wanglab/gogpt-training-data huggingface dataset:
Protein: Heterogeneous nuclear ribonucleoprotein H3 (hnRNP H3) (Heterogeneous nuclear ribonucleoprotein 2H9) (hnRNP 2H9) (P31942)
Organism: Homo sapiens (Human)
Function: Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction.
Subcellular location: Nucleus {ECO:0000269|PubMed:8999868}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein H
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein D-like
- Heterogeneous nuclear ribonucleoprotein D0
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Heterogeneous nuclear ribonucleoprotein A0
- Heterogeneous nuclear ribonucleoprotein F
- TAR DNA-binding protein 43
Sequence:
MDWVMKHNGPNDASDGTVRLRGLPFGCSKEEIVQFFQGLEIVPNGITLTMDYQGRSTGEAFVQFASKEIAENALGKHKERIGHRYIEIFRSSRSEIKGFYDPPRRLLGQRPGPYDRPIGGRGGYYGAGRGSMYDRMRRGGDGYDGGYGGFDDYGGYNNYGYGNDGFDDRMRDGRGMGGHGYGGAGDASSGFHGGHFVHMRGLPFRATENDIANFFSPLNPIRVHIDIGADGRATGEADVEFVTHEDAVAAMSKDKNNMQHRYIELFLNSTPGGGSGMGGSGMGGYGRDGMDNQGGYGSVGRMGMGNNYSGGYGTPDGLGGYGRGGGGSGGYYGQGGMSGGGWRGMY
Protein: Arogenate dehydratase/prephenate dehydratase 6, chloroplastic (AtADT6) (AtPDT6) (EC 4.2.1.51) (EC 4.2.1.91) (Q9SGD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine. Dehydratase that uses arogenate and prephenate as substrates. Utilzes more efficiently arogenate than prephenate.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19136569}.
Interaction partners:
- Arogenate dehydrogenase 2, chloroplastic
- Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
- Chorismate mutase 1, chloroplastic
- Arogenate dehydrogenase 1, chloroplastic
- Chorismate mutase 2
- Chorismate mutase 3, chloroplastic
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Probable aminotransferase TAT4
- Tyrosine aminotransferase
- Probable aminotransferase TAT1
Sequence:
MKALSSSSPILGASQPATATALIARSGRSEWQSSCAILTSKVISQEESESLPVPPVSGGVDHLNGHNSAAARVPGMNLVPIEKSDSNPLVPQHRHNPLKPLSMTDLSPAPMHGSNLRVAYQGVPGAYSEAAAGKAYPNCQAIPCDQFEVAFQAVELWIADRAVLPVENSLGGSIHRNYDLLLRHRLHIVGEVQLPVHHCLLALPGVRKEFLTRVISHPQGLAQCEHTLTKLGLNVAREAVDDTAGAAEFIASNNLRDTAAIASARAAEIYGLEILEDGIQDDVSNVTRFVMLAREPIIPRTDRPFKTSIVFAHEKGTSVLFKVLSAFAFRDISLTKIESRPNHNRPIRVVDDANVGTAKHFEYMFYVDFEASMAEARAQNALAEVQEFTSFLRVLGSYPMDMTPWSPTSSTSS
Protein: Dro1 protein (Drosomycin-like 1) (Drosomycin-like C1) (GEO11745p1) (RT02921p) (Q9VZQ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dorsal-related immunity factor Dif
- Embryonic polarity protein dorsal
Sequence:
MEIKFLIVLSAVLMIIFLGAEESHADCLSGRYRGSCAVWHRKKCVDICQREGRTSGHCSPSLKCWCEGC
Protein: IQ motif and SEC7 domain-containing protein 2 (Q5DU25)
Organism: Mus musculus (Mouse)
Function: Is a guanine nucleotide exchange factor for the ARF GTP-binding proteins.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- BAR/IMD domain-containing adapter protein 2
- Disks large homolog 4
- Ras/Rap GTPase-activating protein SynGAP
- ADP-ribosylation factor 6
Sequence:
MEAGSGPPGGPGSESPNRAVEYLLELNNIIESQQQLLETQRRRIEELEGQLDQLTQENRDLREESQLHRGELHRDPLGARDSPGRESQYQNLRETQFHHRELRESQFHQASRDVGYPNRDGAYQNREAIYRDKEREASYQLQDTTGYTARERDVAQCHLHHENPALGRERGGREAGPAHPGREKEAGYSAAVGVGQRPPRERGQLSRGASRSSSPGAGGGHSTSTSTSPATTLQRNVEGDAPGSDLSTAVDSPGSQPPYRLSQLPPTSSHMGGPPAGVGLPWAQRARLQPASVALRKQEEEEIKRSKALSDSYELSTDLQDKKVEMLERKYGGSFLSRRAARTIQTAFRQYRMNKNFERLRSSASESRMSRRIILSNMRMQFSFEEYEKAQNPAYFEGKPASLDEGAMAGARSHRLERGLPYGGSCGGGIDGGGSSVTTSGEFSNDITELEDSFSKQVKSLAESIDEALNCHPSGPMSEEPGSAQLEKRESKEQQEDSSATSFSDLPLYLDDPVPPPSPERLPSTEPPPQGRPEFWAPAPLPPVPPPMPPGTREDGSREEGTRRGPGCLECRDFRLRAAHLPLLTIEPPSDSSVDLSDRSDRGSVHRQLVYEADGCSPHGTLKHKGPPGRAPIPHRHYPAPEGPAPAPPGPLPPAPNSGTGPSGVAGGRRLGKCEAAGENSDGGDNESLESSSNSNETINCSSGSSSRDSLREPPATGLCKQTYQRETRHSWDSPAFNNDVVQRRHYRIGLNLFNKKPEKGIQYLIERGFLSDTPVGVAHFILERKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSSMDLDDALRKFQSHIRVQGEAQKVERLIEAFSQRYCVCNPALVRQFRNPDTIFILAFAIILLNTDMYSPSVKAERKMKLDDFIKNLRGVDNGEDIPRDLLVGIYQRIQGRELRTNDDHVSQVQAVERMIVGKKPVLSLPHRRLVCCCQLYEVPDPNRPQRLGLHQREVFLFNDLLVVTKIFQKKKILVTYSFRQSFPLVEMHMQLFQNSYYQFGIKLLSAVPGGERKVLIIFNAPSLQDRLRFTSDLRESIAEVQEMEKYRVESELEKQKGMMRPNASQPGGAKDSVNGTLARSSLEDTYGAGDGLKRGALSSSLRDLSDAGKRGRRNSVGSLDSTIEGSVISSPRPHQRMPPPPPPPPPEEYKSQRPVSNSSSFLGSLFGSKRGKGPFQMPPPPTGQASASSSSASSTHHHHHHHHHGHSHGGLGVLPDGQSKLQALHAQYCQGPGPAPPPYLPPQQPPLPPPPQQPPPLPQLGSIPPPPASAPPVGPHRHFHAHGPVPGPQHYTLGRPGRAPRRGAGGHPQFAPHGRHPLHQPTSPLPLYSPAPQHPPAHKQGPKHFIFSHHPQMMPAAGAAGGPGSRPPGGSYSHPHHPQSPLSPHSPIPPHPSYPPLPPPSPHTPHSPLPPTSPHGPLHASGPPGTANPPSANPKAKPSRISTVV
Protein: acid phosphatase (EC 3.1.3.2) (A0A0G2KB67)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Enamelin
- Amelotin
- FAM20A, golgi associated secretory pathway pseudokinase
Sequence:
MAEPRSQGHTVGPLLLLLLLLLPPQALPEGPLLFVALVFRHGDRAPLASYPTDPHKEAASTLWPRGLGQLTKEGIRQQLELGRFLRRRYKAFLSPEYRREEVYIRSTDFDRTLESAQANLAGLFPEAAPGSPEADWKPIPVHTVPVSEDKLLRFPMRSCPRYHELLRESTEAADYQEALEGWTDFLTRLGNFTGLSLVGEPLRRAWKVLDTLICQRAHGLALPSWASPDVLRTLSQISALDIRAHVGPPRAAEKAQLTGGILLDAILSNFSRAQRLGLPLKMVMYSAHDSTLLALQGALGLYDGNTPPYAACMAFEFRGSSREPEEEDGENVTVSLIYRNDTSRPPLPLRVPGCPAPCPLGRFQQLTAPARPPAHGAPCHGSYEPASPPDRWSILWKQAKGGQVRLCLTCPGPSSSPRFYPRRDRIKQHTPQRAMIQPFNRNSRRQKFQGCPPHPSTKSRSTLARGHLCSQGDQTQLEGASRGKGMV
Protein: Cold shock protein 1 (AtCSP1) (Cold shock domain-containing protein 1) (O65639)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone that binds to RNA, single- (ssDNA) and double-stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Exhibits a DNA melting activity. May be involved in cold resistance. Prevents seed germination under dehydration or salt stress conditions.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 4C
- Myb family transcription factor PHL13
- Eukaryotic translation initiation factor 4C
Sequence:
MASEDQSAARSTGKVNWFNASKGYGFITPDDGSVELFVHQSSIVSEGYRSLTVGDAVEFAITQGSDGKTKAVNVTAPGGGSLKKENNSRGNGARRGGGGSGCYNCGELGHISKDCGIGGGGGGGERRSRGGEGCYNCGDTGHFARDCTSAGNGDQRGATKGGNDGCYTCGDVGHVARDCTQKSVGNGDQRGAVKGGNDGCYTCGDVGHFARDCTQKVAAGNVRSGGGGSGTCYSCGGVGHIARDCATKRQPSRGCYQCGGSGHLARDCDQRGSGGGGNDNACYKCGKEGHFARECSSVA
Protein: CREB-H transcription factor homolog let-607 (Lethal 607 protein) (O44743)
Organism: Caenorhabditis elegans
Function: Probable transcription factor, required during migration of the gonadal distal tip cells (DTC). Probably regulates cell adhesion of DTCs via modulation of expression of genes involved in integrin-mediated adhesion, including tln-1, src-1, and integrin pat-2. Modulates expression of genes involved in protein trafficking during embryogenesis, including emo-1, sec-61, calu-1, sec-24.1, enpl-1, sar-1 and tfg-1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Membrane-bound transcription factor site-2 protease
- ER membrane protein complex subunit 4
Sequence:
MDQDFDLDEGAGQFNLKTTLMMFTSNDSQNDDGIWSPGSPYQALEDPSFLDKHFVSDPDRYTADELYSALEKMDGKSDLIGMDDMDNDNCYSLSPPDSGSLPISPASTSPSSYHSSGGEDLMDCYPSIDILQQASEELLYSKDDDYEICSSGPLLAYTNANSVATSAVHQNQQQQQRRLNQAGFPHQNSNGLVRFKSSQPRVLNPASISLNAPSSSFNPQSTSSTPATSSSSSSSTNGGFVKSSTGERRKYPPLRLDEEEIKLCKKEGICLPDFFPLTKAEERDLKRIRRKIRNKRSAQTSRKRKQDYIEQLEDRVSESTKENQALKQQIERLSSENQSVISQLKKLQAQLGQNAKRTTQAGRCLAVFMLSACLLVSPQLSPLGNQDNQKVLECIEEACQPSATSMNSANSAQRAIAGVTAPSVVIPSGGPVMVSTNANRQMNRNAVLNHHNNSKYPASGNQNHHPIALEDLNHPPPTLQPKQSYQQQHQPSMYRRSDETIAMAMAKIGARKGSSTSSSSASSVASSTSTSSATSPIYRTSRTLGAFEDQCDASSDDSNCANMPSLVPMKMSAQPPKRKIVTMNGQPRVTYRAVPASSVNVEQAQYYKVPQQKVQYVTMDRPIKYEVLQLNDYIKMEEESTIRLPNSWSTAGPRLHPQVNASSRTVRPLTVATPVHYNGPSAKKIKTQMF
Protein: E3 ubiquitin-protein ligase hecw-1 (EC 2.3.2.26) (Q09291)
Organism: Caenorhabditis elegans
Function: E3 ubiquitin-protein ligase (By similarity). Functions in the OLL neurons in the anterior ganglion to inhibit avoidance to microbial pathogens such as P.aeruginosa although worms do display avoidance behavior, vacating a P.aeruginosa lawn within 24 hours. Likely to act by inhibiting the neuropeptide receptor npr-1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q76N89}.
Interaction partners:
- DiSHevelled related
- Ubiquitin-ribosomal protein eL40 fusion protein
- F-box domain-containing protein
- 26S proteasome non-ATPase regulatory subunit 4
- Polyubiquitin-A
- Ubiquitin-like domain-containing protein
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MGDEFPFHHLGYVCLNEIYKHLTLKEIFQLSFSSNQIKRSLGIASIPVKSIFVNFDSQYPKIKLIGESSQLEWVFGIPDGLEYTDVGVYKIGHFKFQCKTSGTAFYTEHYDLENAMLVVIRYMISIFKCSNSIITYLSIDLGVIEDSRAICENFVAFKKVERLSIFQTNYGVERNTLNFAQSFDWICDNLEIKNIHIGADVLEPKMVQKTNGEFDIKLCARRFEQVLTMDHIYLQHADWITSEDLLNLDVQTAMLIENNLTEQDLNAFIKQWLRSDSDKLWWLEVKGKMMFNREEVLKDLDVQDDAYRSLNTRWYVARRSRANPSGNGCARKKMGSLRPKLTELWPFKVYIIFGSILIVFGPAALNRMITLRRMDVETDRPSGSETGIFVSKSAVYPFGNKNEVVKVWWNIDKPENCLDWIGLFDNNDSSFYLDQKSLRQHISPVVFTLTSKNLLNASEVYFGLIDGMTGRLLAKSENVEICKSASLVVHEVKKPENINVYLNTNHGRIEIPKKRSFSRKNGSFRSSFEFDFDVEDLHISLVENSEKLNFDHFIASNQLQNNYIQSKSFSHSHVVEIVFSIEPKTSKKSAPDIMEIASSSQTPPESHWKTYLDAKKRKFYVNHVTKETRWTKPDTLNNNHIEPETPVHKRLSDRSASPRNSFITPRRTITVRSAGCPKSDLIQFFQRDEFKTALYENQDAMQIYNECSVVRHAIHRIQKDLDPPSKFENQPLFVRFVNLFADITQPLPSGWECITMNNRTVFLNHANKETSFYDPRIRRFETKTSRRGRSVPSRSSTAHKGKIDHALISKCEDLRKIAQDNFPQIAERISKKLMLIERFGGLAVASLANDLDITLALSMLDSNTEKLAGEGDNIKMFYEDMKKEKLGKGPSRLCWKVSRDRLLDDAFRIILNVDPFVLKKSRLHIRFEGELALDYGGLSREFFILLSRELFHPKNGYFEYEGNDYHLQLRPRGCETEKEKKWLILCGRVLALAVIHRCYIDVFFTNVFYKSLQKRPVTLMDFKESDAEFYKSMNWLLENDVVDLEMSFVYSSMVNGKLAEQELVPGGESQMVTEANKAEFIDLMCQKKAIRGVEKPLEILLTSFNQILNDNLLNSLESSDLKRILSGSLELDLNDWRTNTIYKGGYSDCHIVVEWFWEVIETMTNQERFDLLLFVTGSSSVPFEGFSALRGNEEISKFCIEKWGDATSFPRAHTCFNRLQLPSYNTKQQLKSKLQQAIVNGMSYSIE
Protein: Heat stress transcription factor B-2a (AtHsfB2a) (AtHsf-22) (Heat shock factor protein 6) (HSF 6) (Heat shock transcription factor 6) (HSTF 6) (Q9SCW4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Multiprotein-bridging factor 1c
- Chaperone protein ClpB1
- Dehydration-responsive element-binding protein 2A
- Heat shock protein 90-1
- Calcium-dependent protein kinase 13
- DNA-binding protein S1FA3
- Heat shock protein 90-4
Sequence:
MNSPPVDAMITGESSSQRSIPTPFLTKTFNLVEDSSIDDVISWNEDGSSFIVWNPTDFAKDLLPKHFKHNNFSSFVRQLNTYGFKKVVPDRWEFSNDFFKRGEKRLLREIQRRKITTTHQTVVAPSSEQRNQTMVVSPSNSGEDNNNNQVMSSSPSSWYCHQTKTTGNGGLSVELLEENEKLRSQNIQLNRELTQMKSICDNIYSLMSNYVGSQPTDRSYSPGGSSSQPMEFLPAKRFSEMEIEEEEEASPRLFGVPIGLKRTRSEGVQVKTTAVVGENSDEETPWLRHYNRTNQRVCN
Protein: Inactive protein FRIGIDA (Q67Z93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein SUPPRESSOR OF FRI 4
- Protein FRIGIDA-ESSENTIAL 1
- Protein VERNALIZATION INSENSITIVE 3
- MADS-box protein SOC1
- WD-40 repeat-containing protein MSI4
- Polycomb group protein VERNALIZATION 2
- B3 domain-containing transcription factor VRN1
- MADS-box protein FLOWERING LOCUS C
- Protein LEAFY
- Serine/arginine-rich-splicing factor SR34
Sequence:
MSNYPPTVAAQPTTTANPLLQRHQSEQRRRELPKIVETESTSMDITIGQSKQPQFLKSIDELAAFSVAVETFKRQFDDLQKHIESIENAIDSKLESNGVVLAARNNNFHQPMLSPPRNNVSVETTVTVSQPSQEIVPETSNKPEGERICELMCSKGLRKYIYANISDQAKLMEEIPSALKLAKEPAKFVLDCIGKFYLQGRRAFTKESPMSSARQVSLLILESFLLMPDRGKGKVKIESWIKDEAETAAVAWRKRLMTEGGLAAAEKMDARGLLLLVACFGVPSNFRSTDLLDLIRMSGSNEIAGALKRSQFQV
Protein: Senescence/dehydration-associated protein At3g51250 (Q9SD22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- microtubule-severing ATPase
- Senescence/dehydration-associated protein At4g35985
- Protein EARLY-RESPONSIVE TO DEHYDRATION 7
- Spatacsin carboxy-terminus protein
- RING-H2 finger protein ATL72
- Binding partner of ACD11 1
- Lysophospholipid acyltransferase LPEAT1
- Zinc knuckle
- AP-5 complex subunit zeta-1
- 10 kDa chaperonin, mitochondrial
Sequence:
MNPSHGGDDKQRPAMYPQVDQSIPDNPFASTNPYVASSPYLYPSLSSHNLGPNLFPDHGDASNDQSPSAPPQATEEVLIRVPGAILNLIDKSYSVELACGDFTIVRIIQGQNIVAVLANVGNEIQWPLTKNEVAAKVDGSHYFFSIHPPKEKGQGSGSDSDDEQGQKSKSKSDDEILNYGLTIASKGQENVLLVLDQVLRDYSCFTEQRMSEKAKETGEEVLGNSVVADTSPEELKGERKDVVEGQCAAYWTTLAPNVEDYTHSTAKMIASGSGKLIRGILWCGDVTVERLKKGNEVMKNRLSRAEKEKDVSPETLRRIKRVKRVTQMTEKVATGVLSGVVKVSGFITGSMANSKAGKKLFGLLPGEIVLASLDGFSKICDAVEVAGKNVMSTSSTVTTELVNHRYGTKAAEATNEGLDAAGHAFGTAWVAFKIRKAFNPKNVIKPSSLAKSVSELKAKKGSK
Protein: GPI inositol-deacylase (EC 3.1.-.-) (Q9FN84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU365011}.
Interaction partners:
Sequence:
MASAMVTSLRLRPNFSAATSPSSSSSAGNVKYRPAVILPGLGNNTGDYKKLEVTLGEYGVPAVVAAVSRLDWFRNAAGLVDPAYWRGTLRPRPVLDWYLNRIDDAVREANELAQGQGLCLIGHSAGGWLARVYMEEYGNSDISLLLTLGTPHLPPPRGLPGVIDQTRGLLYYVEENCAKAVYTPELKYVCIAGRYIRGARLVDNADADIDSDVTVGIDSGEGISELAIASNKKSGTFRARFVGQGYKQVCGRADVWGDGVVPEVSAHLEGALNVSFDGVYHSPVGSDDETRPWYGSPVIVKDWIHHLLE
Protein: Long-chain-fatty-acid--CoA ligase 2 (EC 6.2.1.3) (Fatty acid activator 2) (Long-chain acyl-CoA synthetase 2) (Q9P7D7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Esterification, concomitant with transport, of endogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Plays an important role in the determination of viability in the stationary phase.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1
- Long-chain-fatty-acid--CoA ligase 1
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Fatty acid synthase subunit alpha
- Triacylglycerol lipase ptl1
- Putative monoglyceride lipase
- Triacylglycerol lipase ptl3
- Putative lipase atg15
- Secretory component protein psh3
- Probable acyl-CoA desaturase
Sequence:
MDIKDYYCVETKDSKQPGESYIYRSIHSAGKLLDTPEDGVSTVYDLLCTAAKNHGEKQAMGSRKLIKENREEREIIRKVDNEEVVEKKLWTTYELGPYEYISFNKVYEIALALGSGLVASGITSETTMLFFAATSAKWFTTAQGCSSQAIPIVTAYETLGEDGIYTSLDECKSRAIFTDPNLIPKLLGPLKQSTWVKLIVCSSTPSEDLVELVKSTAPDVEIITYDNLLSLGKEKPQPPHPPKADDICCYMYTSGSTGKPKGVVLLHRNIIAALGGINRILSQHINVKDYVLAYLPLAHIFEFIFEMCCLYWGGVLGYASPRTLTDASVVNCKGDLTEFRPTVLIGVPAVYELIKKGILAKVSSMPAHRQKVFSGSLSLKQYLIERNLPGSAALDAIVFNKVKAATGGRLRYCISGGAALAASTQAFLSSCICPVLPGYGLTETCAGSFVLSPEQWHLYANTVGFPIPSIEFKLVDIPDLGYYTDSSPPRGEVWIRGPAVCNGYLNRPEDNKAAFTEDGWFKTGDVGEIAKGNTLRLIDRKKNIVKSLNGEYIALEKIEAQFFTSPLVSNVCAYADVNHAKPVVIVNPDENGLRTYLTKNSGSSFNGNPNDTLTNLCKDSGVQHLILKELINIGKQQRLASIEIPEGVVLSDFEWTAENNFLTASRKVKRQVIVAHYSDEIQKAYSKKH
Protein: Cell cycle protein kinase DBF2 (EC 2.7.11.1) (Dumbbell forming protein 2) (P22204)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ser/Thr-protein kinase involved in the mitotic exit network (MEN) and required after the metaphase to anaphase cell cycle transition. Phosphorylates CHS2 to regulate its dynamics and chitin synthesis at the division site during cytokinesis. Coordinates septin and actomyosin ring (AMR) functions during cytokinesis through the phosphorylation of HOF1. In complex with MOB1, phosphorylates CDC14 at sites adjacent to its nuclear localization sequence, thereby retaining CDC14 in the cytoplasm. Binds also to SWI5 and CLB2 mRNAs cotranscriptionally to regulate their decay. In the nucleus, the DBF2-MOB1 complex regulates passenger protein localization during anaphase. Mediates sorbic acid stress tolerance through promoting vacuolar H(+)-ATPase function, probably through phosphorylation of VMA1 and VMA2 subunits.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Bud neck. Nucleus. Note=Localizes on spindle ole body (SPB) for much of the cell cycle and migrates from there to the bud neck in late mitosis. SPB localization during anaphase coincides with activation kinase activity and depends on TEM1 and CDC15. In absence of BUB2, localizes to SPB in cell cycle stages other than anaphase and telophase.
Interaction partners:
- Cell division control protein 15
- Protein TEM1
- Nucleolar protein NET1
- DBF2 kinase activator protein MOB1
- Sporulation-specific protein 12
- Tyrosine-protein phosphatase CDC14
- Protein SIC1
- G2/mitotic-specific cyclin-2
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Protein phosphatase PP2A regulatory subunit B
Sequence:
MLSKSEKNVDLLAGNMSNLSFDGHGTPGGTGLFPNQNITKRRTRPAGINDSPSPVKPSFFPYEDTSNMDIDEVSQPDMDVSNSPKKLPPKFYERATSNKTQRVVSVCKMYFLEHYCDMFDYVISRRQRTKQVLEYLQQQSQLPNSDQIKLNEEWSSYLQREHQVLRKRRLKPKNRDFEMITQVGQGGYGQVYLARKKDTKEVCALKILNKKLLFKLNETKHVLTERDILTTTRSEWLVKLLYAFQDLQSLYLAMEFVPGGDFRTLLINTRCLKSGHARFYISEMFCAVNALHDLGYTHRDLKPENFLIDAKGHIKLTDFGLAAGTISNERIESMKIRLEKIKDLEFPAFTEKSIEDRRKMYNQLREKEINYANSMVGSPDYMALEVLEGKKYDFTVDYWSLGCMLFESLVGYTPFSGSSTNETYDNLRRWKQTLRRPRQSDGRAAFSDRTWDLITRLIADPINRLRSFEHVKRMSYFADINFSTLRSMIPPFTPQLDSETDAGYFDDFTSEADMAKYADVFKRQDKLTAMVDDSAVSSKLVGFTFRHRNGKQGSSGILFNGLEHSDPFSTFY
Protein: GPI inositol-deacylase (EC 3.1.-.-) (Q582X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- GPI-anchor transamidase subunit 8
- GPI transamidase component GAA1
- COP-coated vesicle membrane protein erv25, putative
- Cytosolic coat protein, putative
Sequence:
MPSQEDEELSGIGAPSSGVNPAATSLPQRKKNLVVLFTLFSLAAALLYALSVVRLGLQIRDYANNNRFRVFPDSVAWHPLSYRRLFLQNPKWGDERSNRGSSPPYSFFEVSCPDCYSTYAPTQEKPPEVIIFFAHGNAGSYMQAHRLGILFLQEQKIKGRLYTFDFSEQANAHRGALLHHQADFVADTIITLYEDRKNETHNPPFIWLIGHSMGGVVVRMALSTLSDSQVFPLIAGVITLNSPNRQMPVFLDLPMWRLYKTLWDPVQKNVLANDRNGYRNPRILSLTSGPLDLMVQSKHTRLSDSIGCNNGSCIDVTTEHPKVCGKTFSHDDIMRDYCVVEFWTSAVIRNSLVRGDGISPESRNLKLRNWSLPEGINDPAPPPHSFSDAFSWWAEASYTHVGLTVLVAFSYGSFVLSAIHPLLLRLLLNLRVLSHCCADWSWKSLFTSSHTAVVMVTPIMGIVGHLLLVQIPCCLLPAMEGCKSPWIADTLVCKPTFDPLMLVWCAFAASGPALKGIWMGIIAYRLLQLLLRGSKFGWTKFWLVTHRACIYLRLPRWVRRSPTRSDDNCDEPWNRIIPVTVFGVVVFLCGVLLPLRICDRALVWLCLTIVLLPLSASYQTATFDSSDGRREEAYMLVSAYALLHLIHLHPFFAWRNALRSATFDDATVVDFTSRAVEVLLLVLILSYVMWPLYHEQRFCEQLHRDKLSSLAKALASPWIQRLSPHLCILLVLIPLVWMISVPVASFRIVWVLLYAFPCFLLGPALVSGGSGGTLLAPGTSN
Protein: Unique cartilage matrix-associated protein (Upper zone of growth plate and cartilage matrix associated protein) [Cleaved into: Unique cartilage matrix-associated protein C-terminal fragment (Ucma-C) (Gla-rich protein) (GRP)] (Q14BU0)
Organism: Mus musculus (Mouse)
Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18156182, ECO:0000269|PubMed:19819238}.; SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Golgi apparatus.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted. Golgi apparatus.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton {ECO:0000305}. Note=Colocalizes with aggresomes, which are aggregates of misfolded proteins, at the centrosome.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytoskeleton {ECO:0000305}. Note=Colocalizes with aggresomes, which are aggregates of misfolded proteins, at the centrosome.
Interaction partners:
- Matrix Gla protein
- Vitamin K-dependent gamma-carboxylase
Sequence:
MSWRRVILLSSLLALVLLCMLQEGTSASVGSRQAAAEGVQEGVKQKIFMQESDASNFLKRRGKRSPKSRDEVNAENRQRLRDDELRREYYEEQRNEFENFVEEQRDEQEERTREAVEQWRQWHYDGLYPSYLYNRQNI
Protein: Frizzled-6 (Q6P0Y7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004439}.
Interaction partners:
Sequence:
MALLLCLCVLLLLDSCVSHTLFTCEPVQVQWCLDMPYNTTFFPNMLEHYDQDIAAVRMKEFMPLVSVRCSPDAHLFLCQAFVPECRTHSHSQTHTHVLRPCRERCERVRSDCRAVMHTFDISWPSELQCERLESCGGSAVDVTTAGRSGAGSSPRDLGFWCPLQLKLRPGQSGSFLGAPDCAPPCENMFLTAAEQHLARLFIGVCSVVCLCATLFTFLTFLMDAQRFRYPERPIVFISVCYCAVSLLYLLGFMLGPSVACGAPGRPGGVWTVVLGARSRGCSLLFTLLYFCSTAGMLWWVILTITWFLAAGPKWSCEAIQKQALWFHAAGWGVPAVLTLLLLALGKVEGDGISGVCFTGLYDLTALRWFLVAPLALAVLLGLALLLAGIVALNRVRQVIQHDQLNQQKLKRFMIRIGVFSGLYLLPLLLLLGCYLYEMTQRRVWESSWVNRHCQEFSIPCARTSSGGVQHPGLSLFLLKYLMTLAVGIPAVFWVSSRKTCSRWASFCRRAHKKDAVSESRRVLQESCEFFLKHNSRPQQSRSSLRLKVLSKSMGTSTGTPASCAPPPAASLDHTAASSDTDRHSRADASSRISSRSTSKGDKPKAPPTSPTANEMSG
Protein: DNA repair protein RAD50 (hRAD50) (EC 3.6.-.-) (Q92878)
Organism: Homo sapiens (Human)
Function: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:26215093}. Chromosome, telomere {ECO:0000269|PubMed:10888888}. Chromosome {ECO:0000269|PubMed:21757780, ECO:0000269|PubMed:26215093}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents (PubMed:10783165, PubMed:26215093). Localizes to DNA double-strand breaks (DSBs) (PubMed:15916964, PubMed:21757780). {ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:21757780, ECO:0000269|PubMed:26215093}.
Interaction partners:
- Breast cancer type 1 susceptibility protein
- Double-strand break repair protein MRE11
- Nibrin
- DNA endonuclease RBBP8
- BRCA1-associated RING domain protein 1
- Serine-protein kinase ATM
- Mediator of DNA damage checkpoint protein 1
- Histone H2AX
- Telomeric repeat-binding factor 2
- RecQ-like DNA helicase BLM
Sequence:
MSRIEKMSILGVRSFGIEDKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRLQFRDVNGELIAVQRSMVCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRIKKNIDQCSEIVKCSVSSLGFNVH