VRK3_HUMAN
ID VRK3_HUMAN Reviewed; 474 AA.
AC Q8IV63; A6NEG5; A8KA53; Q502Y2; Q9P2V8;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Inactive serine/threonine-protein kinase VRK3;
DE AltName: Full=Serine/threonine-protein pseudokinase VRK3;
DE AltName: Full=Vaccinia-related kinase 3;
GN Name=VRK3;
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).
RC TISSUE=Liver;
RA Nezu J.;
RT "Vaccinia related kinase 3 (VRK3).";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ni X., Xie Y., Mao Y.;
RT "Cloning and characterization of a novel human VRK3 gene.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis, and Trachea;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and 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 FUNCTION, SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=14645249; DOI=10.1074/jbc.m310813200;
RA Nichols R.J., Traktman P.;
RT "Characterization of three paralogous members of the Mammalian vaccinia
RT related kinase family.";
RL J. Biol. Chem. 279:7934-7946(2004).
RN [7]
RP INTERACTION WITH RAN.
RX PubMed=18617507; DOI=10.1074/mcp.m700586-mcp200;
RA Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A.;
RT "Proteomics identification of nuclear Ran GTPase as an inhibitor of human
RT VRK1 and VRK2 (vaccinia-related kinase) activities.";
RL Mol. Cell. Proteomics 7:2199-2214(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-59, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83 AND SER-90, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-83, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83; SER-115 AND
RP SER-122, AND 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-59 AND SER-83, 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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 146-474, FUNCTION, AND LACK OF
RP CATALYTIC ACTIVITY.
RX PubMed=19141289; DOI=10.1016/j.str.2008.10.018;
RA Scheeff E.D., Eswaran J., Bunkoczi G., Knapp S., Manning G.;
RT "Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a
RT highly conserved kinase fold, and a putative regulatory binding site.";
RL Structure 17:128-138(2009).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] PHE-59; THR-105; LEU-171; LEU-268; TYR-288;
RP CYS-370 AND GLY-371.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Inactive kinase that suppresses ERK activity by promoting
CC phosphatase activity of DUSP3 which specifically dephosphorylates and
CC inactivates ERK in the nucleus. {ECO:0000250,
CC ECO:0000269|PubMed:14645249, ECO:0000269|PubMed:19141289}.
CC -!- SUBUNIT: Interacts with DUSP3 (By similarity). Interacts with RAN.
CC {ECO:0000250, ECO:0000269|PubMed:18617507}.
CC -!- INTERACTION:
CC Q8IV63; P61244: MAX; NbExp=2; IntAct=EBI-1058605, EBI-751711;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14645249}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IV63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IV63-2; Sequence=VSP_008544, VSP_008545;
CC Name=3;
CC IsoId=Q8IV63-3; Sequence=VSP_043409;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. VRK subfamily. {ECO:0000305}.
CC -!- CAUTION: Inactive as a kinase due to its inability to bind ATP.
CC {ECO:0000305|PubMed:19141289}.
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DR EMBL; AB031052; BAA90769.1; -; mRNA.
DR EMBL; AF514788; AAP47180.1; -; mRNA.
DR EMBL; AK292918; BAF85607.1; -; mRNA.
DR EMBL; AK303010; BAG64141.1; -; mRNA.
DR EMBL; AC011452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023556; AAH23556.1; -; mRNA.
DR EMBL; BC095449; AAH95449.1; -; mRNA.
DR CCDS; CCDS12791.1; -. [Q8IV63-1]
DR CCDS; CCDS33076.1; -. [Q8IV63-3]
DR CCDS; CCDS77334.1; -. [Q8IV63-2]
DR RefSeq; NP_001020949.1; NM_001025778.1. [Q8IV63-3]
DR RefSeq; NP_001295349.1; NM_001308420.1. [Q8IV63-2]
DR RefSeq; NP_057524.3; NM_016440.3. [Q8IV63-1]
DR RefSeq; XP_005259028.1; XM_005258971.3. [Q8IV63-1]
DR RefSeq; XP_005259029.1; XM_005258972.3. [Q8IV63-3]
DR RefSeq; XP_006723300.1; XM_006723237.3. [Q8IV63-1]
DR RefSeq; XP_006723301.1; XM_006723238.3. [Q8IV63-3]
DR RefSeq; XP_011525325.1; XM_011527023.2.
DR PDB; 2JII; X-ray; 2.00 A; A/B=146-474.
DR PDBsum; 2JII; -.
DR AlphaFoldDB; Q8IV63; -.
DR SMR; Q8IV63; -.
DR BioGRID; 119394; 133.
DR IntAct; Q8IV63; 27.
DR MINT; Q8IV63; -.
DR STRING; 9606.ENSP00000469880; -.
DR ChEMBL; CHEMBL3430761; -.
DR GlyGen; Q8IV63; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IV63; -.
DR PhosphoSitePlus; Q8IV63; -.
DR BioMuta; VRK3; -.
DR DMDM; 45593724; -.
DR EPD; Q8IV63; -.
DR jPOST; Q8IV63; -.
DR MassIVE; Q8IV63; -.
DR MaxQB; Q8IV63; -.
DR PaxDb; Q8IV63; -.
DR PeptideAtlas; Q8IV63; -.
DR PRIDE; Q8IV63; -.
DR ProteomicsDB; 70666; -. [Q8IV63-1]
DR ProteomicsDB; 70667; -. [Q8IV63-2]
DR ProteomicsDB; 70668; -. [Q8IV63-3]
DR TopDownProteomics; Q8IV63-1; -. [Q8IV63-1]
DR Antibodypedia; 18806; 95 antibodies from 26 providers.
DR DNASU; 51231; -.
DR Ensembl; ENST00000316763.8; ENSP00000324636.2; ENSG00000105053.11. [Q8IV63-1]
DR Ensembl; ENST00000377011.6; ENSP00000366210.1; ENSG00000105053.11. [Q8IV63-3]
DR Ensembl; ENST00000594092.5; ENSP00000472541.1; ENSG00000105053.11. [Q8IV63-2]
DR Ensembl; ENST00000594948.5; ENSP00000473171.1; ENSG00000105053.11. [Q8IV63-1]
DR Ensembl; ENST00000599538.5; ENSP00000469880.1; ENSG00000105053.11. [Q8IV63-1]
DR Ensembl; ENST00000601341.5; ENSP00000470156.1; ENSG00000105053.11. [Q8IV63-3]
DR GeneID; 51231; -.
DR KEGG; hsa:51231; -.
DR MANE-Select; ENST00000316763.8; ENSP00000324636.2; NM_016440.4; NP_057524.3.
DR UCSC; uc002prg.3; human. [Q8IV63-1]
DR CTD; 51231; -.
DR DisGeNET; 51231; -.
DR GeneCards; VRK3; -.
DR HGNC; HGNC:18996; VRK3.
DR HPA; ENSG00000105053; Tissue enhanced (testis).
DR MIM; 619771; gene.
DR neXtProt; NX_Q8IV63; -.
DR OpenTargets; ENSG00000105053; -.
DR PharmGKB; PA134923990; -.
DR VEuPathDB; HostDB:ENSG00000105053; -.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000158111; -.
DR InParanoid; Q8IV63; -.
DR OMA; AYMEGSR; -.
DR PhylomeDB; Q8IV63; -.
DR TreeFam; TF106473; -.
DR PathwayCommons; Q8IV63; -.
DR Reactome; R-HSA-202670; ERKs are inactivated.
DR SignaLink; Q8IV63; -.
DR SIGNOR; Q8IV63; -.
DR BioGRID-ORCS; 51231; 9 hits in 1117 CRISPR screens.
DR ChiTaRS; VRK3; human.
DR EvolutionaryTrace; Q8IV63; -.
DR GenomeRNAi; 51231; -.
DR Pharos; Q8IV63; Tbio.
DR PRO; PR:Q8IV63; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IV63; protein.
DR Bgee; ENSG00000105053; Expressed in sperm and 190 other tissues.
DR ExpressionAtlas; Q8IV63; baseline and differential.
DR Genevisible; Q8IV63; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0019903; F:protein phosphatase binding; IDA:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IGI:FlyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR026870; Zinc_ribbon_dom.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13240; zinc_ribbon_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..474
FT /note="Inactive serine/threonine-protein kinase VRK3"
FT /id="PRO_0000086808"
FT DOMAIN 166..457
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 41..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..64
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:14645249"
FT COMPBIAS 41..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 47..96
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043409"
FT VAR_SEQ 407..412
FT /note="FVDKPG -> LPWDSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008544"
FT VAR_SEQ 413..474
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008545"
FT VARIANT 59
FT /note="S -> F (in dbSNP:rs2033262)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041295"
FT VARIANT 105
FT /note="P -> T (in dbSNP:rs11547882)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041296"
FT VARIANT 170
FT /note="S -> P (in dbSNP:rs11547881)"
FT /id="VAR_051682"
FT VARIANT 171
FT /note="F -> L (in dbSNP:rs11547883)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041297"
FT VARIANT 188
FT /note="T -> A (in dbSNP:rs11879620)"
FT /id="VAR_051683"
FT VARIANT 268
FT /note="S -> L (in dbSNP:rs10410075)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041298"
FT VARIANT 288
FT /note="C -> Y (in dbSNP:rs10409482)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041299"
FT VARIANT 304
FT /note="H -> L (in dbSNP:rs35261919)"
FT /id="VAR_051684"
FT VARIANT 370
FT /note="R -> C (in dbSNP:rs35331034)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041300"
FT VARIANT 371
FT /note="S -> G (in dbSNP:rs56407496)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041301"
FT CONFLICT 161
FT /note="K -> E (in Ref. 2; AAP47180)"
FT /evidence="ECO:0000305"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:2JII"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2JII"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:2JII"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2JII"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:2JII"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:2JII"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2JII"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 280..299
FT /evidence="ECO:0007829|PDB:2JII"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2JII"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2JII"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 369..385
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 426..436
FT /evidence="ECO:0007829|PDB:2JII"
FT HELIX 446..459
FT /evidence="ECO:0007829|PDB:2JII"
SQ SEQUENCE 474 AA; 52881 MW; 86B9B91050A7F0CC CRC64;
MISFCPDCGK SIQAAFKFCP YCGNSLPVEE HVGSQTFVNP HVSSFQGSKR GLNSSFETSP
KKVKWSSTVT SPRLSLFSDG DSSESEDTLS SSERSKGSGS RPPTPKSSPQ KTRKSPQVTR
GSPQKTSCSP QKTRQSPQTL KRSRVTTSLE ALPTGTVLTD KSGRQWKLKS FQTRDNQGIL
YEAAPTSTLT CDSGPQKQKF SLKLDAKDGR LFNEQNFFQR AAKPLQVNKW KKLYSTPLLA
IPTCMGFGVH QDKYRFLVLP SLGRSLQSAL DVSPKHVLSE RSVLQVACRL LDALEFLHEN
EYVHGNVTAE NIFVDPEDQS QVTLAGYGFA FRYCPSGKHV AYVEGSRSPH EGDLEFISMD
LHKGCGPSRR SDLQSLGYCM LKWLYGFLPW TNCLPNTEDI MKQKQKFVDK PGPFVGPCGH
WIRPSETLQK YLKVVMALTY EEKPPYAMLR NNLEALLQDL RVSPYDPIGL PMVP
