wanglab/gogpt-training-data huggingface dataset:
Protein: Myosin-17 (Myosin XI K) (AtXIK) (F4K5J1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in the tip growth of root hair cells and in the elongation of trichome stalk and branches. Plays a major role in trafficking of Golgi stacks, mitochondria and peroxisomes during root hair development. Acts as the primary contributor to ER streaming with a major role in the movement of Golgi bodies. Required for development of pavement cells, trichomes, and stigmatic papillae.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17288617, ECO:0000269|PubMed:17500056, ECO:0000269|PubMed:18503043, ECO:0000269|PubMed:20351265, ECO:0000269|PubMed:22969781}. Note=Colocalizes with peroxisome, cytoplasmic vesicles, endomembrane vesicles, endoplasmic reticulum and/or organelles.
Interaction partners:
- Myosin-binding protein 1
- Myosin-binding protein 2
- Myosin-binding protein 7
- Protein PHOX1
- Myosin-binding protein 3
- Ras-related protein RABC2a
- Secretory carrier-associated membrane protein 5
- Ras-related protein RABD1
- Myosin-like protein
- Protein ROOT HAIR DEFECTIVE 3
Sequence:
MVGPVNIIVGSHVWIEDPGAAWIDGEVVKINGEEVHAHTTNGKTVVANIANVFPKDTEAPPGGVDDMTKLSYLHEPGVLNNLAMRYELNEIYTYTGNILIAVNPFQRLPHLYDTHMMEQYKGAGFGELSPHVFAIAEVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVELQFDNCGRISGAAVRTYLLERSRVCQISDPERNYHCFYLLCAAPPEEREKFKLGDPKLFHYLNQSKCYKLDGVDDTEEYLATRRAMDIVGISEEEQDAIFRVVAAILHLGNVNFAKGKEIDSSVLKDEKSRYHLDVCAELLRCDAKKMEDALIKRVMVTPEEVITRTLDPDSATGSRDALAKTIYSRLFDWLVDKINNSIGQDPNSKTIIGVLDIYGFESFKINSFEQFCINFTNEKLQQHFNQHVFKMEQEDYTKEEINWSYIEFVDNKDVLELIEKKPGGVIALLDEACMFPKSTHETFAQKLYQTFKNYKRFTKPKLSRTSFAISHYAGEVTYQADLFLDKNKDYVVAEHQDLLIASSDTFVAGLFPRLPEETSSKTKFSSIGSRFKLQLQSLMETLSSTEPHYIRCVKPNNVLKPAIFENVNVIQQLRCGGVLEAIRISCAGYPTKRTFYEFLNRFGVLAPEVLEGNYDDKVACKMLLDKIGLKGYELGKTKVFLRAGQMAELDARRAEVLGNAARRIQRQSRTFIACKEFRALRGAAIVLQSNCRGKLACNLYEEMRRQAAAVKIQKIFRRHIARESYLRIRHSTITVQTALRGMVARNEFRFRKQMKAATIIQARLRSHLTHSYYKQLQKAALSTQCGWRSRVARKELRTLKMAARDTGALREAKDKLEKRVEELTWRLQLEKRQRTELEEAKTQEYAKQQEALETMRLQVEEANAAVIREREAARKAIEEAPPVIKETPVLVEDTEKINSLTSEVEALKASLQAERQAAENLRKAFSEAEARNSELATELENATRKADQLHESVQRLEEKLSNSESEIQVLRQQALAISPTSRTMATRSKTMLLPRTPENGNYLNGGTKTTPDMTLAVREPESEEKPQKHLNEKQQENQDLLVKCISQNLGYNGDKPVAACVIYKCLLHWRSFEVERTSVFDRIIQTIATAIEVPDNNEVLAYWLSNSATLLLLLQRTLKATGAASLTPQRRRTTSASLFGRMSQGLRGSPQSAGLSFLNRQGLTKLDDLRQVEAKYPALLFKQQLTAFLEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGRAQANAVAQQALIAHWQSIRKSLNSYLNLMKANNAPPFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELEQWCIEATDEYAGSAWDELRHIRQAVGFLVIHQKPKKTLDEITRELCPVLSIQQLYRISTMYWDDKYGTHSVSSDVIANMRVMMTEDSNNAVSSSFLLDDDSSIPFTVEDISKSMQQVDVNDIEPPQLIRENSGFGFLLTRKEGSTS
Protein: GIM5A protein (Q9N9D0)
Organism: Trypanosoma brucei brucei
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271}.
Interaction partners:
Sequence:
MSAQAHTYLCDAWNRDKVMAIVQFLPMALEGPARTAGCESLALSLGNLARMGDAYRAVTRLSLLANALSKPTLTSLSKPTGDMVASRIDQLSHLFHIGFCLNENTAVLAGHGVFPKSLHRLSGVAVLCWMYTLVLGIVRQLYLFVKLRPRQASRGAGAGDDKKVPAYTYLELKRAFVNLLKLVCYFLFALTCLPEGKPQLLANASGPLVPLHVMVKALSPNPLHASNTVRGLLGLIASVCEFY
Protein: glycogenin glucosyltransferase (EC 2.4.1.186) (A0A0B4LFW5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glycogen [starch] synthase
- 1,4-alpha-glucan branching enzyme
- Glycogen debranching enzyme
- FI19480p1
- Protein phosphatase 1 regulatory subunit
- Uncharacterized protein, isoform A
- Uncharacterized protein, isoform B
- DNA polymerase delta subunit 2
- DNA polymerase delta catalytic subunit
- DNA polymerase zeta catalytic subunit
Sequence:
MSKFAWVTLTTNDTYSLGALVLAHSLKRAKTAHQLAVLVTPNVSQAMRDRLKEVYNVVQEVNVLDSQDAANLALLSRPELGVTFTKLHCWRLVQFEKCVFLDADTLVLQNCDELFEREELSAAPDVSWPDCFNSGVFVFKPSVDTFAQITEFAVKNGSFDGGDQGLLNQFFADWSTADIKKHLPFVYNVTAYASYCYLPAFKQFRDKIKILHFAGKLKPWLIQFNSETKVASVSSEYAHAQDLIQLWWNIFCENVIQSLSTEMQTPGNVASDRPAGEMAQGSTTLECLCLNIIRTQSEFAADELHQRQQHEFYQQQKLHHHLLHVRQFRDPWADYYENLEKEPQEQEQEQQRHQHQQQHHNPSQNHSQDNGNADAAAHENDSTIANANATDWHHDDACHPPAPTRPLPQIQNQAHNANATANAEDFSFVDVNSNELNISQPPEHASYSSDTATPTATATPTATPTLTPTPHHSVHSQTVEKATSHQQEHEVAATTPPEAGLAGALSQLRIGQQRTPEQEAYENQMRRQCWESGQIDYTGADSFENIWKKISQTLERKTDKESEETDNDNDSDPANPLSSARLLNEAASILLHPPEKSPTSKAMKANGATGNGSHLDQSHPTNSPATNKQPANASASPNASLKQNPQKRQEKPQPQAEPELEPRPQPQPQPTEQHIRMQPGGGNGSVSKSGKQRSARKFK
Protein: Monocarboxylate transporter 1 (MCT 1) (Solute carrier family 16 member 1) (Q03064)
Organism: Cricetulus longicaudatus (Long-tailed dwarf hamster)
Function: Bidirectional proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH (By similarity). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart. Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 302-Asp is essential for the conformational transition (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1429658, ECO:0000269|PubMed:8124722}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Basolateral cell membrane {ECO:0000269|PubMed:8124722}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Apical cell membrane {ECO:0000250|UniProtKB:P53985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Note=Expression at the cell surface requires the ancillary protein BSN. {ECO:0000250|UniProtKB:P53985}.
Interaction partners:
Sequence:
MPPAIGGPVGYTPPDGGWGWAVVVGAFISIGFSYAFPKSITVFFKEIEGIFNATTSEVSWISSIMLAVMYAGGPISSVLVNKYGSRPVMIAGGCLSGCGLIAASFCNTVQELYLCIGVIGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFLSTLAPLNQAFFGIFGWRGSFLILGGLLLNCCVAGSLMRPIGPKPGKIEKLKSKESLQEAGKSEANTDLMGGSPKGEKRSVLQTINKFLDLSLFAHRGFLLYLSGNVVMFFGLFTPLVFLSNYGKSQHYSSEKSAFLLSILAFVDMVARPSMGLAANTKWIRPRIQYFFAASVVANGVCHLLAPLSTSYIGFCIYAGVFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVILIIAGIYLFIGMGINYRLVAKEQKAEEKQKQEEGKEDDTSTDVDEKPKELTKATESPQQNSSGDPAEEESPV
Protein: Na(+)/H(+) exchange regulatory cofactor NHE-RF4 (NHERF-4) (Intestinal and kidney-enriched PDZ protein) (Natrium-phosphate cotransporter IIa C-terminal-associated protein 2) (Na/Pi cotransporter C-terminal-associated protein 2) (NaPi-Cap2) (PDZ domain-containing protein 2) (PDZ domain-containing protein 3) (Sodium-hydrogen exchanger regulatory factor 4) (Q86UT5)
Organism: Homo sapiens (Human)
Function: Acts as a regulatory protein that associates with GUCY2C and negatively modulates its heat-stable enterotoxin-mediated activation. Stimulates SLC9A3 activity in the presence of elevated calcium ions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451, ECO:0000269|PubMed:22627094}; Peripheral membrane protein {ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451}. Cytoplasm {ECO:0000269|PubMed:19088451}. Note=Preferentially accumulates at the apical surface and ileal brush border of intestinal epithelial cells (PubMed:11950846, PubMed:19088451). {ECO:0000269|PubMed:11950846, ECO:0000269|PubMed:19088451}.
Interaction partners:
- Guanylyl cyclase C
- Cystic fibrosis transmembrane conductance regulator
- Sodium-dependent phosphate transport protein 2A
- Atrial natriuretic peptide receptor 3
Sequence:
MVTPSPPGNHSLSLEAPRLHTASDLLGNHSLGLPLITALVGSRDRRGRVFSPVPVPLPTNPTTQHPTRQKLPSTLSGHRVCQAHGEPVLGLCPLLPLFCCPPHPPDPWSLERPRFCLLSKEEGKSFGFHLQQELGRAGHVVCRVDPGTSAQRQGLQEGDRILAVNNDVVEHEDYAVVVRRIRASSPRVLLTVLARHAHDVARAQLGEDAHLCPTLGPGVRPRLCHIVKDEGGFGFSVTHGNQGPFWLVLSTGGAAERAGVPPGARLLEVNGVSVEKFTHNQLTRKLWQSGQQVTLLVAGPEVEEQCRQLGLPLAAPLAEGWALPTKPRCLHLEKGPQGFGFLLREEKGLDGRPGQFLWEVDPGLPAKKAGMQAGDRLVAVAGESVEGLGHEETVSRIQGQGSCVSLTVVDPEADRFFSMVRLSPLLFLENTEAPASPRGSSSASLVETEDPSLEDTSVPSVPLGSRQCFLYPGPGGSYGFRLSCVASGPRLFISQVTPGGSAARAGLQVGDVILEVNGYPVGGQNDLERLQQLPEAEPPLCLKLAARSLRGLEAWIPPGAAEDWALASDLL
Protein: Uncharacterized protein (Q3V0E6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKDIQLRRKEAKSILQAVCTLLNSGGGVVKAHIKNQNYSFTRDGMGLDLVNSLPGIMHLPHDYLDFMQHKDYFFVFVKPLKPNQKGPGITTLKTNLYRRINSISDEVKVANAVQLLKSRTDPEEKAESRPSSPGKIVCNETLNECLSLFNRDWLAYEETFCFTKSIHAEVKLTPKEKIFPKEKILELLPQTVSAFANTDGGFLFIGLDGKTQQIIGFEAEKSNLVLLESEIEKCIQQLPVTHFCGEKEKIKYTCKFIEVRKSGAVCAYVCALRVERFCCAVFAAEPESWHVEGGCVKRFTTEEWVKRQMDATAVMPGKVICCPEALYMKPFSQHEGYEHLVRTELGSLLKGTLVISKSWALDLGLQEKQEVIWDVLHISQGQSPDPVCLCPGR
Protein: Fatty-acid and retinol-binding protein 1 (Og-FAR-1) (Q8WT59)
Organism: Onchocerca gutturosa
Function: Binds retinol and different fatty acids.
Subcellular location: Secreted {ECO:0000269|PubMed:12106870}.
Interaction partners:
Sequence:
MYHQLILMALIGVIMANVVPFSMSNIPEEYKEFIPEEVKNFYKNLTQEDRQILRELASKHATFTNEDAALEALKNKSDKLYQKAVELRNFVKAKIDSLKPDAKTFVDEIIAKVRSLRPEDGQKLDMEKIKQAARDIIAKYEALNEETKEELKATFPNTTKIITNEKFKRIANSFLQKN
Protein: U7 snRNA-associated Sm-like protein LSm11 (Q8BUV6)
Organism: Mus musculus (Mouse)
Function: Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing. Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed. Required for cell cycle progression from G1 to S phases. Binds specifically to the Sm-binding site of U7 snRNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P83369}.
Interaction partners:
- U7 snRNA-associated Sm-like protein LSm10
- Histone RNA hairpin-binding protein
- Small nuclear ribonucleoprotein E
- Zinc finger protein 473 homolog
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein G
- 3'-5' exoribonuclease 1
- Heterogeneous nuclear ribonucleoprotein Q
Sequence:
MEEREWGARSARAGSPASPPSPRLDVSSYSFDPLLALYAPRLPPIPYPNAPCFNNVAEYESFLKGGRTGRGRARGTGEPASAGTSTGTSTGAGSSSRARRRAAPTPDPERIQRLRRLMVVKEDTDGTAGARRQGPGRSKKAPRNVLTRMPLHEGSPLGELHRCIREGVKVNVHIRTFKGLRGVCTGFLVAFDKFWNMALTDVDETYRKPVLGKAYERDSSLTLTRLFDRLKLQDSSKKEADSKSAVEDSTLSRYSQTSTWKVASVWGRGDTDRSSHRRSRSVPSSLQASAREESRSELSGRTTRTEGSSVGGTFSRATTLSRGQSRKKKRKPKVDYQQVFTRHINQIFIRGENVLLVHLAQ
Protein: 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.105) (Q57749)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the condensation of 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a precursor in the biosynthesis of 5,6,7,8-tetrahydromethanopterin (H4MPT). To a lesser extent, is able to condense beta-RFA-P with another arylamine, 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to form 7,8-dihydropterin-6-methyl-1-(4-aminophenyl)-1-deoxy-D-ribitol. Dephosphorylated beta-RFA-P is not a substrate.
Interaction partners:
- Uncharacterized protein MJ0448
- 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
- Uncharacterized protein MJ0107
- Uncharacterized protein MJ1477
Sequence:
MLMNIGKVDNIKIYTLAEDYAGYNSPFWSQHGLSFLIEVESNGIKKRILFDTATYAEPILFNMKLLNINPKSIDMIILSHNHFDHTGGLFGIMKEINKEIPIFAHPNIFKVSFATEPEFMLAGTLNKTLKEDIEKLGGRWVLSRDPIRLMPGIFTLGEIEDEEKINFEKKPTIGLYKLENGRVVLDNVEDEIGLAIVTEKGLIIVSGCSHPGIVSMVKKSIKISGINKVYAVIGGFHLIDADNERIVSTIKALKKLGVKKICTGHCTGFKAENMFMEEFKEDFERLHAGKIIKF
Protein: ISWI chromatin-remodeling complex ATPase ISW1 (EC 3.6.4.-) (P38144)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. They are involved in coordinating transcriptional repression, activation and elongation phases. The ISW1A complex represses gene expression at initiation through specific positioning of a promoter proximal dinucleosome. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:14562095}.
Interaction partners:
- ISWI one complex protein 3
- ISWI one complex protein 2
- Histone H3
- Histone H4
- ISWI one complex protein 4
- Imitation switch two complex protein 1
- ISWI chromatin-remodeling complex ATPase ISW2
- DNA polymerase epsilon subunit D
- Histone H2A.2
- Protein ESC8
Sequence:
MAYMLAIANFHFFKFYTRMRKKHENNSCNEKDKDENLFKIILAIFLQEKKKYDCISSGSIMTASEEYLENLKPFQVGLPPHDPESNKKRYLLKDANGKKFDLEGTTKRFEHLLSLSGLFKHFIESKAAKDPKFRQVLDVLEENKANGKGKGKHQDVRRRKTEHEEDAELLKEEDSDDDESIEFQFRESPAYVNGQLRPYQIQGVNWLVSLHKNKIAGILADEMGLGKTLQTISFLGYLRYIEKIPGPFLVIAPKSTLNNWLREINRWTPDVNAFILQGDKEERAELIQKKLLGCDFDVVIASYEIIIREKSPLKKINWEYIIIDEAHRIKNEESMLSQVLREFTSRNRLLITGTPLQNNLHELWALLNFLLPDIFSDAQDFDDWFSSESTEEDQDKIVKQLHTVLQPFLLRRIKSDVETSLLPKKELNLYVGMSSMQKKWYKKILEKDLDAVNGSNGSKESKTRLLNIMMQLRKCCNHPYLFDGAEPGPPYTTDEHLVYNAAKLQVLDKLLKKLKEEGSRVLIFSQMSRLLDILEDYCYFRNYEYCRIDGSTAHEDRIQAIDDYNAPDSKKFVFLLTTRAGGLGINLTSADVVVLYDSDWNPQADLQAMDRAHRIGQKKQVKVFRLVTDNSVEEKILERATQKLRLDQLVIQQNRTSLKKKENKADSKDALLSMIQHGAADVFKSGTSTGSAGTPEPGSGEKGDDIDLDELLLKSENKTKSLNAKYETLGLDDLQKFNQDSAYEWNGQDFKKKIQRDIISPLLLNPTKRERKENYSIDNYYKDVLNTGRSSTPSHPRMPKPHVFHSHQLQPPQLKVLYEKERMWTAKKTGYVPTMDDVKAAYGDISDEEEKKQKLELLKLSVNNSQPLTEEEEKMKADWESEGFTNWNKLEFRKFITVSGKYGRNSIQAIARELAPGKTLEEVRAYAKAFWSNIERIEDYEKYLKIIENEEEKIKRVKMQQEALRRKLSEYKNPFFDLKLKHPPSSNNKRTYSEEEDRFILLMLFKYGLDRDDVYELVRDEIRDCPLFELDFYFRSRTPVELARRGNTLLQCLEKEFNAGIVLDDATKDRMKKEDENGKRIREEFADQTANEKENVDGVESKKAKIEDTSNVGTEQLVAEKIPENETTH
Protein: Protein CBFA2T1 (Cyclin-D-related protein) (Eight twenty one protein) (Protein ETO) (Protein MTG8) (Zinc finger MYND domain-containing protein 2) (Q06455)
Organism: Homo sapiens (Human)
Function: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Can repress the expression of MMP7 in a ZBTB33-dependent manner. Can repress transactivation mediated by TCF12. Acts as a negative regulator of adipogenesis (By similarity). The AML1-MTG8/ETO fusion protein frequently found in leukemic cells is involved in leukemogenesis and contributes to hematopoietic stem/progenitor cell self-renewal.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440, ECO:0000269|PubMed:10973986}. Note=Colocalizes with ATN1 in discrete nuclear dots.
Interaction partners:
- Runt-related transcription factor 1
- Nuclear receptor corepressor 2
- Transcription factor 12
- Nuclear receptor corepressor 1
- CCAAT/enhancer-binding protein alpha
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- Transcription factor PU.1
- Protein CBFA2T2
- Zinc finger and BTB domain-containing protein 16
- Histone deacetylase 1
Sequence:
MISVKRNTWRALSLVIGDCRKKGNFEYCQDRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGAPSPPNGFSNGPSSSSSSSLANQQLPPACGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTISPGQRYSPNNGLSYQPNGLPHPTPPPPQHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEDLKKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPASGYVPEEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAAEDALAVINQQEDSSESCWNCGRKASETCSGCNTARYCGSFCQHKDWEKHHHICGQTLQAQQQGDTPAVSSSVTPNSGAGSPMDTPPAATPRSTTPGTPSTIETTPR
Protein: Glycogen synthase kinase-3 (EC 2.7.11.26) (Q9U2Q9)
Organism: Caenorhabditis elegans
Function: Phosphorylates oma-1, a regulator of the oocyte-to-embryo transition, enabling its degradation. Phosphorylates skn-1, preventing it from accumulating in nuclei and thus inhibiting phase II gene expression in the oxidative stress defense. Involved in mesendoderm specification and mitotic spindle orientation in EMS blastomeres. Thought to be a branch point in these processes as proteins downstream are not required. Negatively regulates Wnt signaling in vulval precursor cells and acts as a Wnt-independent repressor of med-1 and med-2 in the C lineage inhibiting mesoderm development. Required for normal lifespan and LiCl-induced lifespan extension.
Interaction partners:
- Beta-catenin/armadillo-related protein 1
- Beta-catenin-like protein hmp-2
- Axin-like protein pry-1
- cAMP-dependent protein kinase catalytic subunit
- Armadillo repeat-containing protein wrm-1
- Serine/threonine-protein kinase akt-1
- Serine/threonine-protein kinase akt-2
- DiSHevelled related
- Adenomatous polyposis coli protein-related protein 1
- DiSHevelled related
Sequence:
MNKQLLSCSLKSGKQVTMVVASVATDGVDQQVEISYYDQKVIGNGSFGVVFLAKLSTTNEMVAIKKVLQDKRFKNRELQIMRKLNHPNIVKLKYFFYSSGEKKDELYLNLILEYVPETVYRVARHYSKQRQQIPMIYVKLYMYQLLRSLAYIHSIGICHRDIKPQNLLIDPESGVLKLCDFGSAKYLVRNEPNVSYICSRYYRAPELIFGATNYTNSIDVWSAGTVMAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIQSMNPNYKEFKFPQIKAHPWNKVFRVHTPAEAIDLISKIIEYTPTSRPTPQAACQHAFFDELRNPDARLPSGRPLPTLEMDGPMGTGEVSTTSGDVAGPSA
Protein: N-alpha-acetyltransferase 20 (EC 2.3.1.254) (Methionine N-acetyltransferase) (N-acetyltransferase 5) (N-terminal acetyltransferase B complex catalytic subunit NAA20) (N-terminal acetyltransferase B complex catalytic subunit NAT5) (NatB complex subunit NAT5) (NatB catalytic subunit) (P61599)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18570629, ECO:0000269|PubMed:25732826}. Nucleus {ECO:0000269|PubMed:18570629, ECO:0000269|PubMed:25732826}.
Interaction partners:
- N-alpha-acetyltransferase 25, NatB auxiliary subunit
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- N-alpha-acetyltransferase 60
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
Sequence:
MTTLRAFTCDDLFRFNNINLDPLTETYGIPFYLQYLAHWPEYFIVAEAPGGELMGYIMGKAEGSVAREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNGEPDEDAYDMRKALSRDTEKKSIIPLPHPVRPEDIE
Protein: Keratin-associated protein 25-1 (Q3LHN0)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity).
Interaction partners:
- Keratin-associated protein 27-1
- Keratin-associated protein 24-1
- Keratin-associated protein 26-1
- Small cysteine and glycine repeat-containing protein 1
Sequence:
MHNRSQGFFFSSCHPQNHVSYGCQSPSFIFCRCQSLNFVSRTCYPLSYFSYGNQTIGSISNSFRSLNYVSHSFQPISFMHSSFQPACSDFVGWQSPFLRRTC
Protein: Origin recognition complex subunit 2 (Q60862)
Organism: Mus musculus (Mouse)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3 (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Origin recognition complex subunit 1
- Origin recognition complex subunit 6
- DNA replication licensing factor MCM2
- Origin recognition complex subunit 4
- Origin recognition complex subunit 5
- Cell division control protein 6 homolog
- Origin recognition complex subunit 3
- DNA replication licensing factor MCM5
- DNA replication factor Cdt1
- DNA replication licensing factor MCM3
Sequence:
MSTLQLKETKVPSVQFVGDDDVLSHILDREGGTKLKKEKAQLLVNPQKVIKKADCELEKSDLEVLEDQNYVKVLGRNIQESLGNGSAKDGRNKVYSFQQRKHPEEMTKLALELAKTSGKKDPLDSNDPEITKNIAQKSKGHSTSEKAPLVNNNKTEFLSTQPHNLRKRIIASRSHYDSESEYSASSSEDDEEATKDEEEDTNVARLSQKSQGQNRLLPAPVSKETLPKKKKRDKASDLVEEYFEAHSSSKVLTSDRTLQRLRRARVDQKTLHNLLRKFVPSFSAEIERLNQQHEKLFHKWMLQLHLGFNIVLYGLGSKRDLLEKFRTTMLQDSIHVVINGYFPGVSVKSILNSITEDVLSHVGTFQSVLDQRDWIINRFKEDSSLELFLLIHNLDSQMLRGDNSQQILGQLSSLHNVYLIASIDHLNAPLMWDHAKQSLYNWLWYETTTYSPYTEETSYENSLLVKQSGSLPLSSLIHVLRSLTPNARGIFRLLMKFQLDNQDSPSYIGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGTDGVEYLLIPVDSGILADFLEKEEEEA
Protein: HMG-box transcription factor 1 (C9J8V6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVWEVKTNQMPNAVQKLLLVMDKRASGMNDSLELLQCNENLPSSPGYNSCDEHMELDDLPELQAVQSDPTQSGMYQLSSDVSHQEYPRSSWNQNTSDIPETTYRENEV
Protein: M-phase inducer phosphatase (EC 3.1.3.48) (Mitosis initiation protein MIH1) (Mitotic inducer homolog) (P23748)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Terminates the cell cycle delay. Reverses the CDC28 phosphorylation catalyzed by SWE1.
Interaction partners:
- Cyclin-dependent kinase 1
- Mitosis inhibitor protein kinase SWE1
- Origin recognition complex subunit 3
- Origin recognition complex subunit 6
- Origin recognition complex subunit 2
- Origin recognition complex subunit 5
- G2/mitotic-specific cyclin-2
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Probable serine/threonine-protein kinase HSL1
- Serine/threonine-protein kinase CHK1
Sequence:
MNNIFHGTEDECANEDVLSFQKISLKSPFGKKKNIFRNVQTFFKSKSKHSNVDDDLINKENLAFDKSPLLTNHRSKEIDGPSPNIKQLGHRDELDENENENDDIVLSMHFASQTLQSPTRNSSRRSLTNNRDNDLLSRIKYPGSPQRSSSFSRSRSLSRKPSMNSSSNSSRRVQRQDGKIPRSSRKSSQKFSNITQNTLNFTSASSSPLAPNSVGVKCFESCLAKTQIPYYYDDRNSNDFFPRISPETLKNILQNNMCESFYNSCRIIDCRFEYEYTGGHIINSVNIHSRDELEYEFIHKVLHSDTSNNNTLPTLLIIHCEFSSHRGPSLASHLRNCDRIINQDHYPKLFYPDILILDGGYKAVFDNFPELCYPRQYVGMNSQENLLNCEQEMDKFRRESKRFATKNNSFRKLASPSNPNFFYRDSHQSSTTMASSALSFRFEPPPKLSLNHRRVSSGSSLNSSESTGDENFFPILSKSSMSSNSNLSTSHMLLMDGLDTPSYFSFEDERGNHQQVSGDEEQDGDFTFVGSDREDLPRPARRSLFPSLETEDKK
Protein: 60S ribosomal export protein NMD3 (Q9SI58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364108}. Nucleus {ECO:0000256|RuleBase:RU364108}.
Interaction partners:
- Expressed protein
- Probable ribosome biogenesis protein RLP24
- GTPase LSG1-2
- GTPase LSG1-1
- Eukaryotic translation initiation factor 6-2
- Nucleolar GTP-binding protein 1
- Nucleolar GTP-binding protein 1
- Cytoplasmic 60S subunit biogenesis factor REI1 homolog 2
- Ribosome assembly factor mrt4
- Large ribosomal subunit protein uL18y
Sequence:
MSVMDESGMFNVQQTIGSVLCCKCGVPMAPNAANMCVNCLRSEVDITEGLQKSIQIFYCPECTCYLQPPKTWIKCQWESKELLTFCIKRLKNLNKVKLKNAEFVWTEPHSKRIKVKLTVQAEVLNGAVLEQSYPVEYTVRDNLCESCSRFQANPDQWVASIQLRQHVSHRRTFFYLEQLILRHDAASRAIRIQQVDQGIDFFFGNKSHANSFVEFLRKVVPIEYRQDQQLVSHDVKSSLYNYKYTYSVKICPVCREDLVCLPSKVASGLGNLGPLVVCTKVSDNITLLDPRTLRCAFLDARQYWRSGFRSALTSRQLVKYFVFDVEPPVGEATVGGQKYALSYVQIARESDIGKMFYVQTHLGHILKPGDQALGYDIYGANVNDNEMEKYRLSVKNGLPEAILIKKCYEEQRERKQKKSRNWKLKSLPMEMDDSRGRVDPEKTDKEYEEFLRDLEENPELRFNISLYRDKDYQASETASMTDGEGAPSVPIEELLADLDLSFEEEDDDDEDDMAAE