wanglab/gogpt-training-data huggingface dataset:
Protein: Thioredoxin-like fold domain-containing protein MRL7, chloroplastic (Protein EARLY CHLOROPLAST BIOGENESIS 1) (AtECB1) (Protein MESOPHYLL-CELL RNAI LIBRARY LINE 7) (AtMRL7) (Protein REGULATOR OF CHLOROPLAST BIOGENESIS) (Protein SUPPRESSOR OF VARIEGATION 4) (F4JLC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an essential role in early steps of chloroplast development. Involved in the regulation of plastid gene expression. May positively regulate plastid-encoded RNA polymerase (PEP) activity through binding to FSD3 and CITRX/TRXZ. Involved in redox-mediated regulation of chloroplast development. Possesses disulfide reductase activity in vitro. Required for the proper function of the plastid transcriptional machinery and protein accumulation in thylakoid membranes. May function as molecular chaperone to ensure proper organization of the nucleoids in chloroplasts. May mediate some aspect of thylakoid structure or function that controls non-photochemical quenching (NPQ). Participates in the early light signaling events of photobody biogenesis in chloroplasts. May mediate the degradation of two repressors of chloroplast biogenesis, PIF1 and PIF3 in nucleus.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21220584, ECO:0000269|PubMed:24111559}. Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:21515910, ECO:0000269|PubMed:24132784, ECO:0000269|PubMed:31201314}. Nucleus {ECO:0000269|PubMed:31201314}. Note=Associated with punctuate structures in chloroplasts. {ECO:0000269|PubMed:21220584}.
Interaction partners:
- Protein PEP-RELATED DEVELOPMENT ARRESTED 1, chloroplastic
- Thioredoxin-like protein CITRX, chloroplastic
- Superoxide dismutase 3, chloroplastic
- Fructokinase-like 1, chloroplastic
- Fructokinase-like 2, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 7
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic
- DNA binding protein
- AT3g18370/MYF24_8
- Pentatricopeptide repeat-containing protein At4g25270
Sequence:
MSFFAVACSAPRSSMLLTGLNSSFSDMHRSPLFVFPVTISSRSVKRFAAVSSDSVLDPESKNQTRSRRKNKEAVTPIAETENNEKFPTKVPRKSKRGRRSEADAVEDYVRSSLERTFSTIKEQNPEVFENKEKANFIKDRGVDEEEEEEEEMVVEEEDPDWPVDTDVGWGIKASEYFDTHPIKNVVGDDGSEIDWEGEIDDSWVKEINCLEWESFAFHPSPLVVLVFERYKRASDNWKTLKELEKAIKVYWDAKDRLPPRAVKIDLNIETDLAYALKAKECPQILFLRGNRILYREKDFRTADELVHMIAHFYYKAKRPSCVDKANVTPYC
Protein: Ubiquitin-like-conjugating enzyme ATG10 (EC 2.3.2.-) (Autophagy-related protein 10) (APG10-like) (mAPG10) (Q8R1P4)
Organism: Mus musculus (Mouse)
Function: E2-like enzyme involved in autophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for autophagy. Likely serves as an ATG5-recognition molecule. Not involved in ATG12 conjugation to ATG3. Plays a role in adenovirus-mediated cell lysis.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like protein ATG12
- Autophagy protein 5
- Immunity-related GTPase family M protein 1
- Autophagy-related protein 13
- Autophagy-related protein 16-1
- Ubiquitin-like-conjugating enzyme ATG3
- RB1-inducible coiled-coil protein 1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Microtubule-associated protein 1 light chain 3 beta
Sequence:
MEDEFFGEKSFQHYCAEFIRHSQQIGDGWEWRTAKECSDGYMCKTQFRIKNEASTPHVGTPASVLTCLPTEENLELPMDDSEVTRPAAVAEVIKHEYHVLYSCSYQVPVLYFRASFLDGRPLALEDIWEGVHECYKPRLLQGPWDTITQQEHPILGQPFFVLHPCKTNEFMTAVLKNSQKINRNVNYITSWLSLVGPVVGLNLPLSYAKATSQSE
Protein: Aerobic respiration control protein ArcA (Dye resistance protein) (P0A9Q1)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system ArcB/ArcA. Represses a wide variety of aerobic enzymes under anaerobic conditions. Controls the resistance of E.coli to dyes; required for expression of the alkaline phosphatase and sex factor F genes; it may also be involved in the osmoregulation of envelope proteins. When activated by ArcB, it negatively regulates the expression of genes of aerobic function. Activates the transcription of the plfB operon by binding to its promoter.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Aerobic respiration control sensor protein ArcB
- Trehalose-6-phosphate synthase
- Sensor histidine kinase CpxA
- Sensor histidine kinase EnvZ
- Phosphate regulon sensor protein PhoR
Sequence:
MQTPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEYDINLVIMDINLPGKNGLLLARELREQANVALMFLTGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLLSRTMNLGTVSEERRSVESYKFNGWELDINSRSLIGPDGEQYKLPRSEFRAMLHFCENPGKIQSRAELLKKMTGRELKPHDRTVDVTIRRIRKHFESTPDTPEIIATIHGEGYRFCGDLED
Protein: N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) (Q8LTE6)
Organism: Bacillus phage Gamma
Interaction partners:
Sequence:
MEIQKKLVDPSKYGTKCPYTMKPKYITVHNTYNDAPAENEVSYMISNNNEVSFHIAVDDKKAIQGIPLERNAWACGDGNGSGNRQSISVEICYSKSGGDRYYKAEDNAVDVVRQLMSMYNIPIENVRTHQSWSGKYCPHRMLAEGRWGAFIQKVKNGNVATTSPTKQNIIQSGAFSPYETPDVMGALTSLKMTADFILQSDGLTYFISKPTSDAQLKAMKEYLDRKGWWYEVK
Protein: COP9 signalosome complex subunit 3 (SGN3) (Signalosome subunit 3) (JAB1-containing signalosome subunit 3) (Q9UNS2)
Organism: Homo sapiens (Human)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. 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. 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. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:9535219}.
Interaction partners:
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 7a
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 7b
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 9
- Cullin-2
Sequence:
MASALEQFVNSVRQLSAQGQMTQLCELINKSGELLAKNLSHLDTVLGALDVQEHSLGVLAVLFVKFSMPSVPDFETLFSQVQLFISTCNGEHIRYATDTFAGLCHQLTNALVERKQPLRGIGILKQAIDKMQMNTNQLTSIHADLCQLCLLAKCFKPALPYLDVDMMDICKENGAYDAKHFLCYYYYGGMIYTGLKNFERALYFYEQAITTPAMAVSHIMLESYKKYILVSLILLGKVQQLPKYTSQIVGRFIKPLSNAYHELAQVYSTNNPSELRNLVNKHSETFTRDNNMGLVKQCLSSLYKKNIQRLTKTFLTLSLQDMASRVQLSGPQEAEKYVLHMIEDGEIFASINQKDGMVSFHDNPEKYNNPAMLHNIDQEMLKCIELDERLKAMDQEITVNPQFVQKSMGSQEDDSGNKPSSYS
Protein: FI10506p (Methoprene-tolerant, isoform A) (Methoprene-tolerant, isoform B) (Q9VYW2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein cycle
- Germ cell-expressed bHLH-PAS, isoform C
- Spineless, isoform C
- Dysfusion, isoform D
- Ecdysone receptor
Sequence:
MAAPETGNTGSTGSAGSTGSGSGSGSGSGSSSDPANGREARNLAEKQRRDKLNASIQELATMVPHAAESSRRLDKTAVLRFATHGLRLQYVFGKSASRRRKKTGLKGTGMSASPVGDLPNPSLHLTDTLMQLLDCCFLTLTCSGQIVLVSTSVEQLLGHCQSDLYGQNLLQITHPDDQDLLRQQLIPRDIETLFYQHQHHQQQGHNPQQHSTSTSASTSGSDLEEEEMETEEHRLGRQQGEADDDEDHPYNRRTPSPRRMAHLATIDDRLRMDRRCFTVRLARASTRAEATRHYERVKIDGCFRRSDSSLTGGAAANYPIVSQLIRRSRNNNMLAAAAAVAAEAATVPPQHDAIAQAALHGISGNDIVLVAMARVLREERPPEETEGTVGLTIYRQPEPYQLEYHTRHLIDGSIIDCDQRIGLVAGYMKDEVRNLSPFCFMHLDDVRWVIVALRQMYDCNSDYGESCYRLLSRNGRFIYLHTKGFLEVDRGSNKVHSFLCVNTLLDEEAGRQKVQEMKEKFSTIIKAEMPTQSSSPDLPASQAPQQLERIVLYLIENLQKSVDSAETVGGQGMESLMDDGYSSPANTLTLEELAPSPTPALALVPPAPSSVKSSISKSVSVVNVTAARKFQQEHQKQRERDREQLKERTNSTQGVIRQLSSCLSEAETASCILSPASSLSASEAPDTPDPHSNTSPPPSLHTRPSVLHRTLTSTLR
Protein: Polychaetoid, isoform B (Q9VHK4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKFPDYVPNNMLVGDRTTWEYHTVAVTRVPGYGFGIAVSGGRDNPHFANGDPSIAVSDVLKGGPAEDRLQVNDRIISVNGVSLENVEYATAVQVLRDSGNTVQLVVKRRVPLNPINAAGAVQHQHSHSLSSVGLMANGSGGVAPTPITSLSQPNSLNSSLVQNASSGQPIKVTLTKGGKKDDYGVVLGCRLFVKEISSKAREQLNANGYSLQEGDIITRIHNTNCGDTMSLKEAKKIIDGCKERLNLVVLRDITNQTAVSQLNLNNSASHQASGNIYATHQPQVSGCSSSNNNLEDPYLPGGASYSSQNLYVQPPTRTSNGPNINGNGLNDEKSNLTPRGRSRGPIMDGVSLQQLDRPVTPTRGRSAAIDEPPRPPPPRGSSGGAAQEDFYSSRRQLYEERQSAEPRFISFQKEGSVGIRLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQYCKEEYDEVVTNQRGDSFHIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAEELATAQFNATKKEMNANESRGNFFRRRRSTHRRSKSLSRENWDDVVFSDSISKFPAYERVVLRHPGFVRPVVLFGPVSDLARERLAKDFPDKFSTPLQDDDKSAATSGKCRIVRLSNIRDVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLKTDSKHVIKQLRHGLPKAAHKSSKKLLEQCQKLERVWSHIFSTQIALSDEESWYRKLRDSIDLQQSGAVWMSESKPVESLSDDFLFPMTTSRLSYASSPESDLELSPGPSASLSLGNLPQLVKASSDPSIATNQDNLDRDRDIIGEGLPPPYTVPYDHAVPANPNRRQTMDSSKYSIYGTNVPPQQQQPGVGGDTAAVRPQSLYGINAPDLPPRIDRQSKPGDIPLNTSGSSSRNGTLGRSAQERLFGKAVVQDDVQAEYITRNALVGSGAAETLDRQQQQQQQTHASLERQARLNAQLKANGVGAGGGGASTYDSVSSYDSYNNTQMAMQNLGRLGPNAPDDLKSVPNANGRPLPPTGQSHEYGRTPHDHRSFGGPNDLNRQSSPGRPHYHDMNASRNIDPRNGTPQRPSNLGLESSPRKPLVETKTDYGKYSRNNSVTQADYTKLPKTAPHGVVPPPNVSNGQGQMNGSGTPSSNGSGPFKPVPPPKPKNYRPPVQSGGSSGSGGTTPWENGDSGSPRSPNGFYYPPTPSHHHYGQQATPGSPSNGHMQPPPPQQQQPTYGGSNGNYGQAPPPQSYPQANGYNGNGHHYNGGSGTGPYIAPHRGMPPPIGNLPPHTPERHALDLAGSREQRGSAFELYRKPQIGATAGHHHNMR
Protein: FI07649p (Neprilysin-like 15) (Q9VCU1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MASQPLGLLLGAILFSICAIDASVPHPLAANYSIDILRLAKAAHIKAYMGDEKEQACNNFYNYACANWPRLHPARKSKTRTNYLEELQELYIRKSADMLKSATRGAENSADRQLKYFYGSCRLQTNDTRSALNTLQNVTDFRGGWPEIRVASWYQYEYDWLQVVANLKRKLGVDIFIGLEVILDYKEEKMHRLKIGAPQFPMSRRHYLHPHFEGTREIYERSIENKLKLYFPEQSEHWRQEVASQVVQIEQQLAKGLPHNPALTLAQTTRQRTAAEMKTAYGSYVDVTRYLQLIFNDNLYMDLYETPEDYMSNLVDVIRETPKLQLANYTMWKALEALDIARVPASQRADIWCVQLAQQFFPHQLESLFHRNYNHMQMINELQSTWSDIKRVFREDLQASERLLWLTLETRQKAITKLEALKLHFRTHDDNKLIRQMHGLILNMDRFYPNLVSVLQWKTQRGLAKLMTEPVAEDEVHKLPHYEIQKNRIQVPITFLQARFFWDPAYPNGLKYATLGVLLARQMLHGFDGVGRRYDAYGYKNNWWDHTSESSYSRRTQCFQEQYAIFVEYKGKPVQDKDLLRRIVADNGALDIAYRAYQQWLKNAAETPVIYQRERLPLLDHDHNQIFYLGYAQLYCTDYPETVERFDELPEQLRVNTALSNSQQFANAYGCSREEKLNARFKCTLY
Protein: S phase cyclin A-associated protein in the ER (Scaper protein) (B2RXS3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMASFQRSNSHDKVRRIVAEEGRTARNLIAWSVPLESKDDDGKPKCQTGGKSKRTIQGTHKTTKQNTAVECKITSTTGEKHFDKSPTKTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDYYVRDFKALIDWIQLQEKLEKTDAQSRPTSLAWEVKKMSPGRHVIQSPSTDRMNVTSTARRSLNFGSLPGAVTAPCLAPTGVSWADKVKAHHTGSAPPEATPAQSCAPMTVQKTSRKNERKDAEGWETVQRGRPVRSRSTAVIPKVSLVTETLRSKDDSDKENICLLPEESIQKGKLEDRCSTVESLSKDSLLHSSDHPLSERTQFTVCILDDVKNSGSSQDSSVHTSEIPAIDSDAVCVAPQNTTALPTDRVPAETTGMVTEMTDPSDISNSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGSGSLSFCGVSLDWNDVLADYEARESWRQNTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKQCSLCNVLIASEVYLFSHIKGKKHQQAVRENSSIQGRELSDEEVEHLSLKKYVVDIVIESAAPPEPVKDGEERQKNKKKAKKIKARMNIRAKEYENLVETKNSGSESPYKAKLQRLTKDLVKQLQVQDSGSWVNNKASALDRTLGEIARILEKENVPDQISFQVAGGLTALENILQVVTPATNMNTVSRIPPKSLCNAINVYSLACNNCSENCTDVLFSNKITFLMDLLIHQLTVYVPDENNAVLGRNTNKQVFEGLTTGLLRAGAVVFSCLIANRPDGNSRPATPKISTQEMKNKPSQGDAFNSRVQDLISYVVNMGLIDRLHGCFLSVQGPVDENPKMATFLQHAAGFLRGMCMLCFAVTGRSSSIFDNNHQDPTGLTAALQATDLAGVLHMLYCILFHGTISDAGTSPKDSYTQNTIQVAIQSLRFFNSFAILDLSAFQSVVGAEGLSLAFRHMASSLLGHCSQVSCESLLHEVIVCVGYFTVNHPDNQVIVQSGRHPTVLQKLCQLPFQYFSDPRLIKVLFPSLITACHNNHQNKLILEQEMSCVLLATFIQDFAQTPGHVDNQSSSLKGKFQNPGNYLELANRFPQQAWEEARQFFLKKEKK
Protein: cGMP-specific 3',5'-cyclic phosphodiesterase alpha (PfPDE1) (PfPDEalpha) (EC 3.1.4.35) (Q8I5V4)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes.
Subcellular location: Membrane {ECO:0000305|PubMed:16038615, ECO:0000305|PubMed:18590734}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- cGMP-specific 3',5'-cyclic phosphodiesterase delta
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase beta
- AMP deaminase
- Adenylate kinase 2
- GTP:AMP phosphotransferase
- Adenylate kinase 1
- Guanylate kinase
- Guanylate cyclase beta
- Adenylosuccinate lyase
- Adenylate kinase isoenzyme 6 homolog
Sequence:
MMDTKVDQTIQPKFYVDKKLSKSFDNKLDEDIFNYPFKKESFLKSEKFSFEHTKDSLWKCIKEKAKKKSDMEYFNCVNNLCCKFICTIRKYVKYFLYLKDSSYEIYNINLYNNNNMNIINNKNITNNKNITNNINNSFSNDYINYNHNYNHLNNSSSSKHNNYNVNNIDEKNIKNDYNTYHNIYEQIFFKYNPSFYEYLMFTLMKKLIHYKNYIFNKTKKINNSYNNNDIKNIDGFLIFQNINFEEIFLNTFYSSFPFKLFLHSLYMIFICFIYFVVLYFMLLKKIYTHPFIFHLSVLKFLFDIIFFLSFILYPLFLRLKRIDKIIYSSYISSYIFVCVTFLYSFIIFKCSSYSVKMNSNTYQNNFVFQNMLFLLINIIYICIFCFLKNYMILYSFLYNCRFSIFCILFIFLYYYLFFSLDFYRIIHLPLDNFFFPFLCFLFFSFLFIFKIIMSLYYEYVYEKKYRILFVKKNNLIEKRITKRKNTNINNAYFTKYFSIDNTIPTSPIEDILNNFKHILETINIIEENPNHNLTTNIMKIKEKIKNCDNILRTKNINQVQIGKYRKFEKVYNIWCLDKMYLNYPLNQEETKSFLSNSLNRISFNSFSNMHSLLSSKFQEHYNDIYDWNGNIENIYKANTFISIGYKLLYPLGVLEANFDKEKLKKFLFRICSYYNDIPYHTSLHAAQVAHFSKSMLFMLDMNHKISAIDEFCLHISSLCHDTGHPGLNNYFLINSENNLALTYNDNSVLENYHCSLLFKTLKNPNYNIFEHYPYHIFISCKKNIIKAILSTDMKNHFEYISDFRTSKEFIDYDNLSNDQIWQIFCLILKASDIGHSTLEWNKHLEWTLKINEEFYLQGLLEKSLNIQNSFLCDINTMNKLALSQIDFLKHLCIPLFNELNYICKNNDVYTHCIQPIENNIERWESHKNDNQNLGLHEKYKEENLLSKLELIKFE
Protein: F24J8.11 protein (Q9LPK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Photosystem I reaction center subunit VI-2, chloroplastic
Sequence:
MVAHSLVPLSPAAHAARLSSPSPRSLPQAPPVVLAVPPINRRTILVGLGGALWSWNALAAKEEAMAAARRPPPPPPKEKKDPTVTGVQAKVLASKKRKEEMKASIAKLREKGKPVVEAKPSSSSSE
Protein: Ribosomal protein L10 (X1WI28)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGRRPARCYRYCKNKPYPKSRFCRGVPDAKIRIFDLGRKKAKVDEFPLCGHMVSDEYEQLSSEALEAARICANKYMVKSCGKDGFHIRVRLHPFHVIRINKMLSCAGADRLQTGMRGAFGKPQGTVARVHIGQVIMSIRTKLQNKEHVIEALRRAKFKFPGRQKIHISKKWGFTKFNADEFEDMVAEKRLIPDGCGVKYI
Protein: Protein CLP1 homolog (CLP-like protein 3) (Protein CLP-SIMILAR PROTEIN 3) (Q9SR06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation (By similarity). Functions in gametophyte, embryo and postembryotic development.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03035, ECO:0000269|PubMed:18971429}.
Interaction partners:
- 30-kDa cleavage and polyadenylation specificity factor 30
- Polyadenylation and cleavage factor homolog 5
- Polyadenylation and cleavage factor homolog 4
- Polyadenylation and cleavage factor homolog 1
- Cleavage and polyadenylation specificity factor subunit 2
- Pre-mRNA cleavage complex 2 Pcf11-like protein
- Cleavage stimulation factor subunit 77
- Cleavage stimulating factor 64
- Pre-mRNA cleavage factor Im 25 kDa subunit 2
- Cleavage and polyadenylation specificity factor subunit 3-I
Sequence:
MAYGGPSMNPPALSGAVPGSANLKQVKLERESELRIEVSEEPLRLRVVNGTAEIFGSELPPEIWRTFPPRMKFAVFTWYGATIEMDGVTETDYTADETPMVSYINVHAILDARRRFAKASTSNDPESSQGPRVIVVGPTDSGKSTLTKMLLSWAAKQGWRPTFVDLDVGQGSITIPGSIAAAPIEMPLDPVEGFPLDMALVYYYGHASPNMNVELYKALVKELAQVLEKQFVGNPESRAAGMVINTMGWIEGIGYELLLHAIDTFNASVVLVLGQEKLFSRLKDVLRSKSNVDVVKLHKSGGVVARVKEVRKRSRNFKIQEYFYGLSKELSPYANTSSFSDLQVFRIGGGPQAPKSALPAGSTSVSNPLRVTPVNIDDRDLLHSVLAVSYAEEPDQIISSNVSGFVYVTEVNVQKKKITYLAPSPGTLPSKLLVAGSLAWLESV
Protein: Choline kinase alpha (CK) (EC 2.7.1.32) (CHETK-alpha) (Ethanolamine kinase) (EK) (EC 2.7.1.82) (P35790)
Organism: Homo sapiens (Human)
Function: Plays a key role in phospholipid biosynthesis by catalyzing the phosphorylation of free choline to phosphocholine, the first step in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine, thereby contributing to phosphatidylethanolamine biosynthesis. Has higher activity with choline. May contribute to tumor cell growth.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:34077757}.; SUBCELLULAR LOCATION: [Isoform 1]: Lipid droplet {ECO:0000269|PubMed:34077757}. Note=Isoform 1 localizes to lipid droplets following phosphorylation by AMPK. {ECO:0000269|PubMed:34077757}.
Interaction partners:
- Choline-phosphate cytidylyltransferase B
- Choline-phosphate cytidylyltransferase A
- Ethanolamine-phosphate cytidylyltransferase
- Axin-1
- Glycogen synthase kinase-3 beta
- Glycerophosphocholine phosphodiesterase GPCPD1
- Choline O-acetyltransferase
- Ethanolamine-phosphate phospho-lyase
- Acetylcholinesterase
- Phosphoethanolamine/phosphocholine phosphatase
Sequence:
MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPPPPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV
Protein: Cadherin-15 (Cadherin-14) (Muscle cadherin) (M-cadherin) (P33146)
Organism: Mus musculus (Mouse)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. M-cadherin is part of the myogenic program and may provide a trigger for terminal muscle differentiation.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin beta-1
- Myogenin
- Myoblast determination protein 1
- Myogenic factor 5
- Junction plakoglobin
- Paired box protein Pax-7
- Cell adhesion molecule-related/down-regulated by oncogenes
- Catenin delta-1
- Myogenic factor 6
Sequence:
MGSALLLALGLLAQSLGLSWAVPEPKPSTLYPWRRASAPGRVRRAWVIPPISVSENHKRLPYPLVQIKSDKQQLGSVIYSIQGPGVDEEPRNVFSIDKFTGRVYLNATLDREKTDRFRLRAFALDLGGSTLEDPTDLEIVVVDQNDNRPAFLQDVFRGRILEGAIPGTFVTRAEATDADDPETDNAALRFSILEQGSPEFFSIDEHTGEIRTVQVGLDREVVAVYNLTLQVADMSGDGLTATASAIISIDDINDNAPEFTKDEFFMEAAEAVSGVDVGRLEVEDKDLPGSPNWVARFTILEGDPDGQFKIYTDPKTNEGVLSVVKPLDYESREQYELRVSVQNEAPLQAAAPRARRGQTRVSVWVQDTNEAPVFPENPLRTSIAEGAPPGTSVATFSARDPDTEQLQRISYSKDYDPEDWLQVDGATGRIQTQRVLSPASPFLKDGWYRAIILALDNAIPPSTATGTLSIEILEVNDHAPALALPPSGSLCSEPDQGPGLLLGATDEDLPPHGAPFHFQLNPRVPDLGRNWSVSQINVSHARLRLRHQVSEGLHRLSLLLQDSGEPPQQREQTLNVTVCRCGSDGTCLPGAAALRGGGVGVSLGALVIVLASTVVLLVLILLAALRTRFRGHSRGKSLLHGLQEDLRDNILNYDEQGGGEEDQDAYDINQLRHPVEPRATSRSLGRPPLRRDAPFSYVPQPHRVLPTSPSDIANFISDGLEAADSDPSVPPYDTALIYDYEGDGSVAGTLSSILSSLGDEDQDYDYLRDWGPRFARLADMYGHQ
Protein: Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (P06211)
Organism: Rattus norvegicus (Rat)
Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with ZDHHC7 and ZDHHC21 in the Golgi apparatus where most probably palmitoylation occurs. Associated with the plasma membrane when palmitoylated. {ECO:0000250}.
Interaction partners:
- Proto-oncogene tyrosine-protein kinase Src
- Nuclear receptor coactivator
- Nuclear receptor coactivator 3
- Nuclear receptor corepressor 1
- Transcription factor Jun
- Nuclear receptor coactivator 2
- Protein c-Fos
- Insulin-like growth factor 1 receptor
- Transcription factor Sp1
- Breast cancer type 1 susceptibility protein homolog
Sequence:
MTMTLHTKASGMALLHQIQGNELEPLNRPQLKMPMERALGEVYVDNSKPAVFNYPEGAAYEFNAAAAAAAAGASAPVYGQSSITYGPGSEAAAFGANSLGAFPQLNSVSPSPLMLLHPPPHVSPFLHPHGHQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSSEKGNMIMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGTSGDMRAANLWPSPLVIKHTKKNSPALSLTADQMVSALLDAEPPLIYSEYDPSRPFSEASMMGLLTNLADRELVHMINWAKRVPGFGDLNLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKINDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPASRMGVPPEEPSQSQLTTTSSTSAHSLQTYYIPPEAEGFPNTI
Protein: Centromere protein H (CENP-H) (Q9QYM8)
Organism: Mus musculus (Mouse)
Function: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10488063}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:10488063}. Note=Associates with active centromere-kinetochore complexes throughout the cell cycle. Colocalizes with inner kinetochore plate proteins CENPA and CENPC during both interphase and metaphase.
Interaction partners:
- Centromere protein M
- Centromere protein I
- Centromere protein K
- Centromere protein P
- Centromere protein O
- Centromere protein U
- Centromere protein N
- Centromere protein T
- Centromere protein Q
- Centromere protein W
Sequence:
MEEQPRERSEAGAEACEEKRGLSQAAEERIEDRISLLLRLRAQTKQQLLEYKSMIDTNEEKTPEQIMQEKQIEVKIEELENEIEDVKSNIEMKSLALSRMKLSVALRDNMENMGPENCVLTDDMKHILKLQKLIMKSQEESSELEKKLLDVRKKRLQLKQASRSKLLEIQIEKNKQKEDVDKMENSEMIKTMKKKLQTEIKITTVVQHTFQGLILASKTNWAEDPALRETVLQLEKDLNTL
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (F4J741)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFFSFRLLKVLVFHLQIRPCVLLCVSQRKLQNNIINVGVKIQNRFRVVCMGMLAPRKFLQKRRKMEVFKDAADETDQKRWRGLMLEIESTGSAVPVLRQYKTDGDQGLPRDLVLGTLVRFKQLKKWNLVSEILEWLRYQNWWNFSEIDFLMLITAYGKLGNFNGAERVLSVLSKMGSTPNVISYTALMESYGRGGKCNNAEAIFRRMQSSGPEPSAITYQIILKTFVEGDKFKEAEEVFETLLDEKKSPLKPDQKMYHMMIYMYKKAGNYEKARKVFSSMVGKGVPQSTVTYNSLMSFETSYKEVSKIYDQMQRSDIQPDVVSYALLIKAYGRARREEEALSVFEEMLDAGVRPTHKAYNILLDAFAISGMVEQAKTVFKSMRRDRIFPDLWSYTTMLSAYVNASDMEGAEKFFKRIKVDGFEPNIVTYGTLIKGYAKANDVEKMMEVYEKMRLSGIKANQTILTTIMDASGRCKNFGSALGWYKEMESCGVPPDQKAKNVLLSLASTQDELEEAKELTGIRNETATIIARVYGSDDDEEGVEDISSESSDDEDEGDDDDDDARETVLYDKPQEGSLGYGSLQTEELVGL