PCGF6_HUMAN
ID PCGF6_HUMAN Reviewed; 350 AA.
AC Q9BYE7; A8K3R4; Q5SYD1; Q5SYD6; Q96ID9; Q96SJ1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Polycomb group RING finger protein 6;
DE AltName: Full=Mel18 and Bmi1-like RING finger;
DE AltName: Full=RING finger protein 134;
GN Name=PCGF6; Synonyms=MBLR, RNF134;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSCRIPTIONAL
RP REPRESSION, INTERACTION WITH BMI1; RING1 AND RNF2, PHOSPHORYLATION AT
RP SER-30, MUTAGENESIS OF SER-30; SER-57; SER-59 AND SER-69, VARIANT
RP PRO-PRO-23 INS, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=12167161; DOI=10.1046/j.1365-2443.2002.00565.x;
RA Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.;
RT "MBLR, a new RING finger protein resembling mammalian Polycomb gene
RT products, is regulated by cell cycle-dependent phosphorylation.";
RL Genes Cells 7:835-850(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PRO-PRO-23 INS.
RC TISSUE=Cervix, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH KDM5D, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17320162; DOI=10.1016/j.cell.2007.02.004;
RA Lee M.G., Norman J., Shilatifard A., Shiekhattar R.;
RT "Physical and functional association of a trimethyl H3K4 demethylase and
RT Ring6a/MBLR, a polycomb-like protein.";
RL Cell 128:877-887(2007).
RN [6]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX.
RX PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J.,
RA Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT "Several distinct polycomb complexes regulate and co-localize on the INK4a
RT tumor suppressor locus.";
RL PLoS ONE 4:E6380-E6380(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX4; CBX6; CBX7
RP AND CBX8, AND SUBCELLULAR LOCATION.
RX PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26151332; DOI=10.1038/ncomms8621;
RA Taherbhoy A.M., Huang O.W., Cochran A.G.;
RT "BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.";
RL Nat. Commun. 6:7621-7621(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-223 AND LYS-234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
RP STRUCTURE BY NMR OF 124-182.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain of the human polycomb group RING
RT finger protein 6.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: Transcriptional repressor (PubMed:12167161). May modulate the
CC levels of histone H3K4Me3 by activating KDM5D histone demethylase
CC (PubMed:17320162). Component of a Polycomb group (PcG) multiprotein
CC PRC1-like complex, a complex class required to maintain the
CC transcriptionally repressive state of many genes, including Hox genes,
CC throughout development. PcG PRC1 complex acts via chromatin remodeling
CC and modification of histones; it mediates monoubiquitination of histone
CC H2A 'Lys-119', rendering chromatin heritably changed in its
CC expressibility (PubMed:12167161). Within the PRC1-like complex,
CC regulates RNF2 ubiquitin ligase activity (PubMed:26151332).
CC {ECO:0000269|PubMed:12167161, ECO:0000269|PubMed:17320162,
CC ECO:0000269|PubMed:26151332}.
CC -!- SUBUNIT: Component of a PRC1-like complex (PubMed:19636380,
CC PubMed:26151332). Interacts with BMI1/PCGF4, RING1 and RNF2
CC (PubMed:12167161). Interacts with KDM5D (PubMed:17320162). Interacts
CC with CBX4, CBX6, CBX7 and CBX8 (PubMed:21282530).
CC {ECO:0000269|PubMed:12167161, ECO:0000269|PubMed:17320162,
CC ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530,
CC ECO:0000269|PubMed:26151332}.
CC -!- INTERACTION:
CC Q9BYE7; O00257-3: CBX4; NbExp=2; IntAct=EBI-1048026, EBI-4392727;
CC Q9BYE7; O95931: CBX7; NbExp=4; IntAct=EBI-1048026, EBI-3923843;
CC Q9BYE7; Q9HC52: CBX8; NbExp=4; IntAct=EBI-1048026, EBI-712912;
CC Q9BYE7; Q06587: RING1; NbExp=4; IntAct=EBI-1048026, EBI-752313;
CC Q9BYE7; Q99496: RNF2; NbExp=6; IntAct=EBI-1048026, EBI-722416;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12167161,
CC ECO:0000269|PubMed:21282530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BYE7-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9BYE7-3; Sequence=VSP_042007, VSP_042008;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated during mitosis. Phosphorylated on Ser-30 by CDK7 in
CC vitro. {ECO:0000269|PubMed:12167161}.
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DR EMBL; AB047006; BAB40779.1; -; mRNA.
DR EMBL; AK027885; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK290679; BAF83368.1; -; mRNA.
DR EMBL; AL591408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007602; AAH07602.1; -; mRNA.
DR EMBL; BC010235; AAH10235.1; -; mRNA.
DR CCDS; CCDS31275.1; -. [Q9BYE7-1]
DR CCDS; CCDS7546.1; -. [Q9BYE7-3]
DR RefSeq; NP_001011663.1; NM_001011663.1. [Q9BYE7-1]
DR RefSeq; NP_115530.2; NM_032154.3. [Q9BYE7-3]
DR PDB; 2DJB; NMR; -; A=124-182.
DR PDBsum; 2DJB; -.
DR AlphaFoldDB; Q9BYE7; -.
DR BMRB; Q9BYE7; -.
DR SMR; Q9BYE7; -.
DR BioGRID; 123896; 164.
DR CORUM; Q9BYE7; -.
DR DIP; DIP-50946N; -.
DR IntAct; Q9BYE7; 77.
DR MINT; Q9BYE7; -.
DR STRING; 9606.ENSP00000358862; -.
DR iPTMnet; Q9BYE7; -.
DR PhosphoSitePlus; Q9BYE7; -.
DR BioMuta; PCGF6; -.
DR DMDM; 116242703; -.
DR EPD; Q9BYE7; -.
DR jPOST; Q9BYE7; -.
DR MassIVE; Q9BYE7; -.
DR MaxQB; Q9BYE7; -.
DR PaxDb; Q9BYE7; -.
DR PeptideAtlas; Q9BYE7; -.
DR PRIDE; Q9BYE7; -.
DR ProteomicsDB; 79631; -. [Q9BYE7-1]
DR ProteomicsDB; 79632; -. [Q9BYE7-3]
DR Antibodypedia; 31521; 162 antibodies from 22 providers.
DR DNASU; 84108; -.
DR Ensembl; ENST00000337211.8; ENSP00000338845.4; ENSG00000156374.16. [Q9BYE7-3]
DR Ensembl; ENST00000369847.4; ENSP00000358862.3; ENSG00000156374.16. [Q9BYE7-1]
DR GeneID; 84108; -.
DR KEGG; hsa:84108; -.
DR MANE-Select; ENST00000369847.4; ENSP00000358862.3; NM_001011663.2; NP_001011663.1.
DR UCSC; uc001kwt.3; human. [Q9BYE7-1]
DR CTD; 84108; -.
DR DisGeNET; 84108; -.
DR GeneCards; PCGF6; -.
DR HGNC; HGNC:21156; PCGF6.
DR HPA; ENSG00000156374; Low tissue specificity.
DR MIM; 607816; gene.
DR neXtProt; NX_Q9BYE7; -.
DR OpenTargets; ENSG00000156374; -.
DR PharmGKB; PA134887110; -.
DR VEuPathDB; HostDB:ENSG00000156374; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000158034; -.
DR HOGENOM; CLU_046427_4_0_1; -.
DR InParanoid; Q9BYE7; -.
DR OMA; FSSNRCP; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; Q9BYE7; -.
DR TreeFam; TF324206; -.
DR PathwayCommons; Q9BYE7; -.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q9BYE7; -.
DR SIGNOR; Q9BYE7; -.
DR BioGRID-ORCS; 84108; 16 hits in 1112 CRISPR screens.
DR ChiTaRS; PCGF6; human.
DR EvolutionaryTrace; Q9BYE7; -.
DR GeneWiki; PCGF6; -.
DR GenomeRNAi; 84108; -.
DR Pharos; Q9BYE7; Tbio.
DR PRO; PR:Q9BYE7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BYE7; protein.
DR Bgee; ENSG00000156374; Expressed in ventricular zone and 98 other tissues.
DR ExpressionAtlas; Q9BYE7; baseline and differential.
DR Genevisible; Q9BYE7; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038037; PCGF6.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR10825:SF74; PTHR10825:SF74; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..350
FT /note="Polycomb group RING finger protein 6"
FT /id="PRO_0000055989"
FT ZN_FING 134..173
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 72..110
FT /evidence="ECO:0000255"
FT COMPBIAS 21..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12167161"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 186
FT /note="R -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042007"
FT VAR_SEQ 187..261
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042008"
FT VARIANT 23
FT /note="L -> LPP"
FT /evidence="ECO:0000269|PubMed:12167161,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054312"
FT MUTAGEN 30
FT /note="S->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:12167161"
FT MUTAGEN 57
FT /note="S->A: Does not abolish phosphorylation."
FT /evidence="ECO:0000269|PubMed:12167161"
FT MUTAGEN 59
FT /note="S->A: Does not abolish phosphorylation."
FT /evidence="ECO:0000269|PubMed:12167161"
FT MUTAGEN 69
FT /note="S->A: Does not abolish phosphorylation."
FT /evidence="ECO:0000269|PubMed:12167161"
FT CONFLICT 257
FT /note="L -> P (in Ref. 2; BAF83368)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="G -> S (in Ref. 4; AAH07602)"
FT /evidence="ECO:0000305"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2DJB"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2DJB"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2DJB"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:2DJB"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2DJB"
SQ SEQUENCE 350 AA; 39047 MW; 05977FE6F14972DE CRC64;
MEGVAVVTAG SVGAAKTEGA AALPPPPPVS PPALTPAPAA GEEGPAPLSE TGAPGCSGSR
PPELEPERSL GRFRGRFEDE DEELEEEEEL EEEEEEEEED MSHFSLRLEG GRQDSEDEEE
RLINLSELTP YILCSICKGY LIDATTITEC LHTFCKSCIV RHFYYSNRCP KCNIVVHQTQ
PLYNIRLDRQ LQDIVYKLVI NLEEREKKQM HDFYKERGLE VPKPAVPQPV PSSKGRSKKV
LESVFRIPPE LDMSLLLEFI GANEGTGHFK PLEKKFVRVS GEATIGHVEK FLRRKMGLDP
ACQVDIICGD HLLEQYQTLR EIRRAIGDAA MQDGLLVLHY GLVVSPLKIT
