ID   RFC2_HUMAN              Reviewed;         354 AA.
AC   P35250; B5BU07; D3DXG3; P32846; Q9BU93;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   27-MAR-2024, entry version 224.
DE   RecName: Full=Replication factor C subunit 2;
DE   AltName: Full=Activator 1 40 kDa subunit;
DE            Short=A1 40 kDa subunit;
DE   AltName: Full=Activator 1 subunit 2;
DE   AltName: Full=Replication factor C 40 kDa subunit;
DE            Short=RF-C 40 kDa subunit;
DE            Short=RFC40;
GN   Name=RFC2;
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), AND PROTEIN SEQUENCE OF 232-249.
RX   PubMed=1313560; DOI=10.1073/pnas.89.7.2516;
RA   Chen M., Pan Z.-Q., Hurwitz J.;
RT   "Sequence and expression in Escherichia coli of the 40-kDa subunit of
RT   activator 1 (replication factor C) of HeLa cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2516-2520(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Hurwitz J.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1), AND POSSIBLE INVOLVEMENT IN WBS.
RX   PubMed=11003705; DOI=10.1007/s003350010166;
RA   Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V.,
RA   Koop B.F.;
RT   "Comparative genomic sequence analysis of the Williams syndrome region
RT   (LIMK1-RFC2) of human chromosome 7q11.23.";
RL   Mamm. Genome 11:890-898(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-232.
RG   NIEHS SNPs program;
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA   Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA   Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA   Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA   Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA   Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA   Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in vitro-
RT   expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
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   [9]
RP   INTERACTION WITH PRKAR1A.
RX   PubMed=15655353;
RA   Gupte R.S., Weng Y., Liu L., Lee M.Y.;
RT   "The second subunit of the replication factor C complex (RFC40) and the
RT   regulatory subunit (RIalpha) of protein kinase A form a protein complex
RT   promoting cell survival.";
RL   Cell Cycle 4:323-329(2005).
RN   [10]
RP   INTERACTION WITH DDX11.
RX   PubMed=18499658; DOI=10.1074/jbc.m802696200;
RA   Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S.,
RA   Hurwitz J.;
RT   "Studies with the human cohesin establishment factor, ChlR1. Association of
RT   ChlR1 with Ctf18-RFC and Fen1.";
RL   J. Biol. Chem. 283:20925-20936(2008).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163 AND LYS-304, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, 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).
CC   -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC       delta and epsilon requires the action of the accessory proteins
CC       proliferating cell nuclear antigen (PCNA) and activator 1. This subunit
CC       binds ATP (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC       form a complex either with RFC1 or with RAD17. The former interacts
CC       with PCNA in the presence of ATP, while the latter has ATPase activity
CC       but is not stimulated by PCNA. RFC2 also interacts with PRKAR1A; the
CC       complex may be involved in cell survival (PubMed:15655353). Interacts
CC       with DDX11 (PubMed:18499658). {ECO:0000269|PubMed:15655353,
CC       ECO:0000269|PubMed:18499658}.
CC   -!- INTERACTION:
CC       P35250; P10644: PRKAR1A; NbExp=7; IntAct=EBI-476409, EBI-476431;
CC       P35250; P35251: RFC1; NbExp=4; IntAct=EBI-476409, EBI-476616;
CC       P35250; P35249: RFC4; NbExp=8; IntAct=EBI-476409, EBI-476655;
CC       P35250-2; O14964: HGS; NbExp=3; IntAct=EBI-12936957, EBI-740220;
CC       P35250-2; P25786: PSMA1; NbExp=3; IntAct=EBI-12936957, EBI-359352;
CC       P35250-2; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-12936957, EBI-2510804;
CC       P35250-2; Q15915: ZIC1; NbExp=3; IntAct=EBI-12936957, EBI-11963196;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P35250-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35250-2; Sequence=VSP_005660;
CC   -!- DISEASE: Note=RFC2 is located in the Williams-Beuren syndrome (WBS)
CC       critical region. WBS results from a hemizygous deletion of several
CC       genes on chromosome 7q11.23, thought to arise as a consequence of
CC       unequal crossing over between highly homologous low-copy repeat
CC       sequences flanking the deleted region (PubMed:11003705).
CC       {ECO:0000269|PubMed:11003705}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/rfc2/";
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DR   EMBL; M87338; AAB09786.1; -; mRNA.
DR   EMBL; AF045555; AAC04860.1; -; Genomic_DNA.
DR   EMBL; AF483622; AAL82503.1; -; Genomic_DNA.
DR   EMBL; AC005081; AAP22334.1; -; Genomic_DNA.
DR   EMBL; AB451243; BAG70057.1; -; mRNA.
DR   EMBL; CH471200; EAW69607.1; -; Genomic_DNA.
DR   EMBL; CH471200; EAW69608.1; -; Genomic_DNA.
DR   EMBL; BC002813; AAH02813.1; -; mRNA.
DR   CCDS; CCDS5567.1; -. [P35250-2]
DR   CCDS; CCDS5568.1; -. [P35250-1]
DR   PIR; A42700; A42700.
DR   RefSeq; NP_001265720.1; NM_001278791.1.
DR   RefSeq; NP_001265721.1; NM_001278792.1.
DR   RefSeq; NP_001265722.1; NM_001278793.1.
DR   RefSeq; NP_002905.2; NM_002914.4. [P35250-2]
DR   RefSeq; NP_852136.1; NM_181471.2. [P35250-1]
DR   PDB; 6VVO; EM; 3.40 A; B=1-354.
DR   PDB; 7Z6H; EM; 3.59 A; F=1-354.
DR   PDBsum; 6VVO; -.
DR   PDBsum; 7Z6H; -.
DR   AlphaFoldDB; P35250; -.
DR   EMDB; EMD-14527; -.
DR   EMDB; EMD-21405; -.
DR   SMR; P35250; -.
DR   BioGRID; 111914; 191.
DR   ComplexPortal; CPX-415; DNA replication factor C complex.
DR   ComplexPortal; CPX-7931; DNA replication factor C complex, RAD17 variant.
DR   CORUM; P35250; -.
DR   DIP; DIP-34367N; -.
DR   IntAct; P35250; 62.
DR   MINT; P35250; -.
DR   STRING; 9606.ENSP00000055077; -.
DR   GlyGen; P35250; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P35250; -.
DR   MetOSite; P35250; -.
DR   PhosphoSitePlus; P35250; -.
DR   SwissPalm; P35250; -.
DR   BioMuta; RFC2; -.
DR   DMDM; 2507300; -.
DR   EPD; P35250; -.
DR   jPOST; P35250; -.
DR   MassIVE; P35250; -.
DR   MaxQB; P35250; -.
DR   PaxDb; 9606-ENSP00000055077; -.
DR   PeptideAtlas; P35250; -.
DR   ProteomicsDB; 55014; -. [P35250-1]
DR   ProteomicsDB; 55015; -. [P35250-2]
DR   Pumba; P35250; -.
DR   Antibodypedia; 14601; 556 antibodies from 33 providers.
DR   DNASU; 5982; -.
DR   Ensembl; ENST00000055077.8; ENSP00000055077.3; ENSG00000049541.11. [P35250-1]
DR   Ensembl; ENST00000352131.7; ENSP00000275627.3; ENSG00000049541.11. [P35250-2]
DR   GeneID; 5982; -.
DR   KEGG; hsa:5982; -.
DR   MANE-Select; ENST00000055077.8; ENSP00000055077.3; NM_181471.3; NP_852136.1.
DR   UCSC; uc003uaj.5; human. [P35250-1]
DR   AGR; HGNC:9970; -.
DR   CTD; 5982; -.
DR   DisGeNET; 5982; -.
DR   GeneCards; RFC2; -.
DR   HGNC; HGNC:9970; RFC2.
DR   HPA; ENSG00000049541; Low tissue specificity.
DR   MalaCards; RFC2; -.
DR   MIM; 194050; phenotype.
DR   MIM; 600404; gene.
DR   neXtProt; NX_P35250; -.
DR   OpenTargets; ENSG00000049541; -.
DR   Orphanet; 904; Williams syndrome.
DR   PharmGKB; PA34339; -.
DR   VEuPathDB; HostDB:ENSG00000049541; -.
DR   eggNOG; KOG0991; Eukaryota.
DR   GeneTree; ENSGT00550000075050; -.
DR   HOGENOM; CLU_042324_0_1_1; -.
DR   InParanoid; P35250; -.
DR   OMA; SCNYSSQ; -.
DR   OrthoDB; 275853at2759; -.
DR   PhylomeDB; P35250; -.
DR   TreeFam; TF300585; -.
DR   BRENDA; 3.6.4.B8; 2681.
DR   PathwayCommons; P35250; -.
DR   Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR   Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR   Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR   Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR   Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR   Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR   Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR   Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR   Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-HSA-69091; Polymerase switching.
DR   Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR   Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR   SignaLink; P35250; -.
DR   SIGNOR; P35250; -.
DR   BioGRID-ORCS; 5982; 735 hits in 1167 CRISPR screens.
DR   ChiTaRS; RFC2; human.
DR   GeneWiki; RFC2; -.
DR   GenomeRNAi; 5982; -.
DR   Pharos; P35250; Tbio.
DR   PRO; PR:P35250; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P35250; Protein.
DR   Bgee; ENSG00000049541; Expressed in ventricular zone and 154 other cell types or tissues.
DR   ExpressionAtlas; P35250; baseline and differential.
DR   GO; GO:0031390; C:Ctf18 RFC-like complex; IDA:UniProtKB.
DR   GO; GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR   GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18140; HLD_clamp_RFC; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   InterPro; IPR047854; RFC_lid.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   PANTHER; PTHR11669:SF5; REPLICATION FACTOR C SUBUNIT 2; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR   Genevisible; P35250; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Direct protein sequencing; DNA replication; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Williams-Beuren syndrome.
FT   CHAIN           1..354
FT                   /note="Replication factor C subunit 2"
FT                   /id="PRO_0000121766"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76..83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         163
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         304
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         111..144
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_005660"
FT   VARIANT         232
FT                   /note="A -> V (in dbSNP:rs3135684)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_023126"
FT   CONFLICT        244
FT                   /note="G -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           54..66
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           82..94
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   STRAND          136..142
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           148..160
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   TURN            161..164
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   STRAND          165..173
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           179..182
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   STRAND          185..189
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           195..209
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           215..225
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           229..242
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   STRAND          244..246
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           248..254
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           260..271
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           275..287
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           292..304
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           310..328
FT                   /evidence="ECO:0007829|PDB:6VVO"
FT   HELIX           334..347
FT                   /evidence="ECO:0007829|PDB:6VVO"
SQ   SEQUENCE   354 AA;  39157 MW;  B50AC8EEF89F64A9 CRC64;
     MEVEAVCGGA GEVEAQDSDP APAFSKAPGS AGHYELPWVE KYRPVKLNEI VGNEDTVSRL
     EVFAREGNVP NIIIAGPPGT GKTTSILCLA RALLGPALKD AMLELNASND RGIDVVRNKI
     KMFAQQKVTL PKGRHKIIIL DEADSMTDGA QQALRRTMEI YSKTTRFALA CNASDKIIEP
     IQSRCAVLRY TKLTDAQILT RLMNVIEKER VPYTDDGLEA IIFTAQGDMR QALNNLQSTF
     SGFGFINSEN VFKVCDEPHP LLVKEMIQHC VNANIDEAYK ILAHLWHLGY SPEDIIGNIF
     RVCKTFQMAE YLKLEFIKEI GYTHMKIAEG VNSLLQMAGL LARLCQKTMA PVAS
//