wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase HEL2 (EC 2.3.2.27) (Histone E3 ligase 2) (RING-type E3 ubiquitin transferase HEL2) (Q05580)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- RQC trigger complex helicase SLH1
- E3 ubiquitin-protein ligase listerin
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Ribosome quality control complex subunit 2
- RQC trigger complex subunit CUE3
- Ribosome quality control complex subunit 1
- RQC trigger complex subunit RQT4
- Small ribosomal subunit protein eS10A
- Ubiquitin-conjugating enzyme E2 4
Sequence:
MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENELCVICARKLTYVSLTPCHHKTCHICGFRQRALYNKKSCLICRTENEEVMFTDRIDGDISDKYNFCEKNEKYGINFTSEEVATETLNLLKFFCPLSKDEQVCDFGSFKKYNEHLKSEHNRMICLICATHKHAFPCELEIFTQNQLRNHQTKGNSEGFKGHPMCAFCSGKRFYSDDELYIHMRNQHEKCHICDKMNPASPQYFKDYNQLFDHFKHSHYVCTVQTCLDNKFVVFKDELELQAHILQEHGNILKGKPKFFQSELSTFISAPSRVIRERDDYDLPSISSLPGSSSGSRTDVRSASSPEESRLRLAERAKYYLENSKEDFNKFSSYNEDYSKGRLSAEKLLESYKLLFTKPNADVYLLIHNLAETFPKNSSKYNNLNAIYEQREQTLARQTSLPSLSSDSSLSMSIGRGHWGGTNDGGSAGAALGVRNIKNLPTLKSPSASYDPFATTVKKNTLRPVQNIKRTTPQSVSYRTSTNTVAFSPTYLESKKGSSSTSLNNSKDKLKSLNLPQLPPPKPKVQIPGLNRPQIADPKQWGKKSSTQDTNVHDNLRELNTTSGGNKKKGKQKQLLFHIGV
Protein: Stretchin-MLCK (Q9GV81)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
IPTTRTYTSLLVLPAIRGNSSSSSLAARSCILTRPEDCTALIGGHVRLSVRYEPFPGTKVIWYKACHPIVDSSNVTIRTTSQQSTLYITDISADDSGKYTVEVMNDYGVEAAAASVAVEGPPEPPSAQPSVSLGPDRVAVAWCGPPYDGGCMITGFIIEMQTIGDENCDEDSWQQVTRVVDSLAYTVKNLQPERQYRFRVRAENIHGRSAPGQASELVQITNTPQRSTSSDASDRFGQATVSVQSGGDFKSRFEIIEELGKGRFGIVYKVQERCQPEQLLAAKVIKCIKSQDRQKVLEEISIMRALQHPKLLQLAASFESPREIVMVMEYITGGELFERVVADDFTLTEMDCILFLRQVCDGVAYMHGQSVVHLDLKPENIMCHTRTSHQIKIIDFGLAQRLDTKAPVRVLFGTPEFIPPEIISYEPIGFQSDMWSVGVICYVLLSGLSPFMGDTDVETFSNITRADYDYDDEAFDCVSQEAKDFISQLLVHRKEDRLTAQQCLESKWLSQRPDDSLSNNKICTDKLKKFIIRRKWQQRSREGAVEAHPVYPAKASHPRCVPCPALRCLSDPLRRRG
Protein: Poly(3-hydroxyalkanoate) polymerase subunit PhaE (PHA polymerase) (PHB synthase subunit PhaE) (Poly(3-hydroxybutyrate) polymerase subunit PhaE) (PHB polymerase) (Poly(hydroxyalkanoic acid) synthase subunit PhaE) (PHA synthase) (Polyhydroxyalkanoic acid synthase subunit PhaE) (P73389)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: When expressed in E.coli with Synechocystis PhaC and C.necator PhaA and PhaB, confers the ability to synthesize up to 13% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source; all 4 genes are necessary for PHB production. Cell-free in vitro coexpression with PhaE gives a heterodimer able to polymerize 3-hydroxybutyrate-CoA. This subunit has no catalytic activity but enhances the activity of PhaC, the catalytic subunit (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P45372}.
Interaction partners:
- Poly
- Acetoacetyl-CoA reductase
- Acetyl-CoA acetyltransferase
- Slr0060 protein
- Sll0783 protein
Sequence:
MESTNKTWTELMTPLSQFWLESSSQAWKNWFDLMAKGGAGAMMGSAPQSFESLPQQFLQSQQFYGELLKLSFEAWQSLWPKLDNGSAPGAVQGYLKQLQTQIEQYTATTQALQGDMDGLWQCYIKEVQRFSQLWLSTWQSSVAPLGKLPTGDIHAWLDLNNLYGDALYNKNLSSFMRSPLLGPSREMNGKLLRAFDDWVKLSQAMADYQLLEADIQYRGFAALMEDLLARAKEDKPVKTWKEFQQRWAIAADQVFEEAFCEEKNLKVRGKFINALNRYRIQQQEILEAWLKMLNLPTRSEVDEIHQTIYQLRKEVKSLKKRLGETEANPG
Protein: PIG-P domain-containing protein (Q389W6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- phosphatidylinositol N-acetylglucosaminyltransferase
- PhosphatidylinositolN-acetylglucosaminyltransferase subunit c, putative
- Dolichol phosphate-mannose biosynthesis regulatory protein
- N-acetylglucosaminylphosphatidylinositol deacetylase
- GPI-GlcNAc transferase complex PIG-H component conserved domain-containing protein
- N-acetylglucosaminyltransferase, putative
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MPLRCTKPLGATPATPTAPPTGRKGHQVAINGFITWILVTMSLVVYFLWAFIPTSFLDMVLASYYPDKYWAVAIPAILVMTMVYYLTVHFLLMLYRTDPLTDGFCVAQTNGAVRHESIENLVDVEDGVPPITDIPVSVASRLLFQPWN
Protein: Cytoskeleton-associated protein 2 (Q3V1H1)
Organism: Mus musculus (Mouse)
Function: Possesses microtubule stabilizing properties. Involved in regulating aneuploidy, cell cycling, and cell death in a p53-dependent manner.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Contrary to the ectopically expressed protein, endogenous CKAP2 does not colocalize with microtubules in G1, S and early G2. At late G2 and prophase after separation of duplicated centrosomes, colocalizes with gamma-tubulin and centrosome-proximal microtubules. From prometaphase through anaphase B, colocalizes with mitotic spindle poles and spindle microtubules. During cytokinesis, absent from midbody microtubules (By similarity). {ECO:0000250}.
Interaction partners:
- Centromere protein F
- Kinesin-like protein KIF20A
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Abnormal spindle-like microcephaly-associated protein homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Dual specificity protein kinase TTK
- DNA topoisomerase 2-alpha
- Kinesin-like protein KIF2C
- Kinetochore protein Nuf2
- Cyclin-dependent kinase 1
Sequence:
MAESRKRFLGRAARNPLPVTRDLQLPPTRRDQPAFREQRKQKLKEYLLIRKTVFPYKQENQISRDQKMITSEDRVQEGKKVVKLKTEVADKENIESTVEKNCIPLKAGEVTSSEIHNSKDNVQAVQLLSTRDDLPGQTVTLDPACHHKDNKKMQMTAEKPKQDSNVSKKRVLGYYHGQIVQSKINSFRKLPSVKGESLTTTKKLPTTVSKAMKAQSEPANTVSVKASTTAAATKFADAKPVSTASKDTLVRPPIRSLHSSSHGAAKQGLSRPLANVTVRKGMLDKESHRSEPVVSVVKAGSSQAPSRSIASKDAARTDSSNTRLMVKPKDTDQRRYTIAGASVHRSAQLKDTTAERKAQMTEWRTGKGKGLKRPPHSVVTQAEPKGQSENPVGSFWTTMAEEDEQRLFTEKVNKTISECLNLINEGCPKEEILATLNDLIHNIPDAKKLVKYWICLVRIEPITSPIENIISIYEKAILAGAQPIEEMRHIIIDILTTKSQEKVNLGENIEEAHATKEPIQEVNADANVGSGKPGEENEHHGKVEVYEDDQDNKIKDPDLTTPDSKTEAGCIIRYNVSSTPRLQSMKKMQHDKNSTLKELKFLTPVRRSRRIQDKTSRLPAMLKDHDPSVSSLEQLSELGGDAFVCRPNAALCPLFFETDVAEEE
Protein: E3 ubiquitin-protein ligase TRAF7 (EC 2.3.2.-) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRAF7) (TNF receptor-associated factor 7) (Q922B6)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces apoptosis when overexpressed. Plays a role in the phosphorylation of MAPK1 and/or MAPK3, probably via its interaction with MAP3K3.
Subcellular location: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q6Q0C0}. Cytoplasm {ECO:0000269|PubMed:16162816}. Nucleus {ECO:0000269|PubMed:16162816}. Note=Colocalizes with MAP3K3 to vesicle-like structures throughout the cytoplasm. {ECO:0000250|UniProtKB:Q6Q0C0}.
Interaction partners:
- AN1-type zinc finger protein 4
- Ubiquitin-ribosomal protein eL40 fusion protein
- Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6
- Merlin
- S-phase kinase-associated protein 1
Sequence:
MPPINTPRRSDSAISVRSLHSESSMSLRSTFSLPEEEEEPEPLVFAEQPSVKLCCQLCCSVFKDPVITTCGHTFCRRCALKSEKCPVDNAKLTVVVNNIAVAEQIGELFIHCRHGCHAAGTGKPGVFEVDPRGCPFTIKLSARKDHESSCDYRPVRCPNNPSCPPLLKMNLEAHLKECEHIKCPHSKYGCTFIGNQDTYETHLETCRFEGLKEFLQQTDDRFHEMHVALAQKDQEIAFLRSMLGKLSEKIDQLEKSLELKFDVLDENQSKLSEDLMEFRRDASMLNDELSHINARLNMGILGSYDPQQIFKCKGTFVGHQGPVWCLCVYSMGDLLFSGSSDKTIKVWDTCTTYKCQKTLEGHDGIVLALCIQGCKLYSGSADCTIIVWDIQNLQKVNTIRAHDNPVCTLVSSHNMLFSGSLKAIKVWDIVGTELKLKKELTGLNHWVRALVAAQSYLYSGSYQTIKIWDIRTLDCIHVLQTSGGSVYSIAVTNHHIVCGTYENLIHVWDIESKEQVRTLTGHVGTVYALAVISTPDQTKVFSASYDRSLRVWSMDNMICTQTLLRHQGSVTALAVSRGRLFSGAVDSTVKVWTC
Protein: Epsin-3 (P47160)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12483220}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12483220}; Peripheral membrane protein {ECO:0000269|PubMed:12483220}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:12483220}; Peripheral membrane protein {ECO:0000269|PubMed:12483220}. Note=Associates with the trans Golgi network (TGN) and endosomal clathrin coats.
Interaction partners:
- dTTP/UTP pyrophosphatase
- AP-1 complex subunit gamma-1
- Clathrin heavy chain
- Clathrin light chain
- t-SNARE VTI1
- Epsin-5
- ADP-ribosylation factor-binding protein GGA2
- AP-1 complex subunit sigma-1
- AP-2 complex subunit alpha
- AP-1 complex subunit beta-1
Sequence:
MSLEDTLANMSLYDAKKYFRKAQNVVFNYTEMEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKAGSEWRQIYKALQLLDYLIKHGSERFIDDTRNSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKIRAERKKARETAKKYKGVAGGSASADGSLNSKAGFTSTKVHGISVSADFDSDNEDNEDGSFSQNGYNDNASRATSTPGQGKQEPEDFVDFFSSESSKPSKELIQEDEKKADEEEDDDDEFSEFQSAVPVTNPANSFNLLNTSPIEGMPATTSSMPFYNSSTTDQGKITPAIAEPKKVDPFSSLFSTAKASAEAPSAPKASQAKAAASNPVSNSTTALSTDQDDDDEFGEMHGGAVQQEQNTNNNHTSSKEIDLLSF
Protein: N-acetylneuraminate lyase (AcNeu lyase) (NAL) (Neu5Ac lyase) (EC 4.1.3.3) (N-acetylneuraminate pyruvate-lyase) (N-acetylneuraminic acid aldolase) (NALase) (Sialate lyase) (Sialic acid aldolase) (Sialic acid lyase) (P0A6L4)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Experiments show the true substrate is aceneuramate (linearized Neu5Ac), which forms spontaneously at alkaline pH. Linear aceneuramate can be provided by NanQ.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- N-acetylmannosamine kinase
- Sialic acid transporter NanT
- Putative N-acetylmannosamine-6-phosphate 2-epimerase
- N-acetylneuraminate anomerase NanQ
- HTH-type transcriptional repressor NanR
- N-acetylneuraminic acid outer membrane channel protein NanC
- N-acetylneuraminate epimerase
- 4-hydroxy-tetrahydrodipicolinate reductase
- Glucosamine-6-phosphate deaminase
- Probable 9-O-acetyl-N-acetylneuraminic acid deacetylase
Sequence:
MATNLRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVSTAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGALKQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVIDLLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQERG
Protein: Vascular endothelial zinc finger 1 (J3QSH4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAHEASHHQQQAAQNSLLPLLSSAVEPPDQKPLLPIPITQKPQGAPETLKDAIGIKKEKPKTSFVCTYCSKAFRDSYHLRRHESCHTGIKLVSRPKKTPTTVVPLISTIAGDSSRTSLVSTIAGILSTVTTSSSGTNPSSSASTTAMPVTQSVKKPSKPVKKNHACEMCGKAFRDVYHLNRHKLSHSDEKPFECPICNQRFKRKDRMTYHVRSHEGGITKPYTCSVCGKGFSRPDHLSCHVKHVHSTERPFKCQTCTAAFATKDRLRTHMVRHEGKVSCNICGKLLSAAYITSHLKTHGQSQSINCNTCKQGISKTCMSEETSNQKQQQQQQQQQQQQQQQQQQHVTSWPGKQVETLRLWEEAVKARKKEAANLCQTSTAATTPVTLTTPFSITSSVSSGTMSNPVTVAAAMSMRSPVNVSSAVNITSPMNIGHPVTITSPLSMTSPLTLTTPVNLPTPVTAPVNIAHPVTITSPMNLPTPMTLAAPLNIAMRPVESMPFLPQALPTSPPW
Protein: GEO11103p1 (HDC18488) (IP18534p) (InaF-C) (Q6IIF2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- InaF-A
- GEO10024p1
- InaF-D
- Uncharacterized protein, isoform B
Sequence:
MSTASESARAGLGNAASMANLAKIVNLIESNVKSEDVEVLEEAVRGSTGTGSGSSVRLASSSAPRRSACATSYVPKSPQLEEIVFAEPTYTERFARYFVIVIYLCGLCSLGFFLSIYHIFFWDSRMPPVYKGQKKGPAFG
Protein: ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein) (Q62848)
Organism: Rattus norvegicus (Rat)
Function: GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine.
Subcellular location: Cytoplasm. Golgi apparatus. Note=Associates with the Golgi complex.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor 1
- ADP-ribosylation factor GTPase-activating protein 2
- ADP-ribosylation factor GTPase-activating protein 3
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- ADP-ribosylation factor 5
- Coatomer subunit beta
- Coatomer subunit beta'
- ADP-ribosylation factor 4
- ADP-ribosylation factor 3
Sequence:
MASPRTRKVLKEVRAQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGLGVHLSFVRSVTMDKWKDIELEKMKAGGNAKFREFLEAQDDYEPSWSLQDKYSSRAAALFRDKVATLAEGKEWSLESSPAQNWTPPQPKTLQFTAHRPAGQPQNVTTSGDKAFEDWLNDDLGSYQGAQENRYVGFGNTVPPQKREDDFLNSAMSSLYSGWSSFTTGASKFASAAKEGATKFGSQASQKASELGHSLNENVLKPAQEKVKEGRIFDDVSSGVSQLASKVQGVGSKGWRDVTTFFSGKAEDTSDRPLEGHSYQNSSGDNSQNSTIDQSFWETFGSAEPPKAKSPSSDSWTCADASTGRRSSDSWDIWGSGSASNNKNSNSDGWESWEGASGEGRAKATKKAAPSTAADEGWDNQNW
Protein: Heat shock transcription factor (HSTF) (Heat shock factor protein) (HSF) (Q5KMX8)
Organism: Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Function: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription. Together with its coregulator SSA1, activates expression of laccase LAC1 during glucose starvation.
Subcellular location: Nucleus {ECO:0000269|PubMed:17040492}.
Interaction partners:
- Wos2 protein
- Elongation factor 1-alpha
- Glycogen synthase kinase 3, putative
- Chaperone, putative
- Expressed protein
- Chaperone regulator, putative
- non-chaperonin molecular chaperone ATPase
- Heat shock protein HSP60, putative
- Transcriptional coregulator SSA1
- Transcriptional coregulator SSA1
Sequence:
MTTNLYAIAGPSKPTTPTSTPSPRSEPPSPLKSLTSLPTNPLNSHGTSTPNTLTNQLSSTGIGISKPGLSVDENGEVMKVPAFLNKLYTMVSDPEVDDLIYWGESGDSFFVPNAELFGRELLPRWFKHSNFSSFVRQLNMYGFHKVPHLQSGALKNETPIELWEFANPYFKRGQPQLLTKVTRKNNRPSNSGVGPSSSVGGSGAGGGMSTRSASAAAASGSASGQIQQAISQGHEAGNHSTSGKYLITDGTTPGSVPPSHTSAGPLIAPQTLDLSAINSGIAAIRQTQASIATDLRKLQASNEALWRQAYETQEKQRKHEETIDLIVSFLERLFGTEGEGLKGLKEAMRRGVGVRRDRDGREGRDSRDSRFAEDDDGGQKKRRRVGIDRMIEGGTGDGTGEHGEIESPTSDDRLVEIGSNSEYSIPSVKRTSSSSHPISLGQLGSSRFTALPSEDPSPSASGPGSTSYEGLHTTQTNARGAGADVNVTDPTLGMNHLSPLSDTDPLLPSSSNALAPYSSHLPFPSSNSNQSNSFNPSNPSSAWASNPSQPLLSPTSAAAAAHAYNLDPSLLQTTIGSLLQSPAAAQMFLNSLSASAQGQALASHSHPHNPSPLNPNPNGNASTSASASAHGMNTGGMGTGSGTKDVDPTLALFSPLPSHSSLTSQSNDLLKSYSDALTVGEGVDNLQESIDSLVRSMGLDLPNGGSSVGVDVGDGAGVGTETGEGDGEFNVDEFLQGLAKEGEEEGEREVEGDGGVSSSGAGAGAENGRKEDVIAQSGLKSES
Protein: Counting factor 50 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase 1) (GH family 25 lysozyme 1) (Q556R7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Cell-counting factor that limits the maximum size of the multicellular structure during aggregation. Has a very low lysozyme activity.
Subcellular location: Secreted.
Interaction partners:
- Neutral alpha-glucosidase AB
Sequence:
MNKMNNIFLIISSIILSIVIFVSGECAIDFSSEISVGISDSQWSCLASNNQRVIIQVWSGGGQYNSNISSVVSAAEQAGFDNIDLYAFLCSECDGNYPASSAIQSLVSSLKSDGINFNMLWIDVEQCDGCWGAESDNADYVQEAVETAQGLGVLVGVYSSEGEWPQTVGNLSTLSQYPLWYAHYDDNPSFSDTAFYEFGGWTSPAMKQYIGNTNQCGVSVDLDFYGSGSGCSTSSGSASGSASGSASGSASGSNSGSSNSGSSNSGSSNSGSNSGSSNSGSGNSGSSNSGSASGSGTGSGSSI
Protein: WIZ zinc finger (M0QXA7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVAMDLGSPSLPKKSLPVPGALEQVASRLSSKVAAEVPHGSKQELQDLKAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAHLGLPPGLAKKSSSLKEVVAGAPRPGLLSLAKPLDAPAVNKAIKSPPGFSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTLDSDGGRELDCQLCGAWFETRKGLSSHARAHLRHLGVSDPDAKGSPIDVLHGLIRRDGVQIRLPPRRGALAHPGRPPPTSAALSLLPPPPPAKKAKLKAAGMASPWGKQDLSAAAAAGIFWASDVEPSPLNLSSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQIRVEIKREMLPGALHGELHPSEGPWGAPREDMTPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDTNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEESQAPQAQTAAAEAP
Protein: Early endosome antigen 1 (A0A8I6AIH5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDSHQSSLLLRGYYTNNKNLVYVTDIGFNALLCSLLELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKGLRAAAEQKATHLTEELSKQTTVIQDLKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHANSEATINQLRSELAKGPQEVAVYVQEIQKLKGSVNELTQKSQTLMEKLQKKDLDYTHLEEKHNEEALSRKNTQAALHQRDLDCQQLQARLTASEGSLQRIQGELREKGEAAQKLKEELREVETKHQHLKVEFKQLQQQREEKEQHGLQLQGEVSQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLMEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKVSAQLDQVTAKFQEKQEHCTQLESHLKDYKEKHLSLEQKAEDLEGQIKKLEANNLEVKASREQAVQSLQQQRQLSTDLELRNAELRKQLQEQKEVVSHTKLDLQNKSEALENIKQTLTKKEEEKVVLKQEFEKLSQDSEAQHKELSDRMQAAITELMVMTAQKDALLAELSTTKGKLSKVSDSLQTSRSEFEKESQKGKAAVLDLEKACKELKHQLQQQTESALKEQSELKKSLEKERETSQQLMIELNSVKGEVTQAQNTLKQKEKEEQQLQGNINQLKQATEQKKKQMEALQGELKNVTSQKAQLESKLQQQAAQAAQELAVEKGKLSALQSTYDKCQADLQQLQSDLYGKESELLATRQDLKCVEEKLALAQEDLISNRNQIGNQNKSIQELQAAKAALEQDLAKKEEVLKEQSKALQDAQREKSVKEKELVTEKSKLAEMEEIKCRQEKEIAKLKEELKSHKQESIKEVTNLKDAKQLLIQQKLELQGKVDSLKAALEQEKERQQLMREQMRKEEEKRKEEFSEKEAKLHSEIKEKEAGVKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACFNDLQG
Protein: Carboxylesterase type B domain-containing protein (G5EED7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MERIYLLLLLFLPRIRSYDVRSVTTSWGMVRGEVVSPEGDDLPPVAQYLGIPYGVAPTGQYRFNMAISAAKWTHMPKDARKVSPVCIQTDMPELSETKRFRAFKHTSAQRFDFNHRLLPHLKKQSEDCLYMNIYVPERLEISRDNYLPVMVIVHGEEYGWGTGNAFNGTTLAAYGHIIVVTLNYRLGVFGFLGRCESSSCSGNSGISDLVSALTMLNVILPSFGGDSKSVTLAGWGSGASLVSLLMASPLTQPGRRLFRRAILLDGSALSPWAISQNPQQYFMQLAEELACAPKNRTSSFNDNVDTIVRCMQVHSSENITKAVLKIDVPTFLSGFAPIVDGQLIPNKPQVSFSTQYGSLFREIDLLVGISSNPSHHMISNEDLKVGISKEKRMRIFRSLVRNLYDFHREEILASIINEYTDWENPRDHPKSIRNGVLNALSDVLYTAPLIETLRSHSADEVRKEANTFMFAFAHETRSWSQEQPNSGIRGSLSGDIVPYIFGYPLAQGDSEERLYSGFNTDDKGISKVMMHYVSNFVKSGDPSKPNPMSKNFPMGDVFHSTAWPQFDQPNREAYLEITDRPRVKNYYRNAQVGFWNNFIPQLHKNGKETEPVGEEHHLLSDHFRKDSYFGKTRHFSSYANLPFPPPPMPPSPPPELTTKPKPSESPTTLQTTTESEKAAAGSFTGKALGGVIFIGCGFLIMNVCLLIAVRREWGKKRRNEKKFQLQYQTYNSNHGGGAEQYNSLNSPLSLMPPPPPPLNGVHDDIFDHRVPHLRNGSTVHGTLPRHSFQEQAREPLLSASHKNSTSMRPAGISPTCPRHGRAALALQNSRGNSLTAAQAPTLEEIQV
Protein: Transducin beta like 3 (J3KNP2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
XAWQEGSVTRLWKAIHTAPVATMAFDPTSTLLATGGCDGAVRVWDIVRHYGTHHFRGSPGVVHLVAFHPDPTRLLLFSSATDAAIRVWSLQDRSCLAVLTAHYSAVTSLAFSADGHTMLSSGRDKICIIWDLQSCQATRTVPVFESVEAAVLLPEEPVSQLGVKSPGLYFLTAGDQGTLRVWEAASGQCVYTQAQPPGPGQELTHCTLAHTAGVVLTATADHNLLLYEARSLRLQKQFAGYSEEVLDVRFLGPEDSHVVVASNSPCLKVFELQTSACQILHGHTDIVLALDVFRKGWLFASCAKDQSVRIWRMNKAGQVMLKESFLVTGSQDCTVKLWPLPKALLSKNTAPDNGPILLQAQTTQRCHDKDINSVAIAPNDKLLATGSQDRTAKLWALPQCQLLGVFSGHRRGLWCVQFSPMDQVLATASADGTIKLWALQDFSCLKTFEGHDASVLKVAFVSRGTQLLSSGSDGLVKLWTIKNNECVRTLDAHEDKVWGLHCSRLDDHALTGASDSRVILWKDVTEAEQAEEQARQEEQVVRQQELDNLLHEKRYLRALGLAISLDRPHTVLTVIQAIRRDPEACEKLEATMLRLRRDQKEALLRFCVTWNTNSRHCHEAQAVLGVLLRREAPEELLAYEGVRAALEALLPYTERHFQRLSRTLQAAAFLDFLWHNMKLPVPAAAPTPWETHKGALP
Protein: Ethylene-responsive transcription factor RAP2-3 (Cadmium-induced protein AS30) (Ethylene response factor 72) (ERF72) (Ethylene-responsive element binding protein) (AtEBP) (Protein RELATED TO APETALA2 3) (Related to AP2 3) (P42736)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus. Cytoplasm. Cell membrane.
Interaction partners:
- Transcription factor TGA4
- Acyl-CoA-binding domain-containing protein 4
- Acyl-CoA-binding domain-containing protein 2
- Basic leucine zipper 8
- Acyl-CoA-binding domain-containing protein 1
- Protein ETHYLENE INSENSITIVE 3
Sequence:
MCGGAIISDYAPLVTKAKGRKLTAEELWSELDASAADDFWGFYSTSKLHPTNQVNVKEEAVKKEQATEPGKRRKRKNVYRGIRKRPWGKWAAEIRDPRKGVRVWLGTFNTAEEAAMAYDVAAKQIRGDKAKLNFPDLHHPPPPNYTPPPSSPRSTDQPPAKKVCVVSQSESELSQPSFPVECIGFGNGDEFQNLSYGFEPDYDLKQQISSLESFLELDGNTAEQPSQLDESVSEVDMWMLDDVIASYE
Protein: Superkiller complex protein 8 (Ski8) (Meiotic recombination REC14 protein homolog) (WD repeat-containing protein 61) [Cleaved into: Superkiller complex protein 8, N-terminally processed (WD repeat-containing protein 61, N-terminally processed)] (Q9ERF3)
Organism: Mus musculus (Mouse)
Function: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1C (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9GZS3}. Cytoplasm {ECO:0000250|UniProtKB:Q9GZS3}.
Interaction partners:
- RNA polymerase-associated protein CTR9 homolog
- RNA polymerase-associated protein LEO1
- Superkiller complex protein 3
- Parafibromin
- RNA polymerase-associated protein RTF1 homolog
- Superkiller complex protein 2
- RNA polymerase II-associated factor 1 homolog
- Transcription elongation factor SPT5
- Meiotic recombination protein SPO11
- Elongin-A
Sequence:
MTNQYSILFKQEQAHDDAIWSVAWETNKKENIETVVTGSLDDLVKVWKWRDERLELQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQMKSIDAGPVDAWTLAFSPDSQYLATGTHMGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCIHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHVYDCPI