GenomeNet

Database: UniProt
Entry: CSR2B_HUMAN
LinkDB: CSR2B_HUMAN
Original site: CSR2B_HUMAN 
ID   CSR2B_HUMAN             Reviewed;         782 AA.
AC   Q9H8E8; A2A2I5; Q96GW6; Q96IH3; Q9HBF0; Q9UIY5;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   24-JAN-2024, entry version 186.
DE   RecName: Full=Cysteine-rich protein 2-binding protein;
DE            Short=CSRP2-binding protein;
DE   AltName: Full=ADA2A-containing complex subunit 2;
DE            Short=ATAC2;
DE   AltName: Full=CRP2-binding partner;
DE            Short=CRP2BP;
DE   AltName: Full=Lysine acetyltransferase 14 {ECO:0000312|HGNC:HGNC:15904};
GN   Name=KAT14 {ECO:0000312|HGNC:HGNC:15904}; Synonyms=CSRP2BP;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-400.
RC   TISSUE=Placenta;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   GLY-400.
RC   TISSUE=Eye, and 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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 546-782, AND INTERACTION WITH CSRP2.
RC   TISSUE=Kidney;
RX   PubMed=10924333; DOI=10.1006/bbrc.2000.3187;
RA   Weiskirchen R., Gressner A.M.;
RT   "The cysteine- and glycine-rich LIM domain protein CRP2 specifically
RT   interacts with a novel human protein.";
RL   Biochem. Biophys. Res. Commun. 274:655-663(2000).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX   PubMed=19103755; DOI=10.1128/mcb.01599-08;
RA   Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA   Lill J.R., Zha J.;
RT   "The double-histone-acetyltransferase complex ATAC is essential for
RT   mammalian development.";
RL   Mol. Cell. Biol. 29:1176-1188(2009).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-292, AND IDENTIFICATION BY MASS
RP   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-285 AND SER-416, AND
RP   IDENTIFICATION BY 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).
CC   -!- FUNCTION: Component of the ATAC complex, a complex with histone
CC       acetyltransferase activity on histones H3 and H4. May function as a
CC       scaffold for the ATAC complex to promote ATAC complex stability. Has
CC       also weak histone acetyltransferase activity toward histone H4.
CC       Required for the normal progression through G1 and G2/M phases of the
CC       cell cycle. {ECO:0000269|PubMed:19103755}.
CC   -!- SUBUNIT: Interacts with the LIM 1 domain of CSRP2. Component of the
CC       ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L,
CC       TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it
CC       probably interacts directly with KAT2A, MBIP and WDR5.
CC       {ECO:0000269|PubMed:10924333, ECO:0000269|PubMed:19103755}.
CC   -!- INTERACTION:
CC       Q9H8E8; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-750907, EBI-739624;
CC       Q9H8E8; Q7L190: DPPA4; NbExp=3; IntAct=EBI-750907, EBI-710457;
CC       Q9H8E8; Q9NS73: MBIP; NbExp=6; IntAct=EBI-750907, EBI-741953;
CC       Q9H8E8; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-750907, EBI-10182361;
CC       Q9H8E8; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-750907, EBI-748601;
CC       Q9H8E8; P14373: TRIM27; NbExp=6; IntAct=EBI-750907, EBI-719493;
CC       Q9H8E8; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-750907, EBI-2130429;
CC       Q9H8E8; P08048: ZFY; NbExp=3; IntAct=EBI-750907, EBI-12239601;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H8E8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H8E8-2; Sequence=VSP_000070;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, lung,
CC       placenta, brain, liver, pancreas and kidney. High expression in
CC       skeletal muscle and heart. Lower expression in lung.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC       {ECO:0000305}.
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DR   EMBL; AK023759; BAB14669.1; -; mRNA.
DR   EMBL; AL050321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471133; EAX10255.1; -; Genomic_DNA.
DR   EMBL; BC007537; AAH07537.1; -; mRNA.
DR   EMBL; BC009174; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF252257; AAG10249.1; -; mRNA.
DR   CCDS; CCDS13133.1; -. [Q9H8E8-1]
DR   RefSeq; NP_065397.3; NM_020536.4. [Q9H8E8-1]
DR   AlphaFoldDB; Q9H8E8; -.
DR   SMR; Q9H8E8; -.
DR   BioGRID; 121485; 113.
DR   ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR   ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR   CORUM; Q9H8E8; -.
DR   IntAct; Q9H8E8; 39.
DR   MINT; Q9H8E8; -.
DR   STRING; 9606.ENSP00000392318; -.
DR   GlyGen; Q9H8E8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9H8E8; -.
DR   PhosphoSitePlus; Q9H8E8; -.
DR   BioMuta; KAT14; -.
DR   DMDM; 308153608; -.
DR   EPD; Q9H8E8; -.
DR   jPOST; Q9H8E8; -.
DR   MassIVE; Q9H8E8; -.
DR   MaxQB; Q9H8E8; -.
DR   PaxDb; 9606-ENSP00000392318; -.
DR   PeptideAtlas; Q9H8E8; -.
DR   ProteomicsDB; 81203; -. [Q9H8E8-1]
DR   ProteomicsDB; 81204; -. [Q9H8E8-2]
DR   Pumba; Q9H8E8; -.
DR   Antibodypedia; 24530; 187 antibodies from 23 providers.
DR   DNASU; 57325; -.
DR   Ensembl; ENST00000377681.8; ENSP00000366909.3; ENSG00000149474.15. [Q9H8E8-1]
DR   Ensembl; ENST00000435364.8; ENSP00000392318.2; ENSG00000149474.15. [Q9H8E8-1]
DR   Ensembl; ENST00000464792.2; ENSP00000424752.2; ENSG00000149474.15. [Q9H8E8-1]
DR   Ensembl; ENST00000489634.2; ENSP00000425909.2; ENSG00000149474.15. [Q9H8E8-2]
DR   Ensembl; ENST00000676935.1; ENSP00000503493.1; ENSG00000149474.15. [Q9H8E8-1]
DR   Ensembl; ENST00000677174.1; ENSP00000503109.1; ENSG00000149474.15. [Q9H8E8-1]
DR   Ensembl; ENST00000677266.1; ENSP00000504050.1; ENSG00000149474.15. [Q9H8E8-1]
DR   Ensembl; ENST00000678772.1; ENSP00000504276.1; ENSG00000149474.15. [Q9H8E8-1]
DR   GeneID; 57325; -.
DR   KEGG; hsa:57325; -.
DR   UCSC; uc002wqk.3; human. [Q9H8E8-1]
DR   AGR; HGNC:15904; -.
DR   CTD; 57325; -.
DR   DisGeNET; 57325; -.
DR   GeneCards; KAT14; -.
DR   HGNC; HGNC:15904; KAT14.
DR   HPA; ENSG00000149474; Low tissue specificity.
DR   MIM; 617501; gene.
DR   neXtProt; NX_Q9H8E8; -.
DR   OpenTargets; ENSG00000149474; -.
DR   PharmGKB; PA26969; -.
DR   VEuPathDB; HostDB:ENSG00000149474; -.
DR   eggNOG; KOG3138; Eukaryota.
DR   GeneTree; ENSGT00390000001146; -.
DR   HOGENOM; CLU_022855_0_0_1; -.
DR   InParanoid; Q9H8E8; -.
DR   OMA; RNWPWLQ; -.
DR   OrthoDB; 26652at2759; -.
DR   PhylomeDB; Q9H8E8; -.
DR   TreeFam; TF324809; -.
DR   BRENDA; 2.3.1.48; 2681.
DR   PathwayCommons; Q9H8E8; -.
DR   Reactome; R-HSA-3214847; HATs acetylate histones.
DR   Reactome; R-HSA-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   SignaLink; Q9H8E8; -.
DR   BioGRID-ORCS; 57325; 31 hits in 1147 CRISPR screens.
DR   ChiTaRS; KAT14; human.
DR   GeneWiki; CSRP2BP; -.
DR   GenomeRNAi; 57325; -.
DR   Pharos; Q9H8E8; Tbio.
DR   PRO; PR:Q9H8E8; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9H8E8; Protein.
DR   Bgee; ENSG00000149474; Expressed in deltoid and 184 other cell types or tissues.
DR   ExpressionAtlas; Q9H8E8; baseline and differential.
DR   Genevisible; Q9H8E8; HS.
DR   GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0072686; C:mitotic spindle; NAS:ComplexPortal.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IPI:UniProtKB.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
DR   GO; GO:0030274; F:LIM domain binding; NAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR   GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:ComplexPortal.
DR   GO; GO:0045995; P:regulation of embryonic development; ISO:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.90.980.20; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR20916; CYSTEINE AND GLYCINE-RICH PROTEIN 2 BINDING PROTEIN; 1.
DR   PANTHER; PTHR20916:SF26; CYSTEINE-RICH PROTEIN 2-BINDING PROTEIN; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..782
FT                   /note="Cysteine-rich protein 2-binding protein"
FT                   /id="PRO_0000074603"
FT   DOMAIN          638..782
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          13..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         231
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CID0"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         292
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..128
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_000070"
FT   VARIANT         214
FT                   /note="P -> L (in dbSNP:rs6081011)"
FT                   /id="VAR_028034"
FT   VARIANT         400
FT                   /note="V -> G (in dbSNP:rs1205193)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_028035"
FT   VARIANT         442
FT                   /note="R -> T (in dbSNP:rs2295182)"
FT                   /id="VAR_020466"
FT   VARIANT         600
FT                   /note="P -> R (in dbSNP:rs11557577)"
FT                   /id="VAR_033839"
FT   VARIANT         738
FT                   /note="A -> S (in dbSNP:rs6081027)"
FT                   /id="VAR_048166"
FT   CONFLICT        535
FT                   /note="R -> G (in Ref. 1; BAB14669)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   782 AA;  88844 MW;  E84FAEF06412EA77 CRC64;
     MDSSIHLSSL ISRHDDEATR TSTSEGLEEG EVEGETLLIV ESEDQASVDL SHDQSGDSLN
     SDEGDVSWME EQLSYFCDKC QKWIPASQLR EQLSYLKGDN FFRFTCSDCS ADGKEQYERL
     KLTWQQVVML AMYNLSLEGS GRQGYFRWKE DICAFIEKHW TFLLGNRKKT STWWSTVAGC
     LSVGSPMYFR SGAQEFGEPG WWKLVHNKPP TMKPEGEKLS ASTLKIKAAS KPTLDPIITV
     EGLRKRASRN PVESAMELKE KRSRTQEAKD IRRAQKEAAG FLDRSTSSTP VKFISRGRRP
     DVILEKGEVI DFSSLSSSDR TPLTSPSPSP SLDFSAPGTP ASHSATPSLL SEADLIPDVM
     PPQALFHDDD EMEGDGVIDP GMEYVPPPAG SVASGPVVGV RKKVRGPEQI KQEVESEEEK
     PDRMDIDSED TDSNTSLQTR AREKRKPQLE KDTKPKEPRY TPVSIYEEKL LLKRLEACPG
     AVAMTPEARR LKRKLIVRQA KRDRGLPLFD LDQVVNAALL LVDGIYGAKE GGISRLPAGQ
     ATYRTTCQDF RILDRYQTSL PSRKGFRHQT TKFLYRLVGS EDMAVDQSIV SPYTSRILKP
     YIRRDYETKP PKLQLLSQIR SHLHRSDPHW TPEPDAPLDY CYVRPNHIPT INSMCQEFFW
     PGIDLSECLQ YPDFSVVVLY KKVIIAFGFM VPDVKYNEAY ISFLFVHPEW RRAGIATFMI
     YHLIQTCMGK DVTLHVSASN PAMLLYQKFG FKTEEYVLDF YDKYYPLEST ECKHAFFLRL
     RR
//
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