERAQLEAHLGQVMESVRQLQMERDKYAENLKGESAMWRQRMQQMSEQVHTLREEKECSMSRVQELETSLAELRNQMEPPAGPSEVEQQLQAEAEHLRKELEGLAGQLQAQVQDNEGLSRLNREQEERLLELERAAELWGEQAEARRQILETMQNDRTTISRALSQNRELKEQLAELQSGFVKLTNENMEITSALQSEQHVKRELGKKLGELQEKLSELKETVELKSQEAQSLQQQRDQYLGHLQQYVAAYQQLTSEKEVLHNQLLLQTQLVDQLQQQEAQGKAVAEMARQELQETQERLEAATQQNQQLRAQLSLMAHPGEGDGLDREEEEDEEEEEEEAVAVPQPMPSIPEDLESREAMVAFFNSAVASAEEEQARLRGQLKEQRVRCRRLAHLLASAQKEPEAAAPAPGTGGDSVCGETHRALQGAMEKLQSRFMELMQEKADLKERVEELEHRCIQLSGETDTIGEYIALYQSQRAVLKERHREKEEYISRLAQDKEEMKVKLLELQELVLRLVGDRNEWHGRFLAAAQNPADEPTSGAPAPQELGAANQQGDLCEVSLAGSVEPAQGEAREGSPRDNPTAQQIMQLLREMQNPRERPGLGSNPCIPFFYRADENDEVKITVI
Protein: Cyclin-L1-1 (CycL1;1) (Arginine-rich cyclin 1) (AtRCY1) (Protein MODIFIER OF SNC1 12) (Q8RWV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cognate cyclin for CDKG1. Required for synapsis and male meiosis, and for the proper splicing of specific resistance (R) genes. Involved in regulation of DNA methylation and transcriptional silencing.
Subcellular location: Nucleus {ECO:0000269|PubMed:22248079}.
Interaction partners:
- Cyclin-dependent kinase G1
- Disease resistance protein RPP8
- Pre-mRNA-splicing factor SPF27 homolog
- Transportin MOS14
- Pre-mRNA-processing factor 19 homolog 2
- Partner of Y14 and mago
- Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1
- Protein PATRONUS 1
- Protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1
- Pre-mRNA-processing factor 19 homolog 1
Sequence:
MIYTAIDNFYLSDEQLKASPSRKDGIDETTEISLRIYGCDLIQEGGILLKLPQAVMATGQVLFQRFYCKKSLAKFDVKIVAASCVWLASKLEENPKKARQVIIVFHRMECRRENLPLEHLDMYAKKFSELKVELSRTERHILKEMGFVCHVEHPHKFISNYLATLETPPELRQEAWNLANDSLRTTLCVRFRSEVVACGVVYAAARRFQVPLPENPPWWKAFDADKSSIDEVCRVLAHLYSLPKAQYISVCKDGKPFTFSSRSGNSQGQSATKDLLPGAGEAVDTKCTAGSANNDLKDGMVTTPHEKATDSKKSGTESNSQPIVGDSSYERSKVGDRERESDREKERGRERDRGRSHRGRDSDRDSDRERDKLKDRSHHRSRDRLKDSGGHSDKSRHHSSRDRDYRDSSKDRRRHH
Protein: Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (C8V449)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Phosphoribosylamine-glycine ligase
- Amidophosphoribosyltransferase
- Phosphoribosylformylglycinamidine synthase
- Adenylosuccinate lyase
- Adenylosuccinate lyase C-terminal domain-containing protein
- Phosphoribosylglycinamide formyltransferase
- Hypothetical bifunctional AICARFT/IMPCHase bienzyme
- Formyltetrahydrofolate deformylase, putative
- C-1-tetrahydrofolate synthase, cytoplasmic
Sequence:
MWNSRKVGVLGGGQLGRMFVESANRLNIQCNILDAENSPAKQISAHDDHVTGSFKEREAVRELAKKCDVITAEIEHVDTYALEEIASQVQIEPSWQAIRTIQNKFNQKEHLAKHGIPMAEHRELVENTPEQLAKAGEELGYPLMLKSKTMAYDGRGNYRVNSKDDIPDALEFLKGRPLSQELAVMVIKTKDAVLSYPTVETVQEDSICKLVYAPARNVPEHINQAAQKLARKAVATFEGKGAFGVEMFLMNDNSLLLCELASRVHNSGHYTIEGTALSQFDAHLRAILDLPIPPESLQLRQPSIMLNIIGGSAPDTHLKAAEAALSIPNASIHLYSKGDAKPGRKMGHVTVTASTMHKAEEYIQPLIDVVDEIRSQRQDIKTNPAPSGVTKPPPQVAVMMGSDSDLKTLVPGLKLLRDKFGIEPAVDITSAHRTPTFMAEYSASAAARGIKVIIAAAGGAAHLPGMAAAHTALPVIGVPVKGSSLDGVDSLYSIVQMPRGVPVATVGINNSINAALLAARIIGAFDPDVQRKVEEYAEDARKENMDMKNVKMQDLGWEKYFNQM
Protein: Splicing factor U2AF 26 kDa subunit (U2 auxiliary factor 26) (U2 small nuclear RNA auxiliary factor 1-like protein 4) (U2AF1-like 4) (U2(RNU2) small nuclear RNA auxiliary factor 1-like protein 3) (U2 small nuclear RNA auxiliary factor 1-like protein 3) (U2AF1-like protein 3) (Q8WU68)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that function as a pre-mRNA splicing factor. Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Acts by enhancing the binding of U2AF2 to weak pyrimidine tracts. Also participates in the regulation of alternative pre-mRNA splicing. Activates exon 5 skipping of PTPRC during T-cell activation; an event reversed by GFI1. Binds to RNA at the AG dinucleotide at the 3'-splice site (By similarity). Shows a preference for AGC or AGA (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8BGJ9}. Nucleus speckle {ECO:0000250|UniProtKB:Q8BGJ9}. Cytoplasm {ECO:0000250|UniProtKB:Q8BGJ9}. Note=Interaction with C1QBP is required for the nuclear translocation. Displays active nucleo-cytoplasmic shuttling. {ECO:0000250|UniProtKB:Q8BGJ9}.
Interaction partners:
Sequence:
MAEYLASIFGTEKDKVNCSFYFKIGVCRHGDRCSRLHNKPTFSQTIVLLNLYRNPQNTAQTADGSHCHVSDVEVQEHYDSFFEEVFTELQEKYGEIEEMNVCDNLGDHLVGNVYVKFRREEDGERAVAELSNRWFNGQAVHGELSPVTDFRESCCRQYEMGECTRGGFCNFMHLRPISQNLQRQLYGRGPRRRSPPRFHTGHHPRERNHRCSPDHWHGRF
Protein: Adenylate cyclase type 4 (EC 4.6.1.1) (ATP pyrophosphate-lyase 4) (Adenylate cyclase type IV) (Adenylyl cyclase 4) (P26770)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1946437}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8NFM4}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 6
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Rap guanine nucleotide exchange factor 4
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 8
- Rap guanine nucleotide exchange factor 3
- Protein kinase C gamma type
- Protein kinase C delta type
Sequence:
MARLFSPRPPPSEDLFYETYYSLSQQYPLLILLLVIVLCAIVALPAVAWASGRELTSDPSFLTTVLCALGGFSLLLGLASREQQLQRWTRPLSGLIWAALLALGYGFLFTGGVVSAWDQVSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVLGLYLGWRPESQRDLLPQLAANAVLFLCGNVVGAYHKALMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMKAEIMARLQAGQSSRPENTNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKLRVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVERADMEHRDPYLRELGEPTYLVIDPWAEEEDEKGTERGLLSSLEGHTMRPSLLMTRYLESWGAAKPFAHLSHVDSPASTSTPLPEKAFSPQWSLDRSRTPRGLHDELDTGDAKFFQVIEQLNSQKQWKQSKDFNLLTLYFREKEMEKQYRLSALPAFKYYAACTFLVFLSNFTIQMLVTTRPPALATTYSITFLLFLLLLFVCFSEHLTKCVQKGPKMLHWLPALSVLVATRPGLRVALGTATILLVFTMAVVSLLFLPVSSDCPFLAPNVSSVAFNTSWELPASLPLISIPYSMHCCVLGFLSCSLFLHMSFELKLLLLLLWLVASCSLFLHSHAWLSDCLIARLYQGSLGSRPGVLKEPKLMGAIYFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENVLPAHVAPQLIGQNRRNEDLYHQSYECVCVLFASIPDFKEFYSESNINHEGLECLRLLNEIIADFDELLSKPKFSGVEKIKTIGSTYMAATGLNATPGQDTQQDAERSCSHLGTMVEFAVALGSKLGVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVLGKIQVTEETARALQSLGYTCYSRGVIKVKGKGQLCTYFLNTDLTRTGSPSAS
Protein: RAN binding protein 1, isoform CRA_g (Testis secretory sperm-binding protein Li 221n) (A0A140VK94)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAKDTHEDHDTSTENTDESNHDPQFEPIVSLPEQEIKTLEEDEEELFKMRAKLFRFASENDLPEWKERGTGDVKLLKHKEKGAIRLLMRRDKTLKICANHYITPMMELKPNAGSDRAWVWNTHADFADECPKPELLAIRFLNAENAQKFKTKFEECRKEIEEREKKAGSGKNDHAEKVAEKLEALSVKEETKEDAEEKQ
Protein: Dynein axonemal assembly factor 10 (WD repeat-containing protein 92) (WD repeat-containing protein Monad) (Q96MX6)
Organism: Homo sapiens (Human)
Function: Key assembly factor specifically required for the stability of axonemal dynein heavy chains in cytoplasm.
Subcellular location: Dynein axonemal particle {ECO:0000250|UniProtKB:A8J3F6}.
Interaction partners:
- Protein UXT
- Prefoldin subunit 2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- RNA polymerase II-associated protein 3
- p53 and DNA damage-regulated protein 1
- Prefoldin subunit 6
- PIH1 domain-containing protein 1
- Unconventional prefoldin RPB5 interactor 1
- RuvB-like 2
- RuvB-like 1
Sequence:
MSAFEKPQIIAHIQKGFNYTVFDCKWVPCSAKFVTMGNFARGTGVIQLYEIQHGDLKLLREIEKAKPIKCGTFGATSLQQRYLATGDFGGNLHIWNLEAPEMPVYSVKGHKEIINAIDGIGGLGIGEGAPEIVTGSRDGTVKVWDPRQKDDPVANMEPVQGENKRDCWTVAFGNAYNQEERVVCAGYDNGDIKLFDLRNMALRWETNIKNGVCSLEFDRKDISMNKLVATSLEGKFHVFDMRTQHPTKGFASVSEKAHKSTVWQVRHLPQNRELFLTAGGAGGLHLWKYEYPIQRSKKDSEGIEMGVAGSVSLLQNVTLSTQPISSLDWSPDKRGLCVCSSFDQTVRVLIVTKLNKI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (M9PFM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQKENNVTAENCQFVGPYRLEKTLGKGQTGLVKLGVHCVIGKKVAIKIINREKLSESVLMKVEREIAIMKLIDHPHVLGLSDVYENKKYLYLILEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPAGSMLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFVPPDCQSLLRGMIEVNPDRRLTLAEINRHPWVTAGGKGELELELPMMEVVQTHVIPTATAVDPDVLNAICSLGCFKEKEKLIQELLSSSHNTEKVIYFLLLERKRRRPALEDDDEIAQKSRSELDAVDPPRKRLDTCRINGTNAPSYGQISEGSPLTPRRQAFNFRSYSSTRNHQRRSPTTVTSSVRSSSYHSPTRCNSPMSSAQQQANAISRPSSPAAGTRHSTYGDRDRSGHHSSVSRTPSHSSQKSIEGDVVVVREPRIERRDSLRQERGGGSPRDRGDCGIPPGSPGGNSSGSTSASPSVHHRANSGPTIAIIVNPNGSPMMNNSSPGMPGSPCNTPGGQLWKTRLTNIKNSFLGSPRFHRRKMQVSADEVHLTPESSPELTKRSWFGNLITTEKDETFTILVKGKPIATVKAHLIHAFLSMAELSHSVVSPTSFRVEYKRNGNGPVMFQRHVKFQVDISAICKQGDIADMLFALTFTLLSGNIRRFRRICEHIQSQVCSKRFPGPSSPPTVTSVTQAVSESSSCGSVSSERLSYKRQVIENDMENDSIFSYKSGNGRRASTTNNNNANPVDIPGSPIAVRSNSETAEHERNRELQSERQATTMSGSAIA
Protein: Protein ABHD14A (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 14A) (Abhydrolase domain-containing protein 14A) (Down-regulated in Zic-1-mutant protein) (Q922Q6)
Organism: Mus musculus (Mouse)
Function: Possible role in granule neuron development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14667578}. Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Aminoacylase-1
Sequence:
MVQKFMSRYQAALLGLGLLLVFLLYMGLPGPPEQTSRLWRGPNVTVLTGLTRGNSRIFYREVLPIQQACRAEVVFLHGKAFNSHTWEQLGTLQLLSERGYRAVAIDLPGFGNSAPSEEVSTEAGRVELLERVFQDLQVQNTVLVSPSLSGSYALPFLMQNHHQLRGFVPIAPTYTRNYAQEQFRAVKTPTLILYGELDHTLARESLQQLRHLPNHSMVKLRDAGHACYLHKPEAFHLALLAFLDHLP
Protein: Serine/threonine-protein kinase oca2 (EC 2.7.11.1) (O59763)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Overexpression causes cell cycle arrest.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Barrier septum. Cell tip. {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 10 kDa heat shock protein, mitochondrial
- Uncharacterized transcriptional regulatory protein C2H10.01
- Uncharacterized transcriptional regulatory protein C15D4.02
- Meiotically up-regulated gene 24 protein
- Uncharacterized mitochondrial carrier C1271.11
- Transcription factor fil1
Sequence:
MSVTPPNVQFNLNGDSDHKSDNSSSSLENKLDTELKITSPPRNPPQRLHPVDFSEHADTDDDMNHPLPRVQSPVHIKNHIDPKLAEDRYRSSAARHFEPISIPPSAITSEDEDDYHGSANSSTVLPPRTENALHAASPKPSGSTGYTSPALSQNSGSGGEGESDEGSFNTQHHRSPIFQAYPSSEDLVGDPNDPYRRTRRAPIKTNPHDIPSQFIFRKLGLHHGKHGHHGHSGSLSLKSLVPNHHDKHDKHDKHEKHHSSLDLRRFFKSHQKTDKEKKPSVSKSKSSANLQDDHFGLFKKYGKFGRMLGSGAGGSVRIMKRSSDGKIFAVKEFRARRPTETEREYARKVTAEFCIGSALHHTNIIETLDIVEENKKFYEVMEYAPYDMFSIVMSGKMTMPEVYCCFKQLLSGVAYLHSMGLAHRDLKLDNLVVDSNCFVKIIDFGSAVVFKYPFEADIVEATGVVGSDPYLAPETLVRKLYDPRAVDIWSSAIIFCCMALRRFPWKYPKLSDNSFRLFCMKQPSNDAESPSDILADIKKQRLVEQGCEPIRKTDESHSPNSKTDNSSTHKQELYGPWRLLRLLPRETRAVIAHMLELDPVKRYDIHRVFADNWINDISMCHMENGKVIHSPTHVHNLVASEESPAPPAKH
Protein: DNA repair nuclease/redox regulator APEX1 (APEN) (REF-1) (EC 3.1.11.2) (EC 3.1.21.-) (APEX nuclease) (Apurinic-apyrimidinic endonuclease 1) (Redox factor-1) [Cleaved into: DNA repair nuclease/redox regulator APEX1, mitochondrial] (Q5TZP7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus {ECO:0000256|RuleBase:RU362131}. Cytoplasm {ECO:0000256|RuleBase:RU362131}. Mitochondrion {ECO:0000256|RuleBase:RU362131}.
Interaction partners:
Sequence:
MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL
Protein: Small ribosomal subunit protein eS32 (60S ribosomal protein L41) (HG12) (Large ribosomal subunit protein eL41) (P62945)
Organism: Homo sapiens (Human)
Function: Interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase II alpha by CKII.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
Sequence:
MRAKWRKKRMRRLKRKRRKMRQRSK
Protein: Maltose fermentation regulatory protein MAL63 (P10508)
Organism: Saccharomyces cerevisiae (Baker's yeast)
Function: Regulates the coordinate transcription of structural MAL6S (maltase) and MAL6T (maltose permease) genes.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MGIAKQSCDCCRVRRVKCDRNKPCNRCIQRNLNCTYLQPLKKRGPKSIRAGSLKKIAEVQMVSMNNNIMAAPVVCKKVPKNLIDQCLRLRLYHDNLYVIWPMLSYDDLHKLLEEKYDDRCAYWFLVSLSAATLSDLQIEIEYEEGVTFTGEQLCTLCMLSRQFFDDLSNSDIFRIMTYYCLHRCYAQFADTRTSYRLSCEAVGLIIKIAGFHREETYEFLPFGEQQLRRKVYYLLLMTERFYAVYIKCVTSLDATIAPPLPEVVTDPRLSLESFLEVIRVFTIPGKCFYDALATNCVDDSCTEDSLKRIRNELHTTSLDIEPWSYGYIDFLFSRHWVRTLAWKLVLHMKGMRMNFLSNTNNTHIPVEIARDMLGDTFLTPKNLYDVHGPGIPMKALEIANALVDVVNKYDHNMKLEAWNVLYDVSKFVFSLKHCNNKMFDRFSTKCQGALITLPISKPLQLNDNSKDEDDIIP
Protein: Feruloyl esterase B (EC 3.1.1.73) (Cinnamoyl esterase) (Ferulic acid esterase B) (FAEB) (Q9HE18)
Organism: Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum)
Function: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin. Binds strongly to cellulose.
Subcellular location: Secreted {ECO:0000269|PubMed:11082184}.
Interaction partners:
Sequence:
MAIPLVLVLAWLLPVVLAASLTQVNNFGDNPGSLQMYIYVPNKLASKPAIIVAMHPCGGSATEYYGMYDYHSPADQYGYILIYPSATRDYNCFDAYSSASLTHNGGSDSLSIVNMVKYVISTYGADSSKVYMTGSSSGAIMTNVLAGAYPDVFAAGSAFSGMPYACLYGAGAADPIMSNQTCSQGQIQHTGQQWAAYVHNGYPGYTGQYPRLQMWHGTADNVISYADLGQEISQWTTIMGLSFTGNQTNTPLSGYTKMVYGDGSKFQAYSAAGVGHFVPTDVSVVLDWFGITSGTTTTTTPTTTPTTSTSPSSTGGCTAAHWAQCGGIGYSGCTACASPYTCQKANDYYSQCL
Protein: Tubulin polyglutamylase complex subunit 2 (PGs2) (Q68CL5)
Organism: Homo sapiens (Human)
Function: Subunit of the tubulin polyglutamylase complex (TPGC). The complex mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:34782749}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:34782749}. Note=Associated with microtubules. {ECO:0000269|PubMed:34782749}.
Interaction partners:
- Nicolin-1
- Leucine-rich repeat-containing protein 49
- Polyglutamylase complex subunit TTLL1
- Tubulin polyglutamylase complex subunit 1
- Centriolar satellite-associated tubulin polyglutamylase complex regulator 1
- Protein hinderin
Sequence:
MEEEASSPGLGCSKPHLEKLTLGITRILESSPGVTEVTIIEKPPAERHMISSWEQKNNCVMPEDVKNFYLMTNGFHMTWSVKLDEHIIPLGSMAINSISKLTQLTQSSMYSLPNAPTLADLEDDTHEASDDQPEKPHFDSRSVIFELDSCNGSGKVCLVYKSGKPALAEDTEIWFLDRALYWHFLTDTFTAYYRLLITHLGLPQWQYAFTSYGISPQAKQWFSMYKPITYNTNLLTEETDSFVNKLDPSKVFKSKNKIVIPKKKGPVQPAGGQKGPSGPSGPSTSSTSKSSSGSGNPTRK
Protein: DIP1-d splice isoform (Q86LT0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNRNRRAFAGNNKPFVFGGIYRTRDKKLRQNRQLRKSMLPKNALMALNEVKGVTISDFTIDSNTDGGFTAVVTVNSNQYEGKGTSKMTAKNAACEKAWRDFIIAKMTPKPPRIHQVEMGSEPMDINEDEADAPDDDLPMLNLASFAIYKLFAEWEREGYVVPEMHPSANAAQQAGGDAGTPVPPVPKEPKKPPVRTELPSGWETMHPATILCIMRPGLNYVDYGSSGDKTNGMQHLGIMVDNQEFHANGRSKKIARRNVAVKVCNSLFGTNFTYSDTT
Protein: Spindle defective protein 3 (Q9TYY7)
Organism: Caenorhabditis elegans
Function: In the first mitotic division in embryos, required for mitotic spindle alignment and asymmetric cell division. Required for motor-driven chromosome movement and homolog searching within the nucleus, and subsequently ensures homologous chromosome pairing during the prophase stage of meiosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17947426, ECO:0000269|PubMed:23671424}. Mitochondrion outer membrane {ECO:0000305|PubMed:17947426}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to mitochondria throughout interphase and mitosis (PubMed:17947426, PubMed:23671424). Localizes to mitochondria in the pachytene and transition zone regions of the germ cells (PubMed:23671424). {ECO:0000269|PubMed:17947426, ECO:0000269|PubMed:23671424}.
Interaction partners:
- C2H2-type domain-containing protein
- Spindle-defective protein 2
Sequence:
MDQMTVEEKILEHQELEDGSSSFRWLVSSTVIAIGGATVALYISGKIDWKIPAIEAGLALTAGGTITCGYLWFKKRVKTVRKLILQMNKTRSALRKRRQIFFSISMCMPRHRHPSILRACRLTVSAIECLTEETKSLNNGTTWQDLYTDEIREIISRSTVDSQLLKIEEIQEGDNDKMDFEQVFETLISIFKLHASEYSRVVILNFLNSPVFESKKVSKFFETLGRLQELMYNLESVERLALKTETKLSRNERKMDGKMKNKSLLELGWKQQTALALEAILERLESESVTQSEVESALHKTFLVVKAEPAFPQPVKKIDVEVKNQDQKNPEVIVIEKGTGERTDIDMVFEGTPLSEADKLSASKSAVARDVLLDGSEGRCHEASLFGELKMVLEPRRTDFAKRERTALAKFYGVDEHQLEQKEDEETFEAIASGDGEDPDPYDWRKDAEMSAGIHHDANNDDFLKSLKLRRVDDDIIE
Protein: Sorting nexin (A0A8I6AME1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}.
Interaction partners:
Sequence:
MYDFAAEPGNNELTVNEGEIITITNPNVGGGWLEGKNSKGEQGLVPTDYVEILPNDGKDPFSCGNSVADQAFLDSLSASTAQANSSSANSNNQVGGGSDPWSAWNAPRSGNWDSSDAWGTRTDGAGAQRNSSANNWDTGFGHPQAYQGPVLTPSPWNHGCFPPRSSSLGFMNLLAEAGEAGSRASSAVYASVKLAWASKTFKSVSQNHLVLSLAQVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVVSESEVFQQFLNFRDEKEWKTGKRKAEKDELVGVMIFSTMEPEAPDLDLIEIEQKCDAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLAAVFSSSGYQGETDLNNAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGAHKGAIEKVKESDKLVATSKITPQDKQTMVKRVGTMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETVSAPLPTSLYAYVCVRGASMLRDLDHIELVSL
Protein: Marker for oxidative stress response protein (Q9SIJ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 1
- Myosin heavy chain-related protein
- CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase
- Putative F-box protein At1g26510
- Seed dormancy control protein
- Disease resistance protein RPP1-WsB, putative domain family protein)
- Ubiquinol oxidase 1a, mitochondrial
- Defensin-like protein 195
- protein-synthesizing GTPase
- At5g27290
Sequence:
MASQTNQTVVDTKKIETENPPKPQVPASSCRKRVKDDNATFFANLKDHMDEFIHASMDEHKTCFKNTMDKIFGSFSKAEAVAEKQIEAKEVVEIHSPLQTAVTK
Protein: Alanine dehydrogenase (EC 1.4.1.1) (Stage V sporulation protein N) (Q08352)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the reversible oxidative deamination of L-alanine to pyruvate. Oxidative deamination proceeds through a sequential, ordered ternary-binary mechanism, where NAD(+) binds first followed by L-alanine; the products are released in the order ammonia, pyruvate and NADH (Probable). Disruption blocks sporulation probably in stage V; 20-30% sporulation can be restored if the media is supplemented with pyruvate, suggesting lack of pyruvate blocks sporulation. Thus it is a key factor in the assimilation of L-alanine as an energy source via the tricarboxylic acid cycle during sporulation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A0QVQ8}.
Interaction partners:
- Alanine racemase 1
- Alanine racemase 2
- DNA-binding transcriptional activator AdeR
Sequence:
MIIGVPKEIKNNENRVALTPGGVSQLISNGHRVLVETGAGLGSGFENEAYESAGAEIIADPKQVWDAEMVMKVKEPLPEEYVYFRKGLVLFTYLHLAAEPELAQALKDKGVTAIAYETVSEGRTLPLLTPMSEVAGRMAAQIGAQFLEKPKGGKGILLAGVPGVSRGKVTIIGGGVVGTNAAKMAVGLGADVTIIDLNADRLRQLDDIFGHQIKTLISNPVNIADAVAEADLLICAVLIPGAKAPTLVTEEMVKQMKPGSVIVDVAIDQGGIVETVDHITTHDQPTYEKHGVVHYAVANMPGAVPRTSTIALTNVTVPYALQIANKGAVKALADNTALRAGLNTANGHVTYEAVARDLGYEYVPAEKALQDESSVAGA