TNNT3_HUMAN
ID TNNT3_HUMAN Reviewed; 269 AA.
AC P45378; A8MQ76; A8MSW1; B3KPX3; B7WP64; B7ZL26; B7ZVV9; Q12975; Q12976;
AC Q12977; Q12978; Q17RG9; Q6FH29; Q6N056; Q86TH6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Troponin T, fast skeletal muscle;
DE Short=TnTf;
DE AltName: Full=Beta-TnTF;
DE AltName: Full=Fast skeletal muscle troponin T;
DE Short=fTnT;
GN Name=TNNT3;
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 2).
RC TISSUE=Fetal skeletal muscle;
RX PubMed=8172653; DOI=10.1089/dna.1994.13.217;
RA Wu Q.-L., Jha P.K., Raychowdhury M.K., Du Y., Leavis P.C., Sarkar S.;
RT "Isolation and characterization of human fast skeletal beta troponin T
RT cDNA: comparative sequence analysis of isoforms and insight into the
RT evolution of members of a multigene family.";
RL DNA Cell Biol. 13:217-233(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Stefancsik R., Mao C., Randall J., Jha P.K., Sarkar S.;
RT "Genomic structure of the fast skeletal troponin T gene (TNNT3).";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Skeletal muscle;
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 MRNA] (ISOFORM 7).
RA Li H., Nong W., Zhou G., Ke R., Shen C., Liang M., Tang Z., Huang B.,
RA Lin L., Yang S.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 6 AND 7).
RC TISSUE=Lung;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-67 (ISOFORMS 1; 2; 3; 4 AND 5).
RC TISSUE=Skeletal muscle;
RX PubMed=8062920; DOI=10.1016/0014-5793(94)00729-2;
RA Briggs M.M., Maready M., Schmidt J.M., Schachat F.;
RT "Identification of a fetal exon in the human fast troponin T gene.";
RL FEBS Lett. 350:37-40(1994).
RN [11]
RP INVOLVEMENT IN DA2B2, AND VARIANT DA2B2 HIS-74.
RX PubMed=12865991; DOI=10.1086/376418;
RA Sung S.S., Brassington A.-M.E., Krakowiak P.A., Carey J.C., Jorde L.B.,
RA Bamshad M.;
RT "Mutations in TNNT3 cause multiple congenital contractures: a second locus
RT for distal arthrogryposis type 2B.";
RL Am. J. Hum. Genet. 73:212-214(2003).
RN [12]
RP INVOLVEMENT IN DA2B2, AND VARIANT DA2B2 HIS-74.
RX PubMed=19142688; DOI=10.1007/s11999-008-0694-5;
RA Gurnett C.A., Alaee F., Desruisseau D., Boehm S., Dobbs M.B.;
RT "Skeletal muscle contractile gene (TNNT3, MYH3, TPM2) mutations not found
RT in vertical talus or clubfoot.";
RL Clin. Orthop. Relat. Res. 467:1195-1200(2009).
RN [13]
RP INVOLVEMENT IN DA2B2, AND VARIANT DA2B2 CYS-74.
RX PubMed=21402185; DOI=10.1016/j.ejmg.2011.03.002;
RA Zhao N., Jiang M., Han W., Bian C., Li X., Huang F., Kong Q., Li J.;
RT "A novel mutation in TNNT3 associated with Sheldon-Hall syndrome in a
RT Chinese family with vertical talus.";
RL Eur. J. Med. Genet. 54:351-353(2011).
RN [14]
RP INVOLVEMENT IN DA2B2, AND VARIANT DA2B2 HIS-74.
RX PubMed=25337069; DOI=10.1159/000365057;
RA Daly S.B., Shah H., O'Sullivan J., Anderson B., Bhaskar S., Williams S.,
RA Al-Sheqaih N., Mueed Bidchol A., Banka S., Newman W.G., Girisha K.M.;
RT "Exome sequencing identifies a dominant TNNT3 mutation in a large family
RT with distal arthrogryposis.";
RL Mol. Syndromol. 5:218-228(2014).
CC -!- FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin,
CC the thin filament regulatory complex which confers calcium-sensitivity
CC to striated muscle actomyosin ATPase activity.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Tnt1;
CC IsoId=P45378-1; Sequence=Displayed;
CC Name=2; Synonyms=Tnt3;
CC IsoId=P45378-2; Sequence=VSP_007914;
CC Name=3; Synonyms=Tnt1f;
CC IsoId=P45378-3; Sequence=VSP_007915;
CC Name=4; Synonyms=Tnt3f;
CC IsoId=P45378-4; Sequence=VSP_007914, VSP_007915, VSP_007916;
CC Name=5; Synonyms=Tnt3f*;
CC IsoId=P45378-5; Sequence=VSP_009121;
CC Name=6;
CC IsoId=P45378-6; Sequence=VSP_034964;
CC Name=7;
CC IsoId=P45378-7; Sequence=VSP_007914, VSP_007915;
CC -!- TISSUE SPECIFICITY: In fetal and adult fast skeletal muscles, with a
CC higher level expression in fetal than in adult muscle.
CC -!- DISEASE: Arthrogryposis, distal, 2B2 (DA2B2) [MIM:618435]: A form of
CC distal arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. Distal
CC arthrogryposis type 2 is characterized by contractures of the hands and
CC feet, and a distinctive face characterized by prominent nasolabial
CC folds, small mouth and downslanting palpebral fissures. DA2B2
CC inheritance is autosomal dominant. {ECO:0000269|PubMed:12865991,
CC ECO:0000269|PubMed:19142688, ECO:0000269|PubMed:21402185,
CC ECO:0000269|PubMed:25337069}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 5]: Minor isoform detected in approximately 1%
CC of cDNA clones. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M21984; AAA36777.1; -; mRNA.
DR EMBL; AF026276; AAF21629.1; -; Genomic_DNA.
DR EMBL; AK056968; BAG51835.1; -; mRNA.
DR EMBL; DQ778624; ABG77458.1; -; mRNA.
DR EMBL; BX640689; CAE45814.1; -; mRNA.
DR EMBL; BT019997; AAV38800.1; -; mRNA.
DR EMBL; CR541927; CAG46725.1; -; mRNA.
DR EMBL; AC051649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050446; AAH50446.1; ALT_INIT; mRNA.
DR EMBL; BC117327; AAI17328.1; -; mRNA.
DR EMBL; BC171727; AAI71727.1; -; mRNA.
DR EMBL; BC143537; AAI43538.1; -; mRNA.
DR EMBL; U14641; AAA50359.1; -; mRNA.
DR EMBL; U14642; AAA50360.1; -; mRNA.
DR EMBL; U14643; AAA50361.1; -; mRNA.
DR EMBL; U14644; AAA50362.1; -; mRNA.
DR CCDS; CCDS41594.1; -. [P45378-6]
DR CCDS; CCDS41595.1; -. [P45378-4]
DR CCDS; CCDS41596.1; -. [P45378-7]
DR CCDS; CCDS7727.1; -. [P45378-2]
DR CCDS; CCDS86164.1; -. [P45378-3]
DR PIR; I53021; I53021.
DR PIR; S48660; S48660.
DR PIR; S74259; S74259.
DR PIR; S74260; S74260.
DR PIR; S74261; S74261.
DR RefSeq; NP_001036245.1; NM_001042780.2. [P45378-4]
DR RefSeq; NP_001036246.1; NM_001042781.2. [P45378-6]
DR RefSeq; NP_001036247.1; NM_001042782.2. [P45378-7]
DR RefSeq; NP_001284575.1; NM_001297646.1. [P45378-7]
DR RefSeq; NP_006748.1; NM_006757.3. [P45378-2]
DR RefSeq; XP_006718353.1; XM_006718290.3.
DR RefSeq; XP_006718356.1; XM_006718293.2.
DR RefSeq; XP_006718363.1; XM_006718300.3. [P45378-5]
DR RefSeq; XP_011518645.1; XM_011520343.2. [P45378-1]
DR RefSeq; XP_016873695.1; XM_017018206.1. [P45378-1]
DR AlphaFoldDB; P45378; -.
DR BMRB; P45378; -.
DR BioGRID; 112994; 31.
DR IntAct; P45378; 9.
DR MINT; P45378; -.
DR STRING; 9606.ENSP00000278317; -.
DR ChEMBL; CHEMBL3831282; -.
DR iPTMnet; P45378; -.
DR PhosphoSitePlus; P45378; -.
DR BioMuta; TNNT3; -.
DR DMDM; 33518637; -.
DR MassIVE; P45378; -.
DR PaxDb; P45378; -.
DR PeptideAtlas; P45378; -.
DR PRIDE; P45378; -.
DR ProteomicsDB; 55658; -. [P45378-1]
DR ProteomicsDB; 55659; -. [P45378-2]
DR ProteomicsDB; 55660; -. [P45378-3]
DR ProteomicsDB; 55661; -. [P45378-4]
DR ProteomicsDB; 55662; -. [P45378-5]
DR ProteomicsDB; 55663; -. [P45378-6]
DR ProteomicsDB; 55664; -. [P45378-7]
DR Antibodypedia; 22978; 288 antibodies from 31 providers.
DR DNASU; 7140; -.
DR Ensembl; ENST00000278317.11; ENSP00000278317.6; ENSG00000130595.19. [P45378-2]
DR Ensembl; ENST00000344578.8; ENSP00000344870.4; ENSG00000130595.19. [P45378-5]
DR Ensembl; ENST00000381558.6; ENSP00000370970.1; ENSG00000130595.19. [P45378-7]
DR Ensembl; ENST00000381563.8; ENSP00000370975.4; ENSG00000130595.19. [P45378-3]
DR Ensembl; ENST00000381579.7; ENSP00000370991.3; ENSG00000130595.19. [P45378-4]
DR Ensembl; ENST00000381589.7; ENSP00000371001.3; ENSG00000130595.19. [P45378-6]
DR Ensembl; ENST00000397301.5; ENSP00000380468.1; ENSG00000130595.19. [P45378-1]
DR Ensembl; ENST00000641119.1; ENSP00000492914.1; ENSG00000130595.19. [P45378-6]
DR Ensembl; ENST00000641787.1; ENSP00000493331.1; ENSG00000130595.19. [P45378-7]
DR Ensembl; ENST00000671850.1; ENSP00000500846.1; ENSG00000288250.1. [P45378-6]
DR Ensembl; ENST00000672214.1; ENSP00000500606.1; ENSG00000288250.1. [P45378-2]
DR Ensembl; ENST00000672629.1; ENSP00000500081.1; ENSG00000288250.1. [P45378-6]
DR Ensembl; ENST00000672659.1; ENSP00000500263.1; ENSG00000288250.1. [P45378-4]
DR Ensembl; ENST00000673082.1; ENSP00000500796.1; ENSG00000288250.1. [P45378-1]
DR Ensembl; ENST00000673157.1; ENSP00000499917.1; ENSG00000288250.1. [P45378-7]
DR Ensembl; ENST00000673174.1; ENSP00000500437.1; ENSG00000288250.1. [P45378-5]
DR Ensembl; ENST00000673503.1; ENSP00000500156.1; ENSG00000288250.1. [P45378-7]
DR Ensembl; ENST00000673572.1; ENSP00000500705.1; ENSG00000288250.1. [P45378-3]
DR GeneID; 7140; -.
DR KEGG; hsa:7140; -.
DR MANE-Select; ENST00000278317.11; ENSP00000278317.6; NM_006757.4; NP_006748.1. [P45378-2]
DR UCSC; uc001luo.5; human. [P45378-1]
DR CTD; 7140; -.
DR DisGeNET; 7140; -.
DR GeneCards; TNNT3; -.
DR HGNC; HGNC:11950; TNNT3.
DR HPA; ENSG00000130595; Group enriched (skeletal muscle, tongue).
DR MalaCards; TNNT3; -.
DR MIM; 600692; gene.
DR MIM; 618435; phenotype.
DR neXtProt; NX_P45378; -.
DR OpenTargets; ENSG00000130595; -.
DR Orphanet; 1146; Distal arthrogryposis type 1.
DR Orphanet; 1147; Sheldon-Hall syndrome.
DR PharmGKB; PA36639; -.
DR VEuPathDB; HostDB:ENSG00000130595; -.
DR eggNOG; KOG3634; Eukaryota.
DR GeneTree; ENSGT00940000158477; -.
DR HOGENOM; CLU_076377_2_0_1; -.
DR InParanoid; P45378; -.
DR OMA; EAKTVFM; -.
DR OrthoDB; 1013139at2759; -.
DR PhylomeDB; P45378; -.
DR TreeFam; TF313321; -.
DR PathwayCommons; P45378; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P45378; -.
DR SIGNOR; P45378; -.
DR BioGRID-ORCS; 7140; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; TNNT3; human.
DR GeneWiki; TNNT3; -.
DR GenomeRNAi; 7140; -.
DR Pharos; P45378; Tbio.
DR PRO; PR:P45378; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P45378; protein.
DR Bgee; ENSG00000130595; Expressed in hindlimb stylopod muscle and 92 other tissues.
DR ExpressionAtlas; P45378; baseline and differential.
DR Genevisible; P45378; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005861; C:troponin complex; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0005523; F:tropomyosin binding; IMP:UniProtKB.
DR GO; GO:0030172; F:troponin C binding; IPI:UniProtKB.
DR GO; GO:0031013; F:troponin I binding; IPI:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:1903612; P:positive regulation of calcium-dependent ATPase activity; IDA:UniProtKB.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0006942; P:regulation of striated muscle contraction; IDA:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IDA:UniProtKB.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR027707; TNNT.
DR InterPro; IPR027708; Tnnt3.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR038077; Troponin_sf.
DR PANTHER; PTHR11521; PTHR11521; 1.
DR PANTHER; PTHR11521:SF4; PTHR11521:SF4; 1.
DR Pfam; PF00992; Troponin; 1.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; Muscle protein;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02641"
FT CHAIN 2..269
FT /note="Troponin T, fast skeletal muscle"
FT /id="PRO_0000186178"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P02641"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09739"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09739"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ47"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09739"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09739"
FT VAR_SEQ 23..46
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:8062920"
FT /id="VSP_009121"
FT VAR_SEQ 23..33
FT /note="Missing (in isoform 2, isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8062920,
FT ECO:0000303|PubMed:8172653, ECO:0000303|Ref.4"
FT /id="VSP_007914"
FT VAR_SEQ 34..46
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.6,
FT ECO:0000303|Ref.7"
FT /id="VSP_034964"
FT VAR_SEQ 39..46
FT /note="Missing (in isoform 3, isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8062920,
FT ECO:0000303|Ref.4"
FT /id="VSP_007915"
FT VAR_SEQ 240..252
FT /note="TTLRSRIDQAQKH -> MNVRARVQMLAKF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8062920"
FT /id="VSP_007916"
FT VARIANT 74
FT /note="R -> C (in DA2B2; dbSNP:rs199474721)"
FT /evidence="ECO:0000269|PubMed:21402185"
FT /id="VAR_082280"
FT VARIANT 74
FT /note="R -> H (in DA2B2; dbSNP:rs121434638)"
FT /evidence="ECO:0000269|PubMed:12865991,
FT ECO:0000269|PubMed:19142688, ECO:0000269|PubMed:25337069"
FT /id="VAR_026453"
FT CONFLICT 149
FT /note="E -> G (in Ref. 5; CAE45814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 31825 MW; 87B25AF8773D742F CRC64;
MSDEEVEQVE EQYEEEEEAQ EEAAEVHEEV HEPEEVQEDT AEEDAEEEKP RPKLTAPKIP
EGEKVDFDDI QKKRQNKDLM ELQALIDSHF EARKKEEEEL VALKERIEKR RAERAEQQRI
RAEKERERQN RLAEEKARRE EEDAKRRAED DLKKKKALSS MGANYSSYLA KADQKRGKKQ
TAREMKKKIL AERRKPLNID HLGEDKLRDK AKELWETLHQ LEIDKFEFGE KLKRQKYDIT
TLRSRIDQAQ KHSKKAGTPA KGKVGGRWK