wanglab/gogpt-training-data huggingface dataset:
Protein: Pericentrin-like protein, isoform K (M9PFJ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MNLYTIYDWITSLLRPHGASVSYKAIEAATLEELPATSVATATSTAATSRATGGAAATCVDVEFIPTLNIIFEKPTSSSEQLQCAEKSEHVAGGVSDKEPADDCDSDNDSTRTYIISRSSWTGVTSSSSTPYAVTSTDTAELLRRQNNLSLTEEDQSVSSFSIEQPTSSITIEMADQRTTTTTTTTATTATTPSSANILATTATTTTTTSSSIEEEIEEAIEISEVEEQLNTPLESLSEAAAYARPKDEQSSAKSLSSNPAEDEDADEFRIDDAQLSGGQLAQHFLVDEDESEEGSDLPAASKVEVSLSSNDDDFDISLPLEQRKPVHSLHEDDESVDQSLSNQSTTDDVSELVEEPVHEMDDKTDGSAAISASAPQETQVDESQITDEQDHSMEEIVATNESIEVTYEAEETVNTSQKQDLITDLDEESEDQVHVDNRPTSTLQALKLPALQQPQIVERKAATALTTLRLQADVLEPLELTILEMDDDENEEDDDDEESSLQLMKLRLMAMNQQMIVDNAPKLSPTEAEQTQVTSSSNNLEIKQMERVPLTEFSKDVLEDITEESERLLSMSTTMEEEQDPPSLSLDESKTLLQPGAHKTGGSSSSLVSLNMLKQLEAKVQELHTQLETKDNCLASLNLQLETARRESSAGPASARDSSSLMTNSTEYRTLQEELGGPTLDIYVEMSRRDELIAKLTDSLQQSLNVRDKLQVDADRLGGEVQNLRRQLQETLDAVKRSSAVWPDQECNPGQRISEISMDLISESDDDLDRHFLTDNEERGSRSSKERQLTQLQTNEELGLQASNPEWTPTFSKQIEQFHTYLLPTEQRIFQMVQRKFDDYLNQQITLCRDLGAQELKIARDQWESEKLTSEQNQQAAHAKQMEDLRKYFEHKCADLEKQFSDDVFSHKSQHQTGDSSSECSEVDQLPEEGAAAVSSKEPSPRKRKRAELLLSPSHRQMTPCGLDSLGENTGKTEKDNTADIADLKIFYQTHIKELKRAHEDQVRKLSDRIKFYERQQGDDDYKSLLSENTVDDQHWPKELILLREKFTAKSQLEITQLNIKHAEEMSRLKLEFEKQLNRKNKRHLTFDAARDLEQVICERDGLRELSKSFRSVLCRLAKCVAHCEEDLNATLSEEVQRLLFHSRSQDGGDDLEATISSSLNNTKHMLRVPDVHSLLEVVEDPSLVQFIDSKSNEEPSEDFDLNDCLERLKSEASYLLHLSEDLHKQRTHDESSEHLDEPEKQEHELCCEAEDGLKTTGAVNQQVLSKFLRTNSLNDQQMGVANQRKNSNPEAGKTHSSLPPDLQEHAGNASELSFQLVQLKNRLIKSEADRQNLQQQLSRTIDRNAELGQELQALRDQLSQLNSLNHTDYNEGYGLGTMKSLQEQGLDQSSASFLALQERARHLLSSSPVKEQPSRDHGNSTVILLQMIEDFCREGDKVVEFSKKDREDLQSQIDTADKQLKDTRRFLEDQAAEREQERDEFQREIERLKAQLRDKEKEHSSYANASEELKVAKRKHYAQLESQFREVNQQLCESNAKRDKFEVELKASIDKIFVLREIISELETQVQTKALNEEVLAEKAQQLEEYVSLQMRDNDILQQEVHSLKTDIGEGYQSRIRVLEEKLKQSGPTAEQGVVLSQVAEKLRDIETTLDQKTKALESLHNSNATSNSASLSVTEDVSIHGSKEPTAVGSPSHPSLTVEGVQRVTEKLDRHTRVEEAAIKRIRDLEMQVHQMRAGCVELQHERDTLQGRMEEQTQRISTLQNRLEEQRQRAEQLHRTGTSDLNTRVHELQGEVQNLYEQLAARDKQMANMRQQLQRSKEEITRLETEVEVRTQPDRSLVNKLQAEVQQKGAEIVKLKDKIRTEMINRLAIPDLMETMLADKNDEIDHLRDQLEAKEKELQASQQEASQISSPSGAAGKQEGSGGKLSARTLSDIGSITEFPEPDVERRAAMRSLTALQMSEGAGGFLHQTMETSKEAVANLTHKRTDDLSGFIVPYPVNTFEHPHYFQALGVTAQSTDGLTPGLVPRQINFSNLTEDSKLKTTSLLMHTPELPRPTTPPEIHQLRVKLSDLQTEKQRQQSELEKKLQDLQKELEQEKEKLSRQAQTLQSYEESEAKYRLRIENLESKVLETAAQAASDRENLRKELNCVSAAHEQCENAAAARKRELEKLNSEVKVKADQLHAALRRCADLELQVLTLERDLERLKNSDNSSKQYSVDEIAQQVEKELNYSAQLDSNILKAIESEEENNLDKKLQKGVQTEEETLPGTGNGTDDENFTGERELLNQLEALRAQLAVEREQCEAMSKELLGEKQHSQDIQEQDVIIIEAMRKRLETALDAEDELHKQLDQERERCERLQTQLTSLQRAESRRNSSLLLKSPGDSPRKSPRADFESELGDRLRSEIKLLVAQNERERERSADAQRSSERERQRYEKELQERVAYCERLKQEMEKLSRDKESAETELEHFNERLTLQASEIESLEARLVTLQEAETRRANTRTRQHQENVKLQAEIHELKSKLLAAEAARDCLDQKVTQLRFDVSRSGQREAKLAEALAQANDRLAHSTDDNVPAQFMQKMKEINALLAENTQENRQMAETVQFLVGERIALQKKCEELGGAGNTNVTELEERCRQLIGRYLRVESHRKALVYQKRYLKLTLEGYQASEQLALQNLRGGAEQPPQRNIKKKFKTVALAIIAIQRIKYIGRIWHTGKRIVSKSVFTITQQRSPGLNLNVAPPQSPLPGPNSNLPTNNNNLMGRLSYAPLSPPMVNFSTVQPIMLPSDFTLQAPTTSLQTTIANNNSENTLPSLARLDWPTMQKPKRAHARHH
Protein: Nucleoside kinase (NK) (Adenosine kinase) (EC 2.7.1.20) (Broad specificity nucleoside kinase) (Cytidine kinase) (EC 2.7.1.213) (Guanosine-inosine kinase) (EC 2.7.1.73) (Q9HJT3)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Function: Nucleoside kinase with broad substrate specificity. Catalyzes the phosphorylation of a variety of nucleosides to the corresponding nucleoside 5'-mono-phosphate in the presence of phosphate donors and divalent cations. Displays the most efficient activity with guanosine, followed by inosine, cytidine, and adenosine. Negligible enzymatic activity is detected with thymidine, uridine, and 2-deoxyadenosine. ATP is the most efficient phosphate donor, but can also use GTP and ITP. Shows no sugar kinase activity, since it is unable to phosphorylate ribose, fructose-1-phosphate, or fructose-6-phosphate.
Interaction partners:
- Adenylosuccinate synthetase
- PurH bifunctional enzyme related protein
- GMP synthase subunit B
- Inosine-5'-monophosphate dehydrogenase
- Cytidylate kinase
- GMP synthase subunit A
- Enolase
- Carbonate dehydratase related protein
- Ribulose-phosphate 3-epimerase
- Adenosylhomocysteinase
Sequence:
MRFLAYFGHLNIDVLISVDSIPREGSVNVKDLRPRFGGTAGNFAIVAQKFRIPFDLYSAVGMKTHREYLAMIESMGINTGHVEKFEDESGPICYIATDGKKQVSFMHQGAMEKWKPQLADEYEYVHFSTGPNYLDMAKSIRSKIIFDPSQEIHKYSKDELKKFHEISYMSIFNDHEYRVFREMTGLSSPKVTTIVTNGERGSSLFMDGKKYDFPAIPSSGDTVGAGDSFRAGLYLALYNRRSIEKGMIYGTIIAHHVIDDGIENFSLNMEDLERETENYRRMFTKRS
Protein: Integrin beta-nu (Q27591)
Organism: Drosophila melanogaster (Fruit fly)
Function: Contributes to endodermal integrity and adhesion between the midgut epithelium and the surrounding visceral muscle. Essential for migration of the primordial midgut cells and for maintaining, but not establishing, cell polarity in the midgut epithelium. Can only partially compensate for the loss of beta-PS integrin during primordial midgut cell migration. The two beta subunits mediate midgut migration by distinct mechanisms: beta-PS requires rhea/Talin and beta-nu does not. Integrin alpha-PS3/beta-nu is required for effective phagocytosis of apoptotic cells during embryonic development and for the phagocytic elimination of S.aureus by mediating the binding of S.aureus peptidoglycan to larval hemocytes, which probably activates a signaling pathway involving Rac1 and Rac2. Not required for the production of antimicrobial peptides during S.aureus. Upon activation by LanA, integrin alpha-PS3/beta-nu activates Fak in presynapsis to suppress neuromuscular junction (NMJ) growth during larval development and during low crawling activity, but not during higher-crawling conditions. Mediates, together with LanA, glutamate receptor-modulated NMJ growth.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin alpha-PS3
- Integrin alpha-PS5
- Integrin alpha-PS4
- Integrin alpha-PS1
- Viking, isoform A
- Laminin subunit gamma-1
- Laminin subunit beta-1
- Integrin beta-PS
- Laminin subunit alpha
- Integrin alpha-PS2
Sequence:
MTSLGGRAFLWIYLVFLIAEISHSDADSIDDQCRHADSCERCLSAHLECAWCTDKEYQVGYRCLSRRQLLNYNCSETDIYENQPVLDVLQDKPLKDYETSDQAVQVTPQRAYLKLVKGNTQRMKLSYRTARNNPLDLYVLMDLTWTMRDDKKTLEELGAQLSQTLKNLTGNYRLGFGSFADKPTLPMILPQHRENPCAAERATCEPTYGYRHQLSLTDDIPAFTSAVANSKITGNLDNLEGGLDALMQVIVCTKEIGWKEQARKVVILVTDGFMHLAGDGLLAGIIQRNDKQCHLNKAGEYTGSLNYDYPSLEEIYRELLRRKINVIFAVTEEVVSSYWELSALMKEISYVDILSADSSNILELIKKSYESLIKRTQFADNSPDFIDMAYYTDCGGQFPSLQKRNYCNNVTLGKQIDFYVDVTLKKYPDNQVYTHKIRVEETSLSEFMDLDVELQRPCPCQETPDPENEEGRFLCDYKGYLYCGMCECDEGWTGTYCNCPTDATNVTSNEALLQKCRQPFSDKSTSELVCSNHGDCDCGTCLCDPGYTGPFCECRECLDCDEKLADCFCGQCVCKYGWSGSKCNCDGDTDACVGPTGEICSERGTCQCEECQCEEPYLGKFCEIDPEKDNKLCLFYEPCVTCLIEQKQGMGVCENLTEICSSLDRQETYPYNFVHELDPEQDQCLVRLVNKHGIQCDSFFVYQVIDHSNFLTIQAVDCEPPDYVALVGYISAFTLLIGLLIIFIILWYIRAKDAREYAKFEEDQKNSVRQENPIYRDPVGRYEVPKALSVKYDENPFAS
Protein: SET domain-containing protein 8 (EC 2.1.1.-) (O14135)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein wos2
Sequence:
MDIKYNELVNQFAPGAKQITIKKIRKKGNGIFSLNRYTSGTVLLEVPLENIICRKTVEQFRNSCDKFASIATLEEWNDMSFRTQAMLFLCYLWLGIQPRTNKWDKFLTVLPLSINTPAQWPEKEVYSLQGTSIFNPVCVKRKILQQEWLSLNQRYSDSWPSKITLPKWVHADALFHSRCLESPFKDPVLAPVIDLCNHSSKSNAKWSFSEDAMQLYLDKDIDENEEVTINYGSEKGSAEFLFSYGFLPEPEGDRITNVMKLLIPEDSNDSLDLAKRRSCKTPPMIEFVSDSSGELWWHAPFLFFSVLNVEDFTNFKMVCDESKAQTVDWEFEGQKCSVEDLPKLVQLSPKRDLYILRVFCLAEQLADAALNTNIENMYNPTERRSESVELLKRESFLLKKVLLYLRDVISKLLKSKVVVEFIHSQTIES
Protein: Pluripotency associated transcript 25 (A0A1Y7VLS7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MHTGEKPYECHQWEKAFSSHSNLLQPKGTHTGEKCYECDLCGKAFSQHYTVQKHKRTHIGQKPYKCNECDKAFSQNRDLQTHKRRHTGEKPYNCNKCEKAFSQHNALQYHRRIHSGEKPYKCNKCEKAFSQHNALKYHRRIHSGEKPYKCNECDKVFRQSSDLQKHRRTHTGEKPYKCNQCEKVFSQHHHLQIHKRSHTGEKPFKCNECDKAFSQLGNLQSHRRIHTGEKPYKCNTCEKAFSQHSHLQSHRRIHTGEKPYRCNKCEKAFSQHSNLQSHRRIHNGEKSFKCNKCEKAFLQHYSLQRHKRIHTG
Protein: V-type proton ATPase 16 kDa proteolipid subunit c (Vacuolar proton pump 16 kDa proteolipid subunit c) (Q9VFE5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit H
- Probable V-type proton ATPase subunit d 2
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit G
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase proteolipid subunit
- ATPase H
- ATP synthase subunit a
Sequence:
MISKMSFGLFFMLFVLGAASLGAVGIIFANVMVNMGERMGLGWFLYTSNPFLWSGMGIFLACALSVLGAASGIYMIGCSVAGGGVRSPRIKTKNLISVIFCEAVAIYGLITAILLSGNVNKFSSVRLITDSTVMATNMFTGFATFGAGLCVGMVNVACGIAVGIVGSGAALADAANSALFVKILIVEIFGSAIGLFGLIVAIYMTSKAETIN
Protein: AT29209p (Q8T8U7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METPSELTEKQNQDQPTQDQPTYQPRLNEVAQKFLADLDAERKRLSAEFPLCALLIDESVDRVYSTGRIPGKEPFADVYQQKPMKIIQKVFVPVNKFPKFNFTGKILGPKGNSLRRLQEETHCKIVIKGRNSMRDRNKEEELRSSGDPRYAHLHKDLFLEVSAVAPPAECYARIAYALAEIRKYLIPDDNDDVWHEQQRELMEMNPKSAKKSNGLNMAPYRSNFDKAIGAIRNRAPKYNNQIRRVTENPREVAYMEEVEYDYDEHLMFCSPVVRL
Protein: Variant surface glycoprotein (VSG), putative (Q57TS0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MQATSLVLVVACAAICAANRASAAAANEGDNAAAYATLCSAVAVLSTPYAAPSTPEINDALLAEAQALNFSLHHPEAADELAQEGKDSMDKLKKGGKAQKLATEQSFADYKNKAATAKAMAKERPYARVKKTLNNGFLTTQIKKVIDDIQATVDITQKIKVQEHTNTANSKMNKAVYGTDEPNDSVRVVDAAGATTRDAVCGKPGNANAQRRAGKSLKQDIMCICALLTSGQGQTACANLSPALDKDPTGGTDLEDDWKKLHQTCLARYHKNAPTADRIRAVAANVQHTIAQSTANGNKITHILGKTNRDPATNGCNGDVGDNSGCCVYYGRGAGATLTYKIEWAEAMEEAAQAIKAAEQAAAQKTELLAKLTLLNTTLANLAKAAMEAQAAASPTTERAPQQADTKTAEDQEKVCNAAGNDENKCKDLESQGCKYDENKPADQKCTLKKEVKEKLEKEGKKDGATATTVKCSEYGSQDKCEEVNKEKDKPVCGWRSGKDNEDDKDAKKCRNGSFLASKQFALIAVVFDCLVAF
Protein: DNA replication and repair protein RecF (P0A7H0)
Organism: Escherichia coli (strain K12)
Function: The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Beta sliding clamp
- DNA repair protein RecO
- Chromosomal replication initiator protein DnaA
- Recombination protein RecR
- DNA gyrase subunit B
- ATP-dependent DNA helicase RecG
- Single-stranded-DNA-specific exonuclease RecJ
- Protein RecA
- Holliday junction branch migration complex subunit RuvA
- DNA helicase II
Sequence:
MSLTRLLIRDFRNIETADLALSPGFNFLVGANGSGKTSVLEAIYTLGHGRAFRSLQIGRVIRHEQEAFVLHGRLQGEERETAIGLTKDKQGDSKVRIDGTDGHKVAELAHLMPMQLITPEGFTLLNGGPKYRRAFLDWGCFHNEPGFFTAWSNLKRLLKQRNAALRQVTRYEQLRPWDKELIPLAEQISTWRAEYSAGIAADMADTCKQFLPEFSLTFSFQRGWEKETEYAEVLERNFERDRQLTYTAHGPHKADLRIRADGAPVEDTLSRGQLKLLMCALRLAQGEFLTRESGRRCLYLIDDFASELDDERRGLLASRLKATQSQVFVSAISAEHVIDMSDENSKMFTVEKGKITD
Protein: COP9 signalosome complex subunit 3 (SGN3) (Signalosome subunit 3) (JAB1-containing signalosome subunit 3) (O88543)
Organism: Mus musculus (Mouse)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes (By similarity). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 (By similarity). The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases (By similarity). CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity). Essential to maintain the survival of epiblast cells and thus the development of the postimplantation embryo.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UNS2}. Nucleus {ECO:0000250|UniProtKB:Q9UNS2}.
Interaction partners:
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 7a
- COP9 signalosome complex subunit 7b
- Growth factor receptor-bound protein 2
- Ubiquitin-like protein NEDD8
Sequence:
MASALEQFVNSVRQLSAQGQMTQLCELINKSGELLAKNLSHLDTVLGALDVQEHSLGVLAVLFVKFSMPSVPDFETLFSQVQLFISTCNGEHIRYATDTFAGLCHQLTNALVERKQPLRGIGILKQAIDKMQMNTNQLTSVHADLCQLCLLAKCFKPALPYLDVDMMDICKENGAYDAKHFLCYYYYGGMIYTGLKNFERALYFYEQAITTPAMAVSHIMLESYKKYILVSLILLGKVQQLPKYTSQIVGRFIKPLSNAYHELAQVYSTNNPSELRNLVSKHSETFTRDNNMGLVKQCLSSLYKKNIQRLTKTFLTLSLQDMASRVQLSGPQEAEKYVLHMIEDGEIFASINQKDGMVSFHDNPEKYNNPAMLHNIDQEMLKCIELDERLKAMDQEITVNPQFVQKSMGSQEDDSGNKPSSYS
Protein: V-type proton ATPase 21 kDa proteolipid subunit c'' (V-ATPase 21 kDa proteolipid subunit c'') (G5EDB8)
Organism: Caenorhabditis elegans
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). The V-ATPase is required for the function of the excretory canal. Involved in receptor-mediated endocytosis.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit e
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit C
- V-type proton ATPase subunit D
- V-type proton ATPase subunit
- V-type proton ATPase catalytic subunit A
- Probable V-type proton ATPase subunit F
- V-type proton ATPase 16 kDa proteolipid subunit c 2
- Probable V-type proton ATPase subunit G
- V-type proton ATPase 16 kDa proteolipid subunit c 1
Sequence:
MAAGAILKTTATLTVITTLIILGTGLFYMLSGQGHRFDIGWFLTSTSPHMWAGLGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAPRIRTKNLVSIIFCEAVAIFGIIMAFVFVGKLAEFRREDLPDTEDGMAILARNLASGYMIFGGGLTVGLSNLVCGLAVGIVGSGAAIADAANPALFVKILIIEIFASAIGLFGMIIGIVQTNKASFGNK
Protein: Protein phosphatase EYA4 (EC 3.1.3.48) (Eyes absent homolog 4) (O95677)
Organism: Homo sapiens (Human)
Function: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. May be involved in development of the eye (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99502}. Nucleus {ECO:0000250|UniProtKB:Q99502}.
Interaction partners:
- Homeobox protein SIX1
- Transcription factor 21
- Homeobox protein SIX4
- Homeobox protein SIX2
- NLR family member X1
- RNA-binding protein 20
- ATP-binding cassette sub-family C member 9
Sequence:
MEDSQDLNEQSVKKTCTESDVSQSQNSRSMEMQDLASPHTLVGGGDTPGSSKLEKSNLSSTSVTTNGTGGENMTVLNTADWLLSCNTPSSATMSLLAVKTEPLNSSETTATTGDGALDTFTGSVITSSGYSPRSAHQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAVYTAYSQTGQPYSLPTYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSGSQQDYPSYTAFGQNQYAQYYSASTYGAYMTSNNTADGTPSSTSTYQLQESLPGLTNQPGEFDTMQSPSTPIKDLDERTCRSSGSKSRGRGRKNNPSPPPDSDLERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYSFATDGFHAAASSANLCLPTGVRGGVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLTNALKSLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIMQRFGRKVVYVVIGDGVEEEQAAKKHNMPFWRISSHSDLLALHQALELEYL
Protein: Serine/threonine-protein kinase GIN4 (EC 2.7.11.1) (Growth inhibitory protein 4) (Q12263)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine-protein kinase which regulates the localization and the function of the septins during mitosis. Phosphorylates SHS1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Bud neck {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cell division control protein 12
- Seventh homolog of septin 1
- Mitosis inhibitor protein kinase SWE1
- Cell division control protein 3
- Cell division control protein 11
- Cell division control protein 10
- Nucleosome assembly protein
- Probable serine/threonine-protein kinase HSL1
- Serine/threonine-protein kinase ELM1
- Serine/threonine-protein kinase RIM11/MSD1
Sequence:
MAINGNSIPAIKDNTIGPWKLGETLGLGSTGKVQLARNGSTGQEAAVKVISKAVFNTGNVSGTSIVGSTTPDALPYGIEREIIIMKLLNHPNVLRLYDVWETNTDLYLVLEYAEKGELFNLLVERGPLPEHEAIRFFRQIIIGVSYCHALGIVHRDLKPENLLLDHKYNIKIADFGMAALETEGKLLETSCGSPHYAAPEIVSGIPYQGFASDVWSCGVILFALLTGRLPFDEEDGNIRTLLLKVQKGEFEMPSDDEISREAQDLIRKILTVDPERRIKTRDILKHPLLQKYPSIRDSKSIRGLPREDTYLTPLSESNSSIDATILQNLVILWHGRDPEGIKEKLREPGANAEKTLYALLYRFKCDTQKELIKQQQVKKRQSISSVSVSPSKKVSTTPQRRRNRESLISVTSSRKKPISFNKFTASSASSSNLTTPGSSKRLSKNFSSKKKLSTIVNQSSPTPASRNKRASVINVEKNQKRASIFSTTKKNKRSSRSIKRMSLIPSMKRESVTTKLMSTYAKLAEDDDWEYIEKETKRTSSNFATLIDEIFEYEKYEQIRKEKEELERKVREAKAREELERRRRKQEEKERARKLLEKEDLKRKQEELKKQIEIDISDLEQELSKHKEEKLDGNIRSISAPMENEEKNINHLEVDIDNILRRRNFSLQTRPVSRLDPGIMFSSPTEEVSPVEPKRTENERLTTEKKILETIRRSKFLGSSFNIDKELKLSKMEYPSIIAPQRLSEERVVSDSNDGYESLILPKDGNGVSQLKDSTATTAPVSDGRLRKISEIRVPQFTRKSRHFSESNKRLSVLSMYSTKESFTNLVDILKNGNLDVNNQQSQRIPTPRSADDSEFLFETVNEEAEYTGNSSNDERLYDVGDSTIKDKSALKLNFADRFNGSNEAKQTDNLHLPILPPLNGDNELRKQNSQEGDQAHPKIKSMIPESGSSSHTEKEEENEEKEEKKPEQHKQEEDQEKREKVVDDMEPPLNKSVQKIREKNAGSQAKDHSKDHLKEHKQDKNTAIGNGSFFRKFSKSSDKTMELYAKISAKQLFNGLEKLLRGWTQYGLKNIKSHPNNLTLTGKLSSDNIFSLRSTLFEVNIYPRGKMSVVQFKKVSGSFKAVKKLVNEVENVLNKEGVLQK
Protein: Granulin precursor (K7EQ05)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MWTLVSWVALTAGLVAGTRCPDGQFCPVACCLDPGGASYSCCRPLLDKWPTTLSRHLGGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCLRREAPRWDAPLRDPALRQLL
Protein: UBX domain-containing protein 10 (Q0P3Z8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for ciliogenesis. Acts as a tethering factor that facilitates recruitment of vcp/p97 to the intraflagellar transport complex B (IFT-B) in cilia (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q96LJ8}.
Interaction partners:
- UBX domain protein 2A
- UBX domain-containing protein 6
- ASPSCR1 tether for SLC2A4, UBX domain-containing.
- NSFL1
- Intraflagellar transport 74.
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Intraflagellar transport protein 56
- Intraflagellar transport 88 homolog.
- Transitional endoplasmic reticulum ATPase
- Transitional endoplasmic reticulum ATPase
Sequence:
MHVTRPKSSKGRSRPMITNSSMIYTPSQPSALSPQPPAAAKTKDKSNQSLRSRAILRRSSQPTTDILTEAYDRPPEEPVSLNRYRVLPSIEKKTSTDNQKCSQCVSRHRKCQHTNARLDVVSDSTPPEESDLLLAIRTPCGQRFKRSFRPSDQLKGVLSAAEAEFGDRFDNCIIETMDVPRRTFSNLTMTLAQCGVLNKSVLCISHDDSEMDLT
Protein: Muscular LMNA-interacting protein (Cardiac Isl1-interacting protein) (CIP) (Muscular-enriched A-type laminin-interacting protein) (Q5VWP3)
Organism: Homo sapiens (Human)
Function: Required for precocious cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays an important role in protection against cardiac hypertrophy. Acts as a transcriptional cofactor, represses transactivator activity of ISL1 and MYOCD.
Subcellular location: Nucleus {ECO:0000269|PubMed:34581780}. Nucleus envelope {ECO:0000250|UniProtKB:Q5FW52}. Nucleus, PML body {ECO:0000250|UniProtKB:Q5FW52}. Cytoplasm, cytosol {ECO:0000269|PubMed:34581780}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q5FW52}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5FW52}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5FW52}.
Interaction partners:
Sequence:
MLSEQGLLSDCGNNYFQMTSCILSGSIQTTPQVSAGGSEAKPLIFTFVPTVRRLPTHTQLADTSKFLVKIPEESSDKSPETVNRSKSNDYLTLNAGSQQERDQAKLTCPSEVSGTILQEREFEANKLQGMQQSDLFKAEYVLIVDSEGEDEAASRKVEQGPPGGIGTAAVRPKSLAISSSLVSDVVRPKTQGTDLKTSSHPEMLHGMAPQQKHGQLTSSPTTSEQLACKPPAFSFVSPTNPNTPPDPVNLEGASVLEEFHTRRLDVGGAVVEESATYFQTTAHSTPFSASKGTSSTLLFPHSTQLSGSNLPSSTAADPKPGLTSEVLKKTTLTSHVLSHGESPRTSSSPPSSSASLKSNSASYIPVRIVTHSLSPSPKPFTSSFHGSSSTICSQMSSSGNLSKSGVKSPVPSRLALLTAILKSNPSHQRPFSPASCPTFSLNSPASSTLTLDQKEKQTPPTPKKSLSSCSLRAGSPDQGELQVSELTQQSFHLPVFTKSTPLSQAPSLSPTKQASSSLASMNVERTPSPTLKSNTMLSLLQTSTSSSVGLPPVPPSSSLSSLKSKQDGDLRGPENPRNIHTYPSTLASSALSSLSPPINQRATFSSSEKCFHPSPALSSLINRSKRASSQLSGQELNPSALPSLPVSSADFASLPNLRSSSLPHANLPTLVPQLSPSALHPHCGSGTLPSRLGKSESTTPNHRSPVSTPSLPISLTRTEELISPCALSMSTGPENKKSKQYKTKSSYKAFAAIPTNTLLLEQKALDEPAKTESVSKDNTLEPPVELYFPAQLRQQTEELCATIDKVLQDSLSMHSSDSPSRSPKTLLGSDTVKTPTTLPRAAGRETKYANLSSPSSTVSESQLTKPGVIRPVPVKSRILLKKEEEVYEPNPFSKYLEDNSDLFSEQDVTVPPKPVSLHPLYQTKLYPPAKSLLHPQTLSHADCLAPGPFSHLSFSLSDEQENSHTLLSHNACNKLSHPMVAIPEHEALDSKEQ
Protein: histone deacetylase (EC 3.5.1.98) (C9JEB6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHSPGADGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPMDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVGPQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEP
Protein: UPF0508 protein YJR030C (P47101)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Protein SKG3
Sequence:
MELFNKEEASFETLLKRLLVVCESHSRYHGSSLDPMVKVGHEMRKISGYLRCILRKHAANHDDMSLTQSIVNSYKSLFKDAQILDLYHNLLFGCMHLLLDANMSYFRMDSQKLFAVLLFKVYYKLRDIFYVTNEVRLGSLISAFVYKFKSCYDFISCNSLKYGSVRDVISGEVSLINLPPIDSNKVINRAYYRLDVKKLAINNKLVEILELDNGEIAIFEVLSEKMPYTLQTIDNLFQSLALGNHDLMNVGRSLLFRPFRSGDLDLIRLDDSGAKLKVPINNSIVLRLTCKDPIQWQEYWKHVIRKLFDSTATKEYKRSGSKISQQVYVRSNNPDYTSPKRNDDMPISSVKISDTIHNGRTLHRSIPLPGSLSSLIETSNEYPDEESLSIMSERATVSEDSDLDTSLKDIESLSCEKLIELDKSIQVPLSPKYMDTPTLKNIRTASQTFSLESVSPELIESVASEIDDSESIISEDGKDKRDKDLFDPDIDFYKPTLYRRKSSSLLSIFSKNKKNLTIDIPKNHSRSLFSLPGNQQSVTPVSATPHDDNVDETYVSFPLSINTSGGAVYFENDSVKVSLWNGKSWVPLSKDMLCLSLILSGDNETLLIVYKDFEKEKCKLVVKLEPTWKYNRSTAQDVQLRIPSSDFKASVFGTLHDLTLSIRCAQAAKLVNVLQYQLQSSQTSSLSPSTTTGTLSTVSSSSCFSRNVTRSSTENSELANMKDSSEYISSSLLLSSVKVRQLRNM