PHC1_HUMAN
ID PHC1_HUMAN Reviewed; 1004 AA.
AC P78364; D3DUV4; Q8WVM3; Q9BU63;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Polyhomeotic-like protein 1;
DE Short=hPH1;
DE AltName: Full=Early development regulatory protein 1;
GN Name=PHC1; Synonyms=EDR1, PH1;
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], SUBCELLULAR LOCATION, AND INTERACTION WITH BMI1
RP AND PHC2.
RX PubMed=9121482; DOI=10.1128/mcb.17.4.2326;
RA Gunster M.J., Satijn D.P.E., Hamer K.M., den Blaauwen J.L., de Bruijn D.,
RA Alkema M.J., van Lohuizen M., van Driel R., Otte A.P.;
RT "Identification and characterization of interactions between the vertebrate
RT polycomb-group protein BMI1 and human homologs of polyhomeotic.";
RL Mol. Cell. Biol. 17:2326-2335(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-693.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-1004, AND VARIANT ALA-693.
RC TISSUE=Lung, and Lymph;
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 INTERACTION WITH PHC2.
RX PubMed=9199346; DOI=10.1128/mcb.17.7.4105;
RA Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W.,
RA Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.;
RT "RING1 is associated with the polycomb group protein complex and acts as a
RT transcriptional repressor.";
RL Mol. Cell. Biol. 17:4105-4113(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A PRC1-LIKE
RP HPRC-H COMPLEX WITH BMI1; CBX2; CBX4; CBX8; PHC2; PHC3; RING1 AND RNF2.
RX PubMed=12167701; DOI=10.1128/mcb.22.17.6070-6078.2002;
RA Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
RA Kingston R.E.;
RT "The core of the polycomb repressive complex is compositionally and
RT functionally conserved in flies and humans.";
RL Mol. Cell. Biol. 22:6070-6078(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898 AND THR-922, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, 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 [12]
RP FUNCTION, AND VARIANT MCPH11 PHE-992.
RX PubMed=23418308; DOI=10.1093/hmg/ddt072;
RA Awad S., Al-Dosari M.S., Al-Yacoub N., Colak D., Salih M.A., Alkuraya F.S.,
RA Poizat C.;
RT "Mutation in PHC1 implicates chromatin remodeling in primary microcephaly
RT pathogenesis.";
RL Hum. Mol. Genet. 22:2200-2213(2013).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-763, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development. PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility.
CC Required for proper control of cellular levels of GMNN expression.
CC {ECO:0000269|PubMed:23418308}.
CC -!- SUBUNIT: Homodimer. Component of a PRC1-like complex (PubMed:12167701,
CC PubMed:19636380, PubMed:21282530). Interacts with RNF2 and CBX7 (By
CC similarity). Interacts with PHC2, PHC2 and BMI1 (By similarity).
CC {ECO:0000250|UniProtKB:Q64028, ECO:0000269|PubMed:12167701,
CC ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530}.
CC -!- INTERACTION:
CC P78364; P35226: BMI1; NbExp=6; IntAct=EBI-725403, EBI-2341576;
CC P78364; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-725403, EBI-8468186;
CC P78364; P35227: PCGF2; NbExp=11; IntAct=EBI-725403, EBI-2129767;
CC P78364; Q3KNV8-2: PCGF3; NbExp=5; IntAct=EBI-725403, EBI-12818023;
CC P78364; P78317: RNF4; NbExp=5; IntAct=EBI-725403, EBI-2340927;
CC P78364; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-725403, EBI-742426;
CC P78364; Q5VUG0: SFMBT2; NbExp=4; IntAct=EBI-725403, EBI-12025260;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530,
CC ECO:0000269|PubMed:9121482}.
CC -!- DISEASE: Microcephaly 11, primary, autosomal recessive (MCPH11)
CC [MIM:615414]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age-related
CC mean. Brain weight is markedly reduced and the cerebral cortex is
CC disproportionately small. {ECO:0000269|PubMed:23418308}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The hPRC-H complex purification reported by
CC PubMed:12167701 probably presents a mixture of different PRC1-like
CC complexes.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17748.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U89277; AAC51169.1; -; mRNA.
DR EMBL; AC006581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88600.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88601.1; -; Genomic_DNA.
DR EMBL; BC002871; AAH02871.2; -; mRNA.
DR EMBL; BC017748; AAH17748.1; ALT_INIT; mRNA.
DR CCDS; CCDS8597.1; -.
DR RefSeq; NP_004417.2; NM_004426.2.
DR PDB; 2L8E; NMR; -; A=783-828.
DR PDBsum; 2L8E; -.
DR AlphaFoldDB; P78364; -.
DR SMR; P78364; -.
DR BioGRID; 108233; 73.
DR CORUM; P78364; -.
DR DIP; DIP-44567N; -.
DR IntAct; P78364; 35.
DR MINT; P78364; -.
DR STRING; 9606.ENSP00000440674; -.
DR GlyGen; P78364; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P78364; -.
DR PhosphoSitePlus; P78364; -.
DR BioMuta; PHC1; -.
DR DMDM; 224471881; -.
DR EPD; P78364; -.
DR jPOST; P78364; -.
DR MassIVE; P78364; -.
DR MaxQB; P78364; -.
DR PaxDb; P78364; -.
DR PeptideAtlas; P78364; -.
DR PRIDE; P78364; -.
DR ProteomicsDB; 57594; -.
DR Antibodypedia; 1884; 207 antibodies from 28 providers.
DR DNASU; 1911; -.
DR Ensembl; ENST00000543824.5; ENSP00000440674.1; ENSG00000111752.11.
DR Ensembl; ENST00000544916.6; ENSP00000437659.1; ENSG00000111752.11.
DR GeneID; 1911; -.
DR KEGG; hsa:1911; -.
DR MANE-Select; ENST00000544916.6; ENSP00000437659.1; NM_004426.3; NP_004417.2.
DR UCSC; uc001qvd.4; human.
DR CTD; 1911; -.
DR DisGeNET; 1911; -.
DR GeneCards; PHC1; -.
DR HGNC; HGNC:3182; PHC1.
DR HPA; ENSG00000111752; Low tissue specificity.
DR MalaCards; PHC1; -.
DR MIM; 602978; gene.
DR MIM; 615414; phenotype.
DR neXtProt; NX_P78364; -.
DR OpenTargets; ENSG00000111752; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA27619; -.
DR VEuPathDB; HostDB:ENSG00000111752; -.
DR eggNOG; ENOG502QUTP; Eukaryota.
DR GeneTree; ENSGT00940000156612; -.
DR HOGENOM; CLU_012048_1_0_1; -.
DR InParanoid; P78364; -.
DR OMA; FMPGGTT; -.
DR OrthoDB; 298184at2759; -.
DR PhylomeDB; P78364; -.
DR TreeFam; TF331299; -.
DR PathwayCommons; P78364; -.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; P78364; -.
DR SIGNOR; P78364; -.
DR BioGRID-ORCS; 1911; 27 hits in 1079 CRISPR screens.
DR ChiTaRS; PHC1; human.
DR GeneWiki; PHC1; -.
DR GenomeRNAi; 1911; -.
DR Pharos; P78364; Tbio.
DR PRO; PR:P78364; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P78364; protein.
DR Bgee; ENSG00000111752; Expressed in right uterine tube and 178 other tissues.
DR ExpressionAtlas; P78364; baseline and differential.
DR Genevisible; P78364; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016574; P:histone ubiquitination; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Disease variant; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Primary microcephaly; Reference proteome; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1004
FT /note="Polyhomeotic-like protein 1"
FT /id="PRO_0000058375"
FT DOMAIN 940..1004
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 791..825
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 800
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 803
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 922
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 763
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 693
FT /note="T -> A (in dbSNP:rs1049925)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_054503"
FT VARIANT 992
FT /note="L -> F (in MCPH11; significant reduction in mutant
FT protein levels which is shown to result from proteasome-
FT mediated degradation; patient cells show increased
FT expression of GMNN and decreased interaction between the
FT protein and ubiquitinated H2AC17 compared to control cells;
FT dbSNP:rs587777036)"
FT /evidence="ECO:0000269|PubMed:23418308"
FT /id="VAR_070566"
FT CONFLICT 165..167
FT /note="LGR -> PGS (in Ref. 1; AAC51169)"
FT /evidence="ECO:0000305"
FT CONFLICT 568..569
FT /note="HL -> LK (in Ref. 1; AAC51169)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="S -> T (in Ref. 1; AAC51169)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="V -> G (in Ref. 1; AAC51169)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="L -> F (in Ref. 1; AAC51169)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="L -> F (in Ref. 1; AAC51169)"
FT /evidence="ECO:0000305"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:2L8E"
FT HELIX 789..794
FT /evidence="ECO:0007829|PDB:2L8E"
FT STRAND 796..799
FT /evidence="ECO:0007829|PDB:2L8E"
FT TURN 801..803
FT /evidence="ECO:0007829|PDB:2L8E"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:2L8E"
FT HELIX 809..811
FT /evidence="ECO:0007829|PDB:2L8E"
FT TURN 813..815
FT /evidence="ECO:0007829|PDB:2L8E"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:2L8E"
FT HELIX 821..827
FT /evidence="ECO:0007829|PDB:2L8E"
SQ SEQUENCE 1004 AA; 105534 MW; D53764F80931A938 CRC64;
METESEQNSN STNGSSSSGG SSRPQIAQMS LYERQAVQAL QALQRQPNAA QYFHQFMLQQ
QLSNAQLHSL AAVQQATIAA SRQASSPNTS TTQQQTTTTQ ASINLATTSA AQLISRSQSV
SSPSATTLTQ SVLLGNTTSP PLNQSQAQMY LRPQLGNLLQ VNRTLGRNVP LASQLILMPN
GAVAAVQQEV PSAQSPGVHA DADQVQNLAV RNQQASAQGP QMQGSTQKAI PPGASPVSSL
SQASSQALAV AQASSGATNQ SLNLSQAGGG SGNSIPGSMG PGGGGQAHGG LGQLPSSGMG
GGSCPRKGTG VVQPLPAAQT VTVSQGSQTE AESAAAKKAE ADGSGQQNVG MNLTRTATPA
PSQTLISSAT YTQIQPHSLI QQQQQIHLQQ KQVVIQQQIA IHHQQQFQHR QSQLLHTATH
LQLAQQQQQQ QQQQQQQQQP QATTLTAPQP PQVPPTQQVP PSQSQQQAQT LVVQPMLQSS
PLSLPPDAAP KPPIPIQSKP PVAPIKPPQL GAAKMSAAQQ PPPHIPVQVV GTRQPGTAQA
QALGLAQLAA AVPTSRGMPG TVQSGQAHLA SSPPSSQAPG ALQECPPTLA PGMTLAPVQG
TAHVVKGGAT TSSPVVAQVP AAFYMQSVHL PGKPQTLAVK RKADSEEERD DVSTLGSMLP
AKASPVAESP KVMDEKSSLG EKAESVANVN ANTPSSELVA LTPAPSVPPP TLAMVSRQMG
DSKPPQAIVK PQILTHIIEG FVIQEGAEPF PVGCSQLLKE SEKPLQTGLP TGLTENQSGG
PLGVDSPSAE LDKKANLLKC EYCGKYAPAE QFRGSKRFCS MTCAKRYNVS CSHQFRLKRK
KMKEFQEANY ARVRRRGPRR SSSDIARAKI QGKCHRGQED SSRGSDNSSY DEALSPTSPG
PLSVRAGHGE RDLGNPNTAP PTPELHGINP VFLSSNPSRW SVEEVYEFIA SLQGCQEIAE
EFRSQEIDGQ ALLLLKEEHL MSAMNIKLGP ALKICAKINV LKET
