CLASR_HUMAN
ID CLASR_HUMAN Reviewed; 674 AA.
AC Q8N2M8; B4DDT8; F8WAG9; O96026; Q6UW71; Q96DX2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=CLK4-associating serine/arginine rich protein;
DE AltName: Full=Splicing factor, arginine/serine-rich 16;
DE AltName: Full=Suppressor of white-apricot homolog 2;
GN Name=CLASRP; Synonyms=SFRS16, SWAP2; ORFNames=UNQ2428/PRO4988;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT GLU-174.
RA Yoshiura K., Murray J.C.;
RT "A transcriptional map in the region of 19q13 derived using direct
RT sequencing and exon trapping.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLU-174.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLU-174.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-174.
RC TISSUE=Skin;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; THR-327; SER-331 AND
RP SER-335, AND 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-335, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-547, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-285; SER-294;
RP SER-547 AND THR-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-547, AND
RP IDENTIFICATION BY 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 [13]
RP VARIANT [LARGE SCALE ANALYSIS] SER-213.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Probably functions as an alternative splicing regulator. May
CC regulate the mRNA splicing of genes such as CLK1. May act by regulating
CC members of the CLK kinase family (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Probably interacts with CLK4. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N2M8; Q9NU02: ANKEF1; NbExp=3; IntAct=EBI-751069, EBI-8464238;
CC Q8N2M8; Q9Y6A4: CFAP20; NbExp=4; IntAct=EBI-751069, EBI-1046872;
CC Q8N2M8; P49759-3: CLK1; NbExp=3; IntAct=EBI-751069, EBI-11981867;
CC Q8N2M8; P49760: CLK2; NbExp=3; IntAct=EBI-751069, EBI-750020;
CC Q8N2M8; P49761: CLK3; NbExp=4; IntAct=EBI-751069, EBI-745579;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N2M8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N2M8-3; Sequence=VSP_013894, VSP_013895;
CC Name=3;
CC IsoId=Q8N2M8-4; Sequence=VSP_055717;
CC -!- PTM: Phosphorylated in vitro by CLK4. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC82339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC82340.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH80554.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF042800; AAC82339.1; ALT_INIT; mRNA.
DR EMBL; AF042810; AAC82340.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF042802; AAC82340.1; JOINED; Genomic_DNA.
DR EMBL; AF042803; AAC82340.1; JOINED; Genomic_DNA.
DR EMBL; AF042804; AAC82340.1; JOINED; Genomic_DNA.
DR EMBL; AF042805; AAC82340.1; JOINED; Genomic_DNA.
DR EMBL; AF042806; AAC82340.1; JOINED; Genomic_DNA.
DR EMBL; AF042807; AAC82340.1; JOINED; Genomic_DNA.
DR EMBL; AF042808; AAC82340.1; JOINED; Genomic_DNA.
DR EMBL; AF042809; AAC82340.1; JOINED; Genomic_DNA.
DR EMBL; AY358944; AAQ89303.1; -; mRNA.
DR EMBL; AK293333; BAG56849.1; -; mRNA.
DR EMBL; AC011489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080554; AAH80554.1; ALT_INIT; mRNA.
DR CCDS; CCDS12652.2; -. [Q8N2M8-1]
DR CCDS; CCDS62710.1; -. [Q8N2M8-4]
DR RefSeq; NP_001265368.1; NM_001278439.1.
DR RefSeq; NP_008987.2; NM_007056.2.
DR AlphaFoldDB; Q8N2M8; -.
DR SMR; Q8N2M8; -.
DR BioGRID; 116302; 81.
DR IntAct; Q8N2M8; 32.
DR STRING; 9606.ENSP00000221455; -.
DR GlyGen; Q8N2M8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N2M8; -.
DR PhosphoSitePlus; Q8N2M8; -.
DR BioMuta; CLASRP; -.
DR DMDM; 226694202; -.
DR EPD; Q8N2M8; -.
DR jPOST; Q8N2M8; -.
DR MassIVE; Q8N2M8; -.
DR MaxQB; Q8N2M8; -.
DR PaxDb; Q8N2M8; -.
DR PeptideAtlas; Q8N2M8; -.
DR PRIDE; Q8N2M8; -.
DR ProteomicsDB; 30495; -.
DR ProteomicsDB; 71717; -. [Q8N2M8-1]
DR ProteomicsDB; 71718; -. [Q8N2M8-3]
DR Antibodypedia; 54055; 73 antibodies from 19 providers.
DR DNASU; 11129; -.
DR Ensembl; ENST00000391952.7; ENSP00000375814.2; ENSG00000104859.15.
DR Ensembl; ENST00000391953.8; ENSP00000375815.3; ENSG00000104859.15.
DR GeneID; 11129; -.
DR KEGG; hsa:11129; -.
DR UCSC; uc010xxh.3; human. [Q8N2M8-1]
DR CTD; 11129; -.
DR DisGeNET; 11129; -.
DR GeneCards; CLASRP; -.
DR HGNC; HGNC:17731; CLASRP.
DR HPA; ENSG00000104859; Low tissue specificity.
DR MIM; 618532; gene.
DR neXtProt; NX_Q8N2M8; -.
DR PharmGKB; PA134961731; -.
DR VEuPathDB; HostDB:ENSG00000104859; -.
DR eggNOG; KOG2548; Eukaryota.
DR InParanoid; Q8N2M8; -.
DR OrthoDB; 1620115at2759; -.
DR PhylomeDB; Q8N2M8; -.
DR TreeFam; TF351621; -.
DR PathwayCommons; Q8N2M8; -.
DR SignaLink; Q8N2M8; -.
DR BioGRID-ORCS; 11129; 364 hits in 1096 CRISPR screens.
DR ChiTaRS; CLASRP; human.
DR GeneWiki; SFRS16; -.
DR GenomeRNAi; 11129; -.
DR Pharos; Q8N2M8; Tbio.
DR PRO; PR:Q8N2M8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N2M8; protein.
DR Bgee; ENSG00000104859; Expressed in adenohypophysis and 190 other tissues.
DR ExpressionAtlas; Q8N2M8; baseline and differential.
DR Genevisible; Q8N2M8; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR040397; SWAP.
DR InterPro; IPR019147; SWAP_N_domain.
DR PANTHER; PTHR13161; PTHR13161; 2.
DR Pfam; PF09750; DRY_EERY; 1.
DR SMART; SM01141; DRY_EERY; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..674
FT /note="CLK4-associating serine/arginine rich protein"
FT /id="PRO_0000081945"
FT REGION 172..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 585..647
FT /evidence="ECO:0000255"
FT COMPBIAS 185..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..441
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..491
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 573
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 42..103
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055717"
FT VAR_SEQ 570..594
FT /note="PKLTPQEKLKLRMQKALNRQFKADK -> VTQADASGEAETEDAEGAEQAVQ
FT GG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013894"
FT VAR_SEQ 595..674
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013895"
FT VARIANT 174
FT /note="K -> E (in dbSNP:rs4803794)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.1"
FT /id="VAR_016809"
FT VARIANT 213
FT /note="L -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035490"
SQ SEQUENCE 674 AA; 77161 MW; 454F935EBDD96541 CRC64;
MWHEARKHER KLRGMMVDYK KRAERRREYY EKIKKDPAQF LQVHGRACKV HLDSAVALAA
ESPVNMMPWQ GDTNNMIDRF DVRAHLDHIP DYTPPLLTTI SPEQESDERK CNYERYRGLV
QNDFAGISEE QCLYQIYIDE LYGGLQRPSE DEKKKLAEKK ASIGYTYEDS TVAKVEKAAE
KPEEEESAAE EESNSDEDEV IPDIDVEVDV DELNQEQVAD LNKQATTYGM ADGDFVRMLR
KDKEEAEAIK HAKALEEEKA MYSGRRSRRQ RREFREKRLR GRKISPPSYA RRDSPTYDPY
KRSPSESSSE SRSRSRSPTP GREEKITFIT SFGGSDEEAA AAAAAAAASG VTTGKPPAPP
QPGGPAPGRN ASARRRSSSS SSSSSASRTS SSRSSSRSSS RSRRGGGYYR SGRHARSRSR
SWSRSRSRSR RYSRSRSRGR RHSGGGSRDG HRYSRSPARR GGYGPRRRSR SRSHSGDRYR
RGGRGLRHHS SSRSRSSWSL SPSRSRSLTR SRSHSPSPSQ SRSRSRSRSQ SPSPSPAREK
LTRPAASPAV GEKLKKTEPA AGKETGAAKP KLTPQEKLKL RMQKALNRQF KADKKAAQEK
MIQQEHERQE REDELRAMAR KIRMKERERR EKEREEWERQ YSRQSRSPSP RYSREYSSSR
RRSRSRSRSP HYRH
