wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phosphatase 1 regulatory subunit 12A (MBSP) (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit) (Protein phosphatase subunit 1M) (PP-1M) (Serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110) (Q10728)
Organism: Rattus norvegicus (Rat)
Function: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14974}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}. Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit 14A
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Rho-associated protein kinase 1
- Transforming protein RhoA
- Myosin regulatory light chain 12B
- Rho-associated protein kinase 2
- Protein phosphatase 1 regulatory subunit
- Serine/threonine-protein phosphatase 1 regulatory subunit 10
Sequence:
MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMENNQPQKTFKNKETLIIEPEKNASRIESLEQEKADEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPMASVTNAHTASTQAAPAAVTTPTLSSNQGTPTSPVKKFPTSTTKISPKEEERKDESPASWRLGLRKTGSYGALAEITASKEAQKEKDTAGVIRSASSPRLSSSLDNKEKEKDNKGTRLAYVAPTIPRRLGSTSDIEEKENRESSNLRTSSSYTRRKWEDDLKKNSSINEGSTYHRSCSFGRRQDDLISCSVPSTTSTPTVTSAAGLQKSFLSSTSTTAKTPPGSSPAGTQSSTSNRLWAEDSTEKEKDSAPTAATILVAPTVVSAAASSTTALTTTTAGTLSSTSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKDKEEKEKQDKEKQEEKKESEVSREDEYKQKYSRTYDETYARYRPVSTSSSSTPSSSSLSTLGSSLYASSQLNRPNSLVGITSAYSRGLTKDNEREGEKKEEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQERQSDTEDGSSKRDTQTDSVSRYDSSSTSSSDRYDSLLGRSASYSYLEERKPYGSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSLLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK
Protein: Sex peptide receptor (Q29I83)
Organism: Drosophila pseudoobscura pseudoobscura (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MGGDQGVLIELQEMSTAVTKTVAAAAAAMLGSSMDNNSAYSYDISATDVLYQWSANAAAAAAGGARIAHTMPPSVATLPPATNHGSMHQSVPLPGIGQRLAPNETQFGLLDYGMSSMNDSLDYASYQQQMGEDGQCRQMDANVSYWNLTCDSPLDYALPLYGYCMPFLLIITIISNTLIVLVLSKKSMATPTNFVLMGMAICDMLTVIFPAPGLWYMYTFGNHYKPLHPVSMCLAYSIFNEIMPAMCHTISVWLTLALAVQRYIYVCHAPMARTWCTMPRVKRCTVYIALLAFLHQLPRFFDRTFLPLQIEWNGNETEVCHLETSMWVHEYIGMDLYYTSYYLFRVLFVHLLPCIILVTLNILLFAAMRQAQERRKLLFRENRKKECKKLRESNCTTLMLIVVVTVFLIAEIPIAVVTAMHIVSSLIIEFLDYGIANIFIMLTNFFLVVSYPINFGIYCGMSRQFRETFKEIFLGRIIAKKDSSSKYSIVNGPRTCTNTNETVL
Protein: Always early (Q2PNN2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRHQLKKPRKMVAAWQNDELFIKRPNFAPRIRISEKPEIQGRVKPGVASKRIENFTKKPSKISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREELECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGKSFEGIVNGTVMGYDPQDYTYLVRFNRNDHAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLRILHDYLVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADEKFLKIESDRTQEFVRNLHTILYLNGKLGRENSSNLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: Transport protein particle subunit trs85-2 (TRAPP subunit trs85-2) (O74748)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the TRAPP I and TRAPP II complexes. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II seems to play a role in intra-Golgi transport. Has a role late in meiosis following DNA replication (By similarity).
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}.
Interaction partners:
- Transport protein particle subunit trs31
- Uncharacterized protein C13G6.05c
- Transport protein particle 20 kDa subunit
- Transport protein particle subunit bet3
- Transport protein particle subunit bet5
- Uncharacterized protein CC285.14
- Transport protein particle subunit trs23
- Uncharacterized protein C15A10.12c
- Transport protein particle subunit trs120
- GTP-binding protein ypt1
Sequence:
MESNLSAKGIFQHASANASGELFQEPVTEDLEKVMQSKGLYSMEELCSIIQEAYAPRVSVLCSRDADEFAMRKGYPKGFWELLYPFGDRIRGKVNRRGMNGEMLTLENLNLHFVPIDALESHLSEASFPSLRSVLCERYPGLVSPEPPSDYSFGVHYKNVERWAWTLAHEGNYQMPLPVYVRQLLTGIPITPFETFSHPVAHLVVVTSHNPSPFESLRSLINSIPYLSLPAFVFNDINYLFVYVHDEDQHDLELSMAIFDTMKQTFGDCGYFLRLHSQKATLDYEHTVPFPTSSWLSAEERLHLLSNTDTEIRLLFESDNESLRRLSSHIAFNGIVSYLDKCVRAWDDQYASPRRGITGKLLFASRKYLSSSNASTNSNYFPSSNAYRPFSPEAYLRKLADYSFMLRDYSHANQIYEIASRQYENDGACLYSAASLEMIVITEHILHLKMPYMSLTNTLRINEYMQSAMLNYLNKSFNSYYHAARCFLLLGQFLSCLPAPKVDDAANWNAGLLYSKRLGPVGRAMIFQQTHTLFKSLSYLKTESTDPFSNKRTRKAALWCVLTADAWLRCRIPFRAKPFVEEAKLFYGKIDWKDLKECVAALDEVEVSKQPASNIPSS
Protein: Histone H2A (C6KT18)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU003767}.
Interaction partners:
- Histone H4
- Histone H2B
- Histone H2B
- Ubiquitin-60S ribosomal protein L40
- FACT complex subunit
- Nucleosome assembly protein
- Histone H3
- Histone H3
- Histone H2A
- Histone H3-like centromeric protein CSE4
Sequence:
MSAKGKTGRKKASKGTSNSAKAGLQFPVGRIGRYLKKGKYAKRVGAGAPVYLAAVLEYLCAEILELAGNAARDNKKSRITPRHIQLAVRNDEELNKFLAGVTFASGGVLPNIHNVLLPKKSQLKAGTANQDY
Protein: tRNA wybutosine-synthesizing protein 3 (tRNA-yW-synthesizing protein 3) (EC 2.1.1.282) (tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase) (P53177)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72.
Interaction partners:
- tRNA wybutosine-synthesizing protein 2
- tRNA wybutosine-synthesizing protein 4
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
- tRNA
- Large ribosomal subunit protein mL49
- tRNA
- tRNA A64-2'-O-ribosylphosphate transferase
- Multisubstrate pseudouridine synthase 7
Sequence:
MAAQNAFEQKKRAILNEIDSTQPDLSPKGTIDELCLPIIDLINASADMVTTSSCSGRVSVFLEGTKSYNGEVKIGGKGQGGKWLYVTHDREKVIGWLDELKSKSEFSFELSGKEIPTEKVTGSIRYILYKYEPFILHVKCRDFQAASKLYNTAMSCGFRESGIGSNNLVAIRINIKLDVPLGYLDETSGTLKFFVTPEYVSVLDSLSLSKFDENTRKMQALYDRIEKELINCAPDVNSKVNITPIETKEERRERKKREGMERQRQLKSPQNVL
Protein: Probable spore germination protein GerPF (P62186)
Organism: Bacillus anthracis
Function: Required for the formation of functionally normal spores. Could be involved in the establishment of normal spore coat structure and/or permeability, which allows the access of germinants to their receptor.
Interaction partners:
- Spore gernimation protein GerPC
- Spore gernimation protein GerPB
- Spore germination protein GerPE
- Spore gernimation protein GerPD
- Probable spore germination protein GerPA
- Cell division protein FtsN
- Stage VI sporulation protein D
Sequence:
MPSVVGNLVVQNSNGSFNLGDFYNVSPKENTKAYNGSGASNVGFVVNTFNGVSATNTFDSDVADQDQIGTA
Protein: F-actin-capping protein subunit alpha (P28495)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q10434}. Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:38088874}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:38088874}. Note=Localizes to the actomyosin contractile ring. {ECO:0000269|PubMed:38088874}.
Interaction partners:
- F-actin-capping protein subunit beta
- Transcription factor BYE1
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Nuclear migration protein JNM1
- Altered inheritance of mitochondria protein 21
- Actin-interacting protein 1
- Topoisomerase I damage affected protein 2
- Endoplasmic reticulum membrane protein complex subunit 10
- Twinfilin-1
- Actin-like protein ARP10
Sequence:
MSSSKFEEVINKIINDSPPGELREVYDDLIKITSENSKNTILDAIENYNVQNCIPIEVNGNSVIISKYNKEGAKFFDPVNSVIFSVNHLERKGLDIEPYEFTHAKIEKGQLKELHDKLHEYLLQSFPGDVSFAVYPVPEEISKISIIIVSTKYNPNNFWNGHWRSSYIYDLETRELSGQISTQVHYYEDGNVSFQSGKDINQSNVDDVVCTIRDIETNFENDLDLSFFDLNEKQFKALRRRLPVTRSKINWGSAIGSYRLGKNAAEGK
Protein: Zinc finger protein 627 (Q7L945)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDSVAFEDVAVNFTLEEWALLDPSQKNLYRDVMRETFRNLASVGKQWEDQNIEDPFKIPRRNISHIPERLCESKEGGQGEETFSQIPDGILNKKTPGVKPCESSVCGEVGMGPSSLNRHIRDHTGREPNEYQEYGKKSYTRNQCGRALSYHRSFPVRERTHPGGKPYDCKECGETFISLVSIRRHMLTHRGGVPYKCKVCGKAFDYPSLFRIHERSHTGEKPYECKQCGKAFSCSSYIRIHERTHTGDKPYECKQCGKAFSCSKYIRIHERTHTGEKPYECKQCGKAFRCASSVRSHERTHTGEKLFECKECGKALTCLASVRRHMIKHTGNGPYKCKVCGKAFDFPSSFRIHERTHTGEKPYDCKQCGKAFSCSSSFRKHERIHTGEKPYKCTKCGKAFSRSSYFRIHERTHTGEKPYECKQCGKAFSRSTYFRVHEKIHTGEKPYENPNPNASVVPVLS
Protein: C2H2-type domain-containing protein (Q27GU0)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPVQLSNFVSKTPLIGSEWPPTGDWRSANNNSLGDWNKCCVPGSEIPQHLGPFGNSSLTMLTAQQPGEKIHPDGGYVSPKEDGRKSSEHTNSYDVSASQSPSNDGAQSDSTSDEHIDVECMTETEMDTDEKDSTIKPEDQATPKLEEGSDSKPESTSVEGTSSNYQVTSEPVQMPQMPIPVIPSFLKNSLPAPIPITPTQSANVERSNSPSIEEALLLTLSQQQFAEVFAEAAKIRKSSSESIGFQRSGTSAFLNIEPKEMSMSSANNNNEEAPASTVSACSTPTTTTSASFCRPPGLGPVALPPTQNGQTPMLVCPICGFMCPSKFHFNSHMNTHGDHQCSMCDYTSRTEGRLKKHMRESHTVEEQLRAGFESEPAKESASSPKNLSLSKDGSATSPINEIFNLSTTMASILDSTNNAVSSTSTTEQPSALSALTLDMSSTPSLLSTLAHSSFGVSALDQIKAISENPSFMPEGGINLASALGVVSNAIKGDTPSPEKQSNGECRRSSSGKIKIFKCKQCGHQSLSKDDQWAHARTHIPAEKQLNCQHCNFVTEYKHHLEYHYRNHIGSKPFQCKKCAYNCVNKSMLNSHMKSHTNHYQFRCMDCTYATKYCHSLKLHLKKYNHRRVPEGIEMSGGDSSPPFTSDATITFSPLMKQEIKTETVEPVTSIAQPFPFNPMMGNHGLNFANHMLLNKHLDVGLMGLRNSVMSPLKCSACDFVASSADEKMRHSMSHILNSSNVPTSIASLYNSLNLPSFSHVAPDNDNALESMDCDVKIDDDNITESHCYEEMDQGSDSAVSPTGSSQISSGDEETKKCKSLSLEQISARANGNNSPMSNDSAMEKDGESADDAPHSPSDTTSVPSPPLHSSSIVAPIPITPQPNEFLQSILAQASLLGPLLANRPSAFYCDHCKIPFDTQQVLDSHMRFHTPGNPFMCSDCQYQAFNELSFALHMYQARHQ
Protein: Vacuolar protein sorting-associated protein 72 homolog (Protein YL-1) (Transcription factor-like 1) (Q62481)
Organism: Mus musculus (Mouse)
Function: Deposition-and-exchange histone chaperone specific for H2AZ1, specifically chaperones H2AZ1 and deposits it into nucleosomes. As component of the SRCAP complex, mediates the ATP-dependent exchange of histone H2AZ1/H2B dimers for nucleosomal H2A/H2B, leading to transcriptional regulation of selected genes by chromatin remodeling.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15906}.
Interaction partners:
- RuvB-like 1
- YEATS domain-containing protein 4
- RuvB-like 2
- DNA methyltransferase 1-associated protein 1
- Transformation/transcription domain-associated protein
- E1A-binding protein p400
- Mortality factor 4-like protein 1
- Histone acetyltransferase KAT5
- MRG/MORF4L-binding protein
- Bromodomain-containing protein 8
Sequence:
MSLAGGRAPRKTAGNRLSGLLEAEEEDEFYQTTYGGFTEESGDDEYQGDQSDTEDEVDSDFDIDEGDEPSSDGEAEEPRRKRRVVTKAYKEPLKSLRPRKVSTPASSSQKAREEKTLLPLELQDDGSDSRKSMRQSTAEHTRQTFLRVQERQGQSRRRKGPHCERPLTQEELLREAKITEELNLRSLETYERLEADKKKQVHKKRKCPGPIITYHSVTVPLVGEPGPKEENVDVEGLDPAPTASALAPHAGTGTGAAAATPPAHCSRTFITFSDDATFEEWFPQGRPPKVPVREVCPVTHRPALYRDPVTDIPYATARAFKIIREAYKKYITAHGLPPTASALGPGPPPPEPLPGSGPRALRQKIVIK
Protein: Translation initiation factor IF-3 (P65144)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00080}.
Interaction partners:
Sequence:
MFFSNKTKEVKTIAKQDLFINDEIRVREVRLIGLEGEQLGIKPLSEAQALADNANVDLVLIQPQAKPPVAKIMDYGKFKFEYQKKQKEQRKKQSVVTVKEVRLSPTIDKGDFDTKLRNARKFLEKGNKVKVSIRFKGRMITHKEIGAKVLAEFAEATQDIAIIEQRAKMDGRQMFMQLAPATDKK
Protein: GH03227p (Versager) (Q9VG65)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH07855p
- Uncharacterized protein, isoform E
- Cytosol aminopeptidase
- GH20441p
- GH06435p
- AT18965p
- GH14656p
- GEO12122p1
- Cytosol aminopeptidase
- FI13205p
Sequence:
MDEFRVPKKVNRNVFKAISILQSSRTDFVCANAIVDQVKFQMRNRIPVEHIDEAIKQSLANLTMLGIVRRLGSSKYSLSTIVYGRLGMPNPIAHPPGNPGRPHRRAAQNARQKRPVGRLDPWKSVSKILSEDSLSGTEMTKMRKRMRTNTKRVVKKKRIPNRRLSRARKYKETEMATTSIDLRCSESRLGLDNNVQILFGSPGWTYTKPIQSTLVLPDAPLRLDQKANDPETPKTTVLSGNSSSTSVTDVKGNVVKDEEGGSQPSISGTNCRAVPIGLGIRPAYHTSGGESDVENASVVGLCGSPLCLQSTMSQSLAHDSAPTTSRPTAKQSNNLGIQQITECQENDRVVESSEVQETFENNLDKQASQPSDVLEECQSALNYDFYK
Protein: Lipid transferase CIDEC (Cell death activator CIDE-3) (Cell death-inducing DFFA-like effector protein C) (Fat-specific protein FSP27 homolog) (Q96AQ7)
Organism: Homo sapiens (Human)
Function: Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:23399566}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P56198}. Nucleus {ECO:0000250|UniProtKB:P56198}. Note=Diffuses quickly on lipid droplet surface, but becomes trapped and clustered at lipid droplet contact sites, thereby enabling its rapid enrichment at lipid droplet contact sites. {ECO:0000250|UniProtKB:P56198}.
Interaction partners:
- Perilipin-1
- Lipid transferase CIDEA
- DNA fragmentation factor subunit alpha
- Peroxisome proliferator-activated receptor gamma
- Hormone-sensitive lipase
- Perilipin-4
- Leptin
- Platelet glycoprotein 4
- Adiponectin
- Cyclic AMP-responsive element-binding protein 3-like protein 3
Sequence:
MEYAMKSLSLLYPKSLSRHVSVRTSVVTQQLLSEPSPKAPRARPCRVSTADRSVRKGIMAYSLEDLLLKVRDTLMLADKPFFLVLEEDGTTVETEEYFQALAGDTVFMVLQKGQKWQPPSEQGTRHPLSLSHKPAKKIDVARVTFDLYKLNPQDFIGCLNVKATFYDTYSLSYDLHCCGAKRIMKEAFRWALFSMQATGHVLLGTSCYLQQLLDATEEGQPPKGKASSLIPTCLKILQ
Protein: Immediate early response gene 5 protein (Q5VY09)
Organism: Homo sapiens (Human)
Function: Plays a role as a transcription factor. Mediates positive transcriptional regulation of several chaperone genes during the heat shock response in a HSF1-dependent manner. Mediates negative transcriptional regulation of CDC25B expression. Plays a role in the dephosphorylation of the heat shock factor HSF1 and ribosomal protein S6 kinase (S6K) by the protein phosphatase PP2A. Involved in the regulation of cell proliferation and resistance to thermal stress. Involved in the cell cycle checkpoint and survival in response to ionizing radiation. Associates with chromatin to the CDC25B promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:25816751}. Cytoplasm {ECO:0000269|PubMed:25816751}. Note=Predominantly cytoplasmic (PubMed:25816751). Translocated in the nucleus during heat shock (PubMed:25816751). {ECO:0000269|PubMed:25816751}.
Interaction partners:
- Multiple PDZ domain protein
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
Sequence:
MEFKLEAHRIVSISLGKIYNSRVQRGGIKLHKNLLVSLVLRSARQVYLSDPCPGLYLAGPAGTPAPPPQQQPGEPAAGPPAGWGEPPPPAARASWPETEPQPERSSVSDAPRVGDEVPVATVTGVGDVFQGGEADATEAAWSRVEGPRQAAAREAEGTAGGWGVFPEVSRAARRPCGCPLGGEDPPGTPAATPRAACCCAPQPAEDEPPAPPAVCPRKRCAAGVGGGPAGCPAPGSTPLKKPRRNLEQPPSGGEDDDAEEMETGNVANLISIFGSSFSGLLRKSPGGGREEEEGEESGPEAAEPGQICCDKPVLRDMNPWSTAIVAF
Protein: glycine--tRNA ligase (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Q54PF9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- tyrosine--tRNA ligase
- Probable isoleucine--tRNA ligase, cytoplasmic
- Probable methionine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Probable tyrosine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Probable glutamine--tRNA ligase
- Probable glutamate--tRNA ligase, cytoplasmic
- Probable isoleucine--tRNA ligase, mitochondrial
- Probable arginine--tRNA ligase, cytoplasmic
Sequence:
MILLKSLINKSSLSSPSFKSINKSLTFKNINNYYTTTTTTTSLNLKSNILFNNSDNKMSIDNKEKIRAGLEDLMKRRFFITQSFSIYGGQAGLYDYGPPGCAVKANLINLWRQHFVLNEDMSEVDCVSVTPEQVLKASGHVAKFADFMVKDEVTKAFFRADHILEAHIQTLLKDTSKMSKEQIEELNFVLAKAGDYNQEQLKESLIKYNVKAPETGNALTEPYPFNLMFQTQIGPSGLSTGYLRPETAQGIFTNFGKLYEYNGKKLPFAAAQIGNAFRNEIAPRAGLLRVREFTMAEIEHFVNPNNKTHPKFNEIKDVEANLLSSDSQDKTSEIQVCTFGEAVEKKLIDNETLAYFMARTQQFLHTVGIKPAGLRFRQHQKNEMAHYAQDCWDAEILSSYGWVECVGHADRSCYDLKVHATESKSNLSAYEEFKEPQFVDIAKVVVNPGAISKKHRAAVSPIKKYLTELKDDLAKALEIQETITKDGSYNLVLDGNTYDITADMVTISKAQEKKNGHTFFPHVIEPSFGLGRIIYSILEQNYYTRENDEQRGVLSLPAIIAPVKASILPLTSSDRIAPFVQTISKALKEANISTKVDDTGNAIGRKYARTDEIGVPFGVTIDFQTVEDNTVTLRERDTTKQVRIPISELASTLRKLCDLTVSWSDILKTFPIYEGQSE
Protein: Centriole, cilia and spindle-associated protein (Q6IQ19)
Organism: Homo sapiens (Human)
Function: Plays a role in microtubule (MT) stabilization and this stabilization involves the maintenance of NUMA1 at the spindle poles. Colocalizes with polyglutamylated MTs to promote MT stabilization and regulate bipolar spindle formation in mitosis. Binding of CCSAP to centrosomes and the spindle around centrosomes during mitosis inhibits MT depolymerization, thereby stabilizing the mitotic spindle. May play a role in embryonic development. May be required for proper cilia beating (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:22493317}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22493317, ECO:0000269|PubMed:26562023}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22493317}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22493317}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:22493317}. Cell projection, axon {ECO:0000269|PubMed:22493317}. Cell projection, cilium {ECO:0000269|PubMed:22493317}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:26562023}. Note=Localizes to two to four centrioles throughout the cell cycle. Localizes to mitotic spindle microtubules during prometaphase and throughout the remainder of mitosis. Localizes to cytoskeleton on interphase. Localizes at the ciliary transition zone which connects the basal bodies to ciliary microtubules. Colocalizes with polyglutamylated tubulin. {ECO:0000269|PubMed:22493317, ECO:0000269|PubMed:26562023}.
Interaction partners:
Sequence:
MSPGSGVKSEYMKRYQEPRWEEYGPCYRELLHYRLGRRLLEQAHAPWLWDDWGPAGSSEDSASSESSGAGGPAPRCAPPSPPPPVEPATQEEAERRARGAPEEQDAEAGDAEAEDAEDAALPALPVKDVEDKPEQQTRTRETDKSPTSTEPRQQPSALFARGNRKAVKSPQRSSSKIKENKHPFALYGWGEKQTDTGSQKTHNVCASAPVHEIHESALRAKNRRQVEKRKLVAQRQRAHSVDVEKNRKMKASSSENPWMTEYMRCYSARA
Protein: Cytosolic carboxypeptidase 1 (EC 3.4.17.24) (ATP/GTP-binding protein 1) (Protein deglutamylase CCP1) (J3KNS1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRTGSAASSAAAAAAAAAASASPATGVCMKTPGGGRRGIRRDPGAEPGAAALRGPRQRPILSRLTNNSRIVGLLAQLEKINAEPSESDTARYVTSKILHLAQSQEKTRREMTAKGSTGMEILLSTLENTKDLQTTLNILSILVELVSAGGGRRVSFLVTKGGSQILLQLLMNASKESPPHEDLMVQIHSILAKIGPKDKKFGVKARINGALNITLNLVKQNLQNHRLVLPCLQLLRVYSANSVNSVSLGKNGVVELMFKIIGPFSKKNSSLIKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSSFHFQLPVIPVTGPVAQLYSLPPEVDDVVDESDDNDDIDVEAENETENEDDLDQNFKNDDIETDINKLKPQQEPGRTIEDLKMYEHLFPELVDDFQDYDLISKEPKPFVFEGKVRGPIVVPTAGEETSGNSGNLRKVVMKENISSKGDEGEKKSTFMDLAKEDIKDNDRTLQQQPGDQNRTISSVHGLNNDIVKALDRITLQNIPSQTAPGFTAEMKKDCSLPLTVLTCAKACPHMATCGNVLFEGRTVQLGKLCCTGVETEDDEDTESNSSVEQASVEVPDGPTLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKIAQDIERLIHQSDIIDRVVYDLDNPNYTIPEEGDILKFNSKFESGNLRKVIQIRKNEYDLILNSDINSNHYHQWFYFEVSGMRPGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALNARPWWIRMGTDICYYKNHFSRSSVAAGGQKGKSYYTITFTVNFPHKDDVCYFAYHYPYTYSTLQMHLQKLESAHNPQQIYFRKDVLCETLSGNSCPLVTITAMPESNYYEHICHFRNRPYVFLSARVHPGETNASWVMKGTLEYLMSNNPTAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPSPDLHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMYGCSIKETVWHTNDNATSCDVVEDTGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGKYKGLQIGTRELEEMGAKFCVGLLRLKRLTSPLEYNLPSSLLDFENDLIESSCKVTSPTTYVLDEDEPRFLEEVDYSAESNDELDIELAENVGDYEPSAQEEVLSDSELSRTYLP
Protein: Aconitate hydratase A (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (Iron-responsive protein-like) (IRP-like) (RNA-binding protein) (Q8ZP52)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The (2S,3S)-2-methylcitrate (2-MC) is a very poor substrate. The apo form of AcnA functions as a RNA-binding regulatory protein (By similarity).
Interaction partners:
- Isocitrate dehydrogenase
- Citrate synthase
- Aconitate hydratase B
- Isocitrate lyase
- Fumarate hydratase class I, aerobic
- 2-methylcitrate synthase
- Fumarate hydratase class II
- Superoxide dismutase
- Succinate dehydrogenase cytochrome b556 subunit
- Superoxide dismutase
Sequence:
MSSTLREASKDTLQAKDKTYHYYSLPLAAKSLGDIARLPKSLKVLLENLLRWQDGESVTDEDIQALAGWLKNAHADREIAWRPARVLMQDFTGVPAVVDLAAMREAVKRLGGDTSKVNPLSPVDLVIDHSVTVDHFGDDDAFEENVRLEMERNHERYMFLKWGKQAFSRFSVVPPGTGICHQVNLEYLGKAVWSELQDGEWIAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAITLEYMRLSGRSDDLVELVETYAKAQGMWRNPGDEPVFTSTLELDMGDVEASLAGPKRPQDRVALGDVPKAFAASAELELNTAQRDRQPVDYTMNGQPYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLAQAKLTPYLDELGFNLVGYGCTTCIGNSGPLPEPIETAIKKGDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYALAGNMNINLATDPLGYDRKGDPVYLKDIWPSAQEIARAVELVSSDMFRKEYAEVFEGTEEWKSIQVESSDTYGWQSDSTYIRLSPFFDEMQAQPAPVKDIHGARILAMLGDSVTTDHISPAGSIKPDSPAGRYLQNHGVERKDFNSYGSRRGNHEVMMRGTFANIRIRNEMLPGVEGGMTRHLPGTEAMSIYDAAMLYQQEKTPLAVIAGKEYGSGSSRDWAAKGPRLLGIRVVIAESFERIHRSNLIGMGILPLEFPQGVTRKTLGLTGEEVIDIADLQNLRPGATIPVTLTRSDGSKETVPCRCRIDTATELTYYQNDGILHYVIRNMLN