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Troponin I, cardiac muscle (Cardiac troponin I)

 TNNI3_HUMAN             Reviewed;         210 AA.
P19429;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 178.
RecName: Full=Troponin I, cardiac muscle;
AltName: Full=Cardiac troponin I;
Name=TNNI3; Synonyms=TNNC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart muscle;
PubMed=2226790; DOI=10.1016/0014-5793(90)81234-F;
Vallins W.J., Brand N.J., Dabhade N., Butler-Browne G., Yacoub M.H.,
Barton P.J.R.;
"Molecular cloning of human cardiac troponin I using polymerase chain
reaction.";
FEBS Lett. 270:57-61(1990).
[2]
SEQUENCE REVISION TO 85, AND NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8406024; DOI=10.1016/0378-1119(93)90308-P;
Armour K.L., Harris W.J., Tempest P.R.;
"Cloning and expression in Escherichia coli of the cDNA encoding human
cardiac troponin I.";
Gene 131:287-292(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1934363; DOI=10.1161/01.RES.69.5.1409;
Hunkeler N.M., Kullman J., Murphy A.M.;
"Troponin I isoform expression in human heart.";
Circ. Res. 69:1409-1414(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8661099; DOI=10.1006/geno.1996.0317;
Bhavsar P.K., Brand N.J., Yacoub M.H., Barton P.J.R.;
"Isolation and characterization of the human cardiac troponin I gene
(TNNI3).";
Genomics 35:11-23(1996).
[5]
PROTEIN SEQUENCE OF 11-36, ACETYLATION AT ALA-2, AND PHOSPHORYLATION
AT SER-23 AND SER-24.
PubMed=2226863; DOI=10.1016/0014-5793(90)81046-Q;
Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.;
"A common motif of two adjacent phosphoserines in bovine, rabbit and
human cardiac troponin I.";
FEBS Lett. 273:41-45(1990).
[6]
PHOSPHORYLATION AT SER-23 AND SER-24.
PubMed=9346285; DOI=10.1111/j.1432-1033.1997.00329.x;
Keane N.E., Quirk P.G., Gao Y., Patchell V.B., Perry S.V.,
Levine B.A.;
"The ordered phosphorylation of cardiac troponin I by the cAMP-
dependent protein kinase -- structural consequences and functional
implications.";
Eur. J. Biochem. 248:329-337(1997).
[7]
PHOSPHORYLATION AT SER-150 BY PAK3.
PubMed=12242269; DOI=10.1161/01.RES.0000035246.27856.53;
Buscemi N., Foster D.B., Neverova I., Van Eyk J.E.;
"p21-activated kinase increases the calcium sensitivity of rat triton-
skinned cardiac muscle fiber bundles via a mechanism potentially
involving novel phosphorylation of troponin I.";
Circ. Res. 91:509-516(2002).
[8]
PHOSPHORYLATION AT SER-23 AND SER-24.
PubMed=15514163; DOI=10.1161/01.RES.0000149299.34793.3c;
Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C.,
Gautel M., Avkiran M.;
"Protein kinase D is a novel mediator of cardiac troponin I
phosphorylation and regulates myofilament function.";
Circ. Res. 95:1091-1099(2004).
[9]
INTERACTION WITH TRIM63.
PubMed=15601779; DOI=10.1073/pnas.0404341102;
Kedar V., McDonough H., Arya R., Li H.-H., Rockman H.A., Patterson C.;
"Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that
degrades cardiac troponin I.";
Proc. Natl. Acad. Sci. U.S.A. 101:18135-18140(2004).
[10]
INTERACTION WITH STK4/MST1, AND PHOSPHORYLATION AT THR-31; THR-51;
THR-129 AND THR-143.
PubMed=18986304; DOI=10.1042/BJ20081340;
You B., Yan G., Zhang Z., Yan L., Li J., Ge Q., Jin J.P., Sun J.;
"Phosphorylation of cardiac troponin I by mammalian sterile 20-like
kinase 1.";
Biochem. J. 418:93-101(2009).
[11]
PHOSPHORYLATION AT SER-5; SER-6; SER-23; SER-24; TYR-26; SER-42;
SER-44; THR-51; SER-77; THR-78; THR-143; SER-166; THR-181 AND SER-199.
PubMed=22972900; DOI=10.1161/CIRCULATIONAHA.112.096388;
Zhang P., Kirk J.A., Ji W., dos Remedios C.G., Kass D.A.,
Van Eyk J.E., Murphy A.M.;
"Multiple reaction monitoring to identify site-specific troponin I
phosphorylated residues in the failing human heart.";
Circulation 126:1828-1837(2012).
[12]
STRUCTURE BY NMR OF 148-164.
PubMed=10387074; DOI=10.1021/bi9901679;
Li M.X., Spyracopoulos L., Sykes B.D.;
"Binding of cardiac troponin-I147-163 induces a structural opening in
human cardiac troponin-C.";
Biochemistry 38:8289-8298(1999).
[13]
STRUCTURE BY NMR OF 149-165 IN COMPLEX WITH CARDIAC TROPONIN C.
PubMed=12060657; DOI=10.1074/jbc.M203896200;
Wang X., Li M.X., Sykes B.D.;
"Structure of the regulatory N-domain of human cardiac troponin C in
complex with human cardiac troponin I147-163 and bepridil.";
J. Biol. Chem. 277:31124-31133(2002).
[14]
VARIANTS CMH7 GLY-145 AND GLN-206.
PubMed=9241277; DOI=10.1038/ng0897-379;
Kimura A., Harada H., Park J.-E., Nishi H., Satoh M., Takahashi M.,
Hiroi S., Sasaoka T., Ohbuchi N., Nakamura T., Koyanagi T.,
Hwang T.-H., Choo J., Chung K.-S., Hasegawa A., Nagai R., Okazaki O.,
Nakamura H., Matsuzaki M., Sakamoto T., Toshima H., Koga Y.,
Imaizumi T., Sasazuki T.;
"Mutations in the cardiac troponin I gene associated with hypertrophic
cardiomyopathy.";
Nat. Genet. 16:379-382(1997).
[15]
VARIANTS CMH7 SER-82 AND ASN-196.
PubMed=11815426; DOI=10.1161/hc0402.102990;
Niimura H., Patton K.K., McKenna W.J., Soults J., Maron B.J.,
Seidman J.G., Seidman C.E.;
"Sarcomere protein gene mutations in hypertrophic cardiomyopathy of
the elderly.";
Circulation 105:446-451(2002).
[16]
VARIANTS RCM1 GLN-144; TRP-145; THR-171; GLU-178; HIS-190 AND HIS-192.
PubMed=12531876; DOI=10.1172/JCI200316336;
Mogensen J., Kubo T., Duque M., Uribe W., Shaw A., Murphy R.,
Gimeno J.R., Elliott P., McKenna W.J.;
"Idiopathic restrictive cardiomyopathy is part of the clinical
expression of cardiac troponin I mutations.";
J. Clin. Invest. 111:209-216(2003).
[17]
VARIANTS CMH7 GLN-141; VAL-157; PRO-162; LYS-177 DEL; GLN-186 AND
ASN-196.
PubMed=12707239; DOI=10.1161/01.CIR.0000066323.15244.54;
Richard P., Charron P., Carrier L., Ledeuil C., Cheav T.,
Pichereau C., Benaiche A., Isnard R., Dubourg O., Burban M.,
Gueffet J.-P., Millaire A., Desnos M., Schwartz K., Hainque B.,
Komajda M.;
"Hypertrophic cardiomyopathy: distribution of disease genes, spectrum
of mutations, and implications for a molecular diagnosis strategy.";
Circulation 107:2227-2232(2003).
[18]
ERRATUM.
Richard P., Charron P., Carrier L., Ledeuil C., Cheav T.,
Pichereau C., Benaiche A., Isnard R., Dubourg O., Burban M.,
Gueffet J.-P., Millaire A., Desnos M., Schwartz K., Hainque B.,
Komajda M.;
Circulation 109:3258-3258(2004).
[19]
VARIANT CMH7 PHE-166.
PubMed=12974739; DOI=10.1034/j.1399-0004.2003.00151.x;
Erdmann J., Daehmlow S., Wischke S., Senyuva M., Werner U., Raible J.,
Tanis N., Dyachenko S., Hummel M., Hetzer R., Regitz-Zagrosek V.;
"Mutation spectrum in a large cohort of unrelated consecutive patients
with hypertrophic cardiomyopathy.";
Clin. Genet. 64:339-349(2003).
[20]
VARIANT CMD2A VAL-2.
PubMed=15070570; DOI=10.1016/S0140-6736(04)15468-8;
Murphy R.T., Mogensen J., Shaw A., Kubo T., Hughes S., McKenna W.J.;
"Novel mutation in cardiac troponin I in recessive idiopathic dilated
cardiomyopathy.";
Lancet 363:371-372(2004).
[21]
VARIANTS CMH7 PRO-162; GLN-162 AND HIS-204.
PubMed=16199542; DOI=10.1136/jmg.2005.033886;
Ingles J., Doolan A., Chiu C., Seidman J., Seidman C., Semsarian C.;
"Compound and double mutations in patients with hypertrophic
cardiomyopathy: implications for genetic testing and counselling.";
J. Med. Genet. 42:E59-E59(2005).
[22]
VARIANTS CMD1FF GLN-36 AND LYS-185.
PubMed=19590045; DOI=10.1161/CIRCRESAHA.109.196055;
Carballo S., Robinson P., Otway R., Fatkin D., Jongbloed J.D.,
de Jonge N., Blair E., van Tintelen J.P., Redwood C., Watkins H.;
"Identification and functional characterization of cardiac troponin I
as a novel disease gene in autosomal dominant dilated
cardiomyopathy.";
Circ. Res. 105:375-382(2009).
[23]
VARIANT CMD1FF GLY-116.
PubMed=21846512; DOI=10.1016/j.ejmg.2011.07.005;
Millat G., Bouvagnet P., Chevalier P., Sebbag L., Dulac A.,
Dauphin C., Jouk P.S., Delrue M.A., Thambo J.B., Le Metayer P.,
Seronde M.F., Faivre L., Eicher J.C., Rousson R.;
"Clinical and mutational spectrum in a cohort of 105 unrelated
patients with dilated cardiomyopathy.";
Eur. J. Med. Genet. 54:E570-E575(2011).
-!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the
thin filament regulatory complex which confers calcium-sensitivity
to striated muscle actomyosin ATPase activity.
-!- SUBUNIT: Binds to actin and tropomyosin. Interacts with TRIM63.
Interacts with STK4/MST1. {ECO:0000269|PubMed:12060657,
ECO:0000269|PubMed:15601779, ECO:0000269|PubMed:18986304}.
-!- INTERACTION:
Q5VU43-11:PDE4DIP; NbExp=4; IntAct=EBI-704146, EBI-10769071;
Q9UKA8-1:RCAN3; NbExp=3; IntAct=EBI-704146, EBI-10762111;
Q9UKA8-4:RCAN3; NbExp=2; IntAct=EBI-704146, EBI-10762136;
P02585:TNNC2; NbExp=3; IntAct=EBI-704146, EBI-10249681;
Q59H18:TNNI3K; NbExp=2; IntAct=EBI-704146, EBI-704142;
Q59H18-2:TNNI3K; NbExp=2; IntAct=EBI-704146, EBI-10762055;
-!- PTM: Phosphorylated at Ser-42 and Ser-44 by PRKCE; phosphorylation
increases myocardium contractile dysfunction (By similarity).
Phosphorylated at Ser-23 and Ser-24 by PRKD1; phosphorylation
reduces myofilament calcium sensitivity. Phosphorylated
preferentially at Thr-31. Phosphorylation by STK4/MST1 alters its
binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T).
{ECO:0000250, ECO:0000269|PubMed:12242269,
ECO:0000269|PubMed:15514163, ECO:0000269|PubMed:18986304,
ECO:0000269|PubMed:2226863, ECO:0000269|PubMed:22972900,
ECO:0000269|PubMed:9346285}.
-!- DISEASE: Cardiomyopathy, familial hypertrophic 7 (CMH7)
[MIM:613690]: A hereditary heart disorder characterized by
ventricular hypertrophy, which is usually asymmetric and often
involves the interventricular septum. The symptoms include
dyspnea, syncope, collapse, palpitations, and chest pain. They can
be readily provoked by exercise. The disorder has inter- and
intrafamilial variability ranging from benign to malignant forms
with high risk of cardiac failure and sudden cardiac death.
{ECO:0000269|PubMed:11815426, ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:16199542,
ECO:0000269|PubMed:9241277}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, familial restrictive 1 (RCM1)
[MIM:115210]: A heart disorder characterized by impaired filling
of the ventricles with reduced diastolic volume, in the presence
of normal or near normal wall thickness and systolic function.
{ECO:0000269|PubMed:12531876}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, dilated 2A (CMD2A) [MIM:611880]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:15070570}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, dilated 1FF (CMD1FF) [MIM:613286]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:19590045, ECO:0000269|PubMed:21846512}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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EMBL; X54163; CAA38102.1; -; mRNA.
EMBL; M64247; AAA16157.1; -; mRNA.
EMBL; X90780; CAA62301.1; -; Genomic_DNA.
CCDS; CCDS42628.1; -.
PIR; A61229; TPHUIC.
RefSeq; NP_000354.4; NM_000363.4.
UniGene; Hs.709179; -.
PDB; 1J1D; X-ray; 2.61 A; C/F=31-163.
PDB; 1J1E; X-ray; 3.30 A; C/F=31-210.
PDB; 1LXF; NMR; -; I=148-164.
PDB; 1MXL; NMR; -; I=148-164.
PDB; 1OZS; NMR; -; B=129-148.
PDB; 2KGB; NMR; -; I=145-164.
PDB; 2KRD; NMR; -; I=148-164.
PDB; 2L1R; NMR; -; B=145-164.
PDB; 2MZP; NMR; -; I=145-171.
PDB; 2N7L; NMR; -; C=145-174.
PDB; 4Y99; X-ray; 2.00 A; C=1-210.
PDB; 5VLN; NMR; -; A=139-164.
PDB; 5W88; NMR; -; A=133-164.
PDB; 5WCL; NMR; -; A=139-164.
PDBsum; 1J1D; -.
PDBsum; 1J1E; -.
PDBsum; 1LXF; -.
PDBsum; 1MXL; -.
PDBsum; 1OZS; -.
PDBsum; 2KGB; -.
PDBsum; 2KRD; -.
PDBsum; 2L1R; -.
PDBsum; 2MZP; -.
PDBsum; 2N7L; -.
PDBsum; 4Y99; -.
PDBsum; 5VLN; -.
PDBsum; 5W88; -.
PDBsum; 5WCL; -.
DisProt; DP00166; -.
ProteinModelPortal; P19429; -.
SMR; P19429; -.
BioGrid; 112991; 15.
DIP; DIP-34065N; -.
IntAct; P19429; 18.
MINT; MINT-2801556; -.
STRING; 9606.ENSP00000341838; -.
ChEMBL; CHEMBL2095202; -.
DrugBank; DB04513; N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide.
iPTMnet; P19429; -.
PhosphoSitePlus; P19429; -.
BioMuta; TNNI3; -.
DMDM; 136213; -.
PaxDb; P19429; -.
PeptideAtlas; P19429; -.
PRIDE; P19429; -.
DNASU; 7137; -.
Ensembl; ENST00000344887; ENSP00000341838; ENSG00000129991.
GeneID; 7137; -.
KEGG; hsa:7137; -.
CTD; 7137; -.
DisGeNET; 7137; -.
EuPathDB; HostDB:ENSG00000129991.12; -.
GeneCards; TNNI3; -.
GeneReviews; TNNI3; -.
HGNC; HGNC:11947; TNNI3.
HPA; CAB009349; -.
HPA; HPA046428; -.
MalaCards; TNNI3; -.
MIM; 115210; phenotype.
MIM; 191044; gene.
MIM; 611880; phenotype.
MIM; 613286; phenotype.
MIM; 613690; phenotype.
neXtProt; NX_P19429; -.
OpenTargets; ENSG00000129991; -.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
Orphanet; 75249; Familial isolated restrictive cardiomyopathy.
PharmGKB; PA36636; -.
eggNOG; KOG3977; Eukaryota.
eggNOG; ENOG410Y9IX; LUCA.
GeneTree; ENSGT00390000002746; -.
HOGENOM; HOG000293300; -.
HOVERGEN; HBG052737; -.
InParanoid; P19429; -.
KO; K12044; -.
OMA; KMFDTGG; -.
OrthoDB; EOG091G0NOD; -.
PhylomeDB; P19429; -.
TreeFam; TF313374; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
Reactome; R-HSA-5578775; Ion homeostasis.
SIGNOR; P19429; -.
ChiTaRS; TNNI3; human.
EvolutionaryTrace; P19429; -.
GeneWiki; TNNI3; -.
GenomeRNAi; 7137; -.
PRO; PR:P19429; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000129991; -.
CleanEx; HS_TNNC1; -.
CleanEx; HS_TNNI3; -.
ExpressionAtlas; P19429; baseline and differential.
Genevisible; P19429; HS.
GO; GO:0097512; C:cardiac myofibril; IMP:CAFA.
GO; GO:1990584; C:cardiac Troponin complex; IMP:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030017; C:sarcomere; TAS:BHF-UCL.
GO; GO:0005861; C:troponin complex; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0051015; F:actin filament binding; IPI:CAFA.
GO; GO:0019855; F:calcium channel inhibitor activity; IPI:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0030172; F:troponin C binding; IPI:UniProtKB.
GO; GO:0031014; F:troponin T binding; IPI:UniProtKB.
GO; GO:0060048; P:cardiac muscle contraction; IMP:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0060047; P:heart contraction; IMP:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0032780; P:negative regulation of ATPase activity; IDA:UniProtKB.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:CAFA.
GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0001980; P:regulation of systemic arterial blood pressure by ischemic conditions; ISS:UniProtKB.
GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:HGNC.
InterPro; IPR001978; Troponin.
InterPro; IPR021666; Troponin-I_N.
Pfam; PF00992; Troponin; 1.
Pfam; PF11636; Troponin-I_N; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Calcium; Cardiomyopathy;
Complete proteome; Direct protein sequencing; Disease mutation;
Metal-binding; Muscle protein; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2226863}.
CHAIN 2 210 Troponin I, cardiac muscle.
/FTId=PRO_0000186151.
CA_BIND 137 148 {ECO:0000250}.
REGION 32 79 Involved in binding TNC.
REGION 129 149 Involved in binding TNC and actin.
SITE 80 80 Involved in TNI-TNT interactions.
SITE 97 97 Involved in TNI-TNT interactions.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:2226863}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000269|PubMed:22972900}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000269|PubMed:22972900}.
MOD_RES 23 23 Phosphoserine; by PKA and PKD/PRKD1.
{ECO:0000269|PubMed:15514163,
ECO:0000269|PubMed:2226863,
ECO:0000269|PubMed:22972900,
ECO:0000269|PubMed:9346285}.
MOD_RES 24 24 Phosphoserine; by PKA and PKD/PRKD1.
{ECO:0000269|PubMed:15514163,
ECO:0000269|PubMed:2226863,
ECO:0000269|PubMed:22972900,
ECO:0000269|PubMed:9346285}.
MOD_RES 26 26 Phosphotyrosine.
{ECO:0000269|PubMed:22972900}.
MOD_RES 31 31 Phosphothreonine; by STK4/MST1.
{ECO:0000269|PubMed:18986304}.
MOD_RES 42 42 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:P48787}.
MOD_RES 44 44 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:P48787}.
MOD_RES 51 51 Phosphothreonine; by STK4/MST1.
{ECO:0000269|PubMed:18986304,
ECO:0000269|PubMed:22972900}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000269|PubMed:22972900}.
MOD_RES 78 78 Phosphothreonine.
{ECO:0000269|PubMed:22972900}.
MOD_RES 129 129 Phosphothreonine; by STK4/MST1.
{ECO:0000269|PubMed:18986304}.
MOD_RES 143 143 Phosphothreonine; by STK4/MST1.
{ECO:0000269|PubMed:18986304,
ECO:0000269|PubMed:22972900}.
MOD_RES 150 150 Phosphoserine; by PAK3.
{ECO:0000269|PubMed:12242269}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000269|PubMed:22972900}.
MOD_RES 181 181 Phosphothreonine.
{ECO:0000269|PubMed:22972900}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000269|PubMed:22972900}.
VARIANT 2 2 A -> V (in CMD2A; dbSNP:rs397516359).
{ECO:0000269|PubMed:15070570}.
/FTId=VAR_043989.
VARIANT 36 36 K -> Q (in CMD1FF; dbSNP:rs267607130).
{ECO:0000269|PubMed:19590045}.
/FTId=VAR_063548.
VARIANT 79 79 R -> C (in dbSNP:rs3729712).
/FTId=VAR_029453.
VARIANT 82 82 P -> S (in CMH7; dbSNP:rs77615401).
{ECO:0000269|PubMed:11815426}.
/FTId=VAR_016078.
VARIANT 116 116 A -> G (in CMD1FF; dbSNP:rs777177571).
{ECO:0000269|PubMed:21846512}.
/FTId=VAR_067264.
VARIANT 141 141 R -> Q (in CMH7; dbSNP:rs397516347).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019872.
VARIANT 144 144 L -> Q (in RCM1; dbSNP:rs121917760).
{ECO:0000269|PubMed:12531876}.
/FTId=VAR_016079.
VARIANT 145 145 R -> G (in CMH7; dbSNP:rs104894724).
{ECO:0000269|PubMed:9241277}.
/FTId=VAR_007603.
VARIANT 145 145 R -> W (in RCM1; dbSNP:rs28934871).
{ECO:0000269|PubMed:12531876}.
/FTId=VAR_016080.
VARIANT 157 157 A -> V (in CMH7; dbSNP:rs397516353).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019873.
VARIANT 162 162 R -> P (in CMH7; dbSNP:rs397516354).
{ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:16199542}.
/FTId=VAR_019874.
VARIANT 162 162 R -> Q (in CMH7; dbSNP:rs397516354).
{ECO:0000269|PubMed:16199542}.
/FTId=VAR_042745.
VARIANT 166 166 S -> F (in CMH7; dbSNP:rs727504242).
{ECO:0000269|PubMed:12974739}.
/FTId=VAR_029454.
VARIANT 171 171 A -> T (in RCM1; dbSNP:rs121917761).
{ECO:0000269|PubMed:12531876}.
/FTId=VAR_016081.
VARIANT 177 177 Missing (in CMH7).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019875.
VARIANT 178 178 K -> E (in RCM1; dbSNP:rs28934870).
{ECO:0000269|PubMed:12531876}.
/FTId=VAR_016082.
VARIANT 185 185 N -> K (in CMD1FF; dbSNP:rs267607129).
{ECO:0000269|PubMed:19590045}.
/FTId=VAR_063549.
VARIANT 186 186 R -> Q (in CMH7; dbSNP:rs397516357).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019876.
VARIANT 190 190 D -> H (in CMH7 and RCM1).
{ECO:0000269|PubMed:12531876}.
/FTId=VAR_016083.
VARIANT 192 192 R -> H (in RCM1; dbSNP:rs104894729).
{ECO:0000269|PubMed:12531876}.
/FTId=VAR_016084.
VARIANT 196 196 D -> N (in CMH7; dbSNP:rs104894727).
{ECO:0000269|PubMed:11815426,
ECO:0000269|PubMed:12707239}.
/FTId=VAR_016085.
VARIANT 204 204 R -> H (in CMH7; dbSNP:rs727504275).
{ECO:0000269|PubMed:16199542}.
/FTId=VAR_042746.
VARIANT 206 206 K -> Q (in CMH7; dbSNP:rs104894725).
{ECO:0000269|PubMed:9241277}.
/FTId=VAR_007604.
HELIX 43 79 {ECO:0000244|PDB:4Y99}.
HELIX 85 87 {ECO:0000244|PDB:1J1E}.
HELIX 90 136 {ECO:0000244|PDB:4Y99}.
HELIX 151 159 {ECO:0000244|PDB:4Y99}.
HELIX 160 162 {ECO:0000244|PDB:4Y99}.
HELIX 163 188 {ECO:0000244|PDB:1J1E}.
SEQUENCE 210 AA; 24008 MW; 20A804F8C24AE1B0 CRC64;
MADGSSDAAR EPRPAPAPIR RRSSNYRAYA TEPHAKKKSK ISASRKLQLK TLLLQIAKQE
LEREAEERRG EKGRALSTRC QPLELAGLGF AELQDLCRQL HARVDKVDEE RYDIEAKVTK
NITEIADLTQ KIFDLRGKFK RPTLRRVRIS ADAMMQALLG ARAKESLDLR AHLKQVKKED
TEKENREVGD WRKNIDALSG MEGRKKKFES


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