TRIM2_HUMAN
ID TRIM2_HUMAN Reviewed; 744 AA.
AC Q9C040; D3DP09; O60272; Q9BSI9; Q9UFZ1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Tripartite motif-containing protein 2;
DE EC=2.3.2.27;
DE AltName: Full=E3 ubiquitin-protein ligase TRIM2;
DE AltName: Full=RING finger protein 86;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM2 {ECO:0000305};
GN Name=TRIM2; Synonyms=KIAA0517, RNF86;
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).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 516-744.
RC TISSUE=Fetal kidney;
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 [7]
RP INTERACTION WITH BCL2L11.
RX PubMed=21478148; DOI=10.1074/jbc.m110.197707;
RA Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P.,
RA Henshall D.C., Morris K.T., Simon R.P., Meller R.;
RT "Identification of a novel Bcl-2-interacting mediator of cell death (Bim)
RT E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in
RT rapid ischemic tolerance-induced neuroprotection.";
RL J. Biol. Chem. 286:19331-19339(2011).
RN [8]
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 [9]
RP VARIANT CMT2R VAL-227, AND CHARACTERIZATION OF VARIANT CMT2R VAL-227.
RX PubMed=23562820; DOI=10.1093/hmg/ddt149;
RA Ylikallio E., Poeyhoenen R., Zimon M., De Vriendt E., Hilander T.,
RA Paetau A., Jordanova A., Loennqvist T., Tyynismaa H.;
RT "Deficiency of the E3 ubiquitin ligase TRIM2 in early-onset axonal
RT neuropathy.";
RL Hum. Mol. Genet. 22:2975-2983(2013).
CC -!- FUNCTION: UBE2D1-dependent E3 ubiquitin-protein ligase that mediates
CC the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a
CC neuroprotective function. May play a role in neuronal rapid ischemic
CC tolerance. {ECO:0000250|UniProtKB:Q9ESN6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with myosin V; myosin V may not be a substrate for
CC ubiquitination (By similarity). Interacts with NEFL (By similarity).
CC Interacts with phosphorylated BCL2L11. {ECO:0000250|UniProtKB:Q9ESN6,
CC ECO:0000269|PubMed:21478148}.
CC -!- INTERACTION:
CC Q9C040; Q8IZL9: CDK20; NbExp=3; IntAct=EBI-749840, EBI-6128565;
CC Q9C040; Q96Q77: CIB3; NbExp=6; IntAct=EBI-749840, EBI-10292696;
CC Q9C040; Q96JB2-2: COG3; NbExp=3; IntAct=EBI-749840, EBI-9091495;
CC Q9C040; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-749840, EBI-11954971;
CC Q9C040; Q6NSJ5: LRRC8E; NbExp=6; IntAct=EBI-749840, EBI-8647013;
CC Q9C040; O75382: TRIM3; NbExp=4; IntAct=EBI-749840, EBI-2129889;
CC Q9C040; Q9BSL1: UBAC1; NbExp=10; IntAct=EBI-749840, EBI-749370;
CC Q9C040; P61086: UBE2K; NbExp=3; IntAct=EBI-749840, EBI-473850;
CC Q9C040; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-749840, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C040-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C040-2; Sequence=VSP_046923;
CC -!- DOMAIN: The interaction with myosin V is dependent upon its NHL
CC repeats, which form a beta-propeller (NHL) domain containing six
CC blades. {ECO:0000250|UniProtKB:Q9ESN6}.
CC -!- PTM: RING-type zinc finger-dependent and UBE2D1-dependent
CC autoubiquitination. {ECO:0000250|UniProtKB:Q9ESN6}.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2R (CMT2R) [MIM:615490]: An axonal
CC form of Charcot-Marie-Tooth disease, a disorder of the peripheral
CC nervous system, characterized by progressive weakness and atrophy,
CC initially of the peroneal muscles and later of the distal muscles of
CC the arms. Charcot-Marie-Tooth disease is classified in two main groups
CC on the basis of electrophysiologic properties and histopathology:
CC primary peripheral demyelinating neuropathies (designated CMT1 when
CC they are dominantly inherited) and primary peripheral axonal
CC neuropathies (CMT2). Neuropathies of the CMT2 group are characterized
CC by signs of axonal degeneration in the absence of obvious myelin
CC alterations, normal or slightly reduced nerve conduction velocities,
CC and progressive distal muscle weakness and atrophy.
CC {ECO:0000269|PubMed:23562820}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG53472.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA25443.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF220018; AAG53472.1; ALT_INIT; mRNA.
DR EMBL; AB011089; BAA25443.1; ALT_INIT; mRNA.
DR EMBL; AC013477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04960.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04962.1; -; Genomic_DNA.
DR EMBL; BC005016; AAH05016.1; -; mRNA.
DR EMBL; BC011052; AAH11052.1; -; mRNA.
DR EMBL; AL110234; CAB53687.2; -; mRNA.
DR CCDS; CCDS3781.2; -. [Q9C040-2]
DR CCDS; CCDS47147.1; -. [Q9C040-1]
DR PIR; T00082; T00082.
DR RefSeq; NP_001123539.1; NM_001130067.1. [Q9C040-1]
DR RefSeq; NP_056086.2; NM_015271.4. [Q9C040-2]
DR RefSeq; XP_016863433.1; XM_017007944.1. [Q9C040-1]
DR RefSeq; XP_016863434.1; XM_017007945.1.
DR RefSeq; XP_016863437.1; XM_017007948.1. [Q9C040-1]
DR RefSeq; XP_016863438.1; XM_017007949.1. [Q9C040-1]
DR RefSeq; XP_016863439.1; XM_017007950.1. [Q9C040-1]
DR RefSeq; XP_016863440.1; XM_017007951.1.
DR RefSeq; XP_016863441.1; XM_017007952.1.
DR PDB; 7B2R; X-ray; 1.60 A; A/B=466-740.
DR PDB; 7B96; X-ray; 1.80 A; A/B=469-744.
DR PDBsum; 7B2R; -.
DR PDBsum; 7B96; -.
DR AlphaFoldDB; Q9C040; -.
DR SMR; Q9C040; -.
DR BioGRID; 116910; 45.
DR IntAct; Q9C040; 34.
DR MINT; Q9C040; -.
DR STRING; 9606.ENSP00000339659; -.
DR iPTMnet; Q9C040; -.
DR PhosphoSitePlus; Q9C040; -.
DR BioMuta; TRIM2; -.
DR DMDM; 21363034; -.
DR EPD; Q9C040; -.
DR jPOST; Q9C040; -.
DR MassIVE; Q9C040; -.
DR MaxQB; Q9C040; -.
DR PaxDb; Q9C040; -.
DR PeptideAtlas; Q9C040; -.
DR PRIDE; Q9C040; -.
DR ProteomicsDB; 79960; -. [Q9C040-1]
DR Antibodypedia; 27852; 358 antibodies from 31 providers.
DR DNASU; 23321; -.
DR Ensembl; ENST00000338700.10; ENSP00000339659.5; ENSG00000109654.16. [Q9C040-2]
DR Ensembl; ENST00000437508.7; ENSP00000415812.2; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000674874.1; ENSP00000502519.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000674876.1; ENSP00000501652.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000674976.1; ENSP00000502356.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000675054.1; ENSP00000502543.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000675159.1; ENSP00000501792.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000675293.1; ENSP00000502348.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000675315.1; ENSP00000502676.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000675384.1; ENSP00000502114.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000675745.1; ENSP00000501662.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000675835.1; ENSP00000501951.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000676172.1; ENSP00000501822.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000676252.1; ENSP00000501586.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000676264.1; ENSP00000502089.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000676348.1; ENSP00000502159.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000676374.1; ENSP00000502273.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000676423.1; ENSP00000501612.1; ENSG00000109654.16. [Q9C040-1]
DR Ensembl; ENST00000676458.1; ENSP00000501994.1; ENSG00000109654.16. [Q9C040-1]
DR GeneID; 23321; -.
DR KEGG; hsa:23321; -.
DR MANE-Select; ENST00000338700.10; ENSP00000339659.5; NM_015271.5; NP_056086.2. [Q9C040-2]
DR UCSC; uc003ing.3; human. [Q9C040-1]
DR CTD; 23321; -.
DR DisGeNET; 23321; -.
DR GeneCards; TRIM2; -.
DR GeneReviews; TRIM2; -.
DR HGNC; HGNC:15974; TRIM2.
DR HPA; ENSG00000109654; Tissue enhanced (brain).
DR MalaCards; TRIM2; -.
DR MIM; 614141; gene.
DR MIM; 615490; phenotype.
DR neXtProt; NX_Q9C040; -.
DR OpenTargets; ENSG00000109654; -.
DR Orphanet; 397968; Charcot-Marie-Tooth disease type 2R.
DR PharmGKB; PA38070; -.
DR VEuPathDB; HostDB:ENSG00000109654; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155905; -.
DR HOGENOM; CLU_008645_5_0_1; -.
DR InParanoid; Q9C040; -.
DR OMA; CTSGEHR; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q9C040; -.
DR TreeFam; TF331018; -.
DR PathwayCommons; Q9C040; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9C040; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23321; 11 hits in 1114 CRISPR screens.
DR ChiTaRS; TRIM2; human.
DR GenomeRNAi; 23321; -.
DR Pharos; Q9C040; Tbio.
DR PRO; PR:Q9C040; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9C040; protein.
DR Bgee; ENSG00000109654; Expressed in inferior olivary complex and 207 other tissues.
DR ExpressionAtlas; Q9C040; baseline and differential.
DR Genevisible; Q9C040; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Charcot-Marie-Tooth disease; Cytoplasm;
KW Disease variant; Metal-binding; Neurodegeneration; Neuropathy;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..744
FT /note="Tripartite motif-containing protein 2"
FT /id="PRO_0000056195"
FT REPEAT 320..421
FT /note="Filamin"
FT REPEAT 473..516
FT /note="NHL 1"
FT REPEAT 520..563
FT /note="NHL 2"
FT REPEAT 564..605
FT /note="NHL 3"
FT REPEAT 609..652
FT /note="NHL 4"
FT REPEAT 656..699
FT /note="NHL 5"
FT REPEAT 700..743
FT /note="NHL 6"
FT ZN_FING 23..64
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 113..154
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 432..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZQG6"
FT MOD_RES 371
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT VAR_SEQ 1
FT /note="M -> MHRSGRYGTQQQRAGSKTAGPPCQWSRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:9628581"
FT /id="VSP_046923"
FT VARIANT 227
FT /note="E -> V (in CMT2R; reduced stability of the mutant
FT protein; dbSNP:rs587777063)"
FT /evidence="ECO:0000269|PubMed:23562820"
FT /id="VAR_070874"
FT CONFLICT 737..744
FT /note="FKVYRYLQ -> LILIYSRHLFFYESKC (in Ref. 5; AAH05016)"
FT /evidence="ECO:0000305"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 485..494
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:7B2R"
FT TURN 505..508
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 533..541
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:7B2R"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:7B2R"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 576..583
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 589..593
FT /evidence="ECO:0007829|PDB:7B2R"
FT TURN 594..597
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 622..630
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 636..640
FT /evidence="ECO:0007829|PDB:7B2R"
FT HELIX 641..643
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 655..659
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 669..677
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 683..687
FT /evidence="ECO:0007829|PDB:7B2R"
FT TURN 688..691
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 692..696
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 714..721
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 727..731
FT /evidence="ECO:0007829|PDB:7B2R"
FT HELIX 732..734
FT /evidence="ECO:0007829|PDB:7B2R"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:7B2R"
SQ SEQUENCE 744 AA; 81530 MW; B69A5876188B1A27 CRC64;
MASEGTNIPS PVVRQIDKQF LICSICLERY KNPKVLPCLH TFCERCLQNY IPAHSLTLSC
PVCRQTSILP EKGVAALQNN FFITNLMDVL QRTPGSNAEE SSILETVTAV AAGKPLSCPN
HDGNVMEFYC QSCETAMCRE CTEGEHAEHP TVPLKDVVEQ HKASLQVQLD AVNKRLPEID
SALQFISEII HQLTNQKASI VDDIHSTFDE LQKTLNVRKS VLLMELEVNY GLKHKVLQSQ
LDTLLQGQES IKSCSNFTAQ ALNHGTETEV LLVKKQMSEK LNELADQDFP LHPRENDQLD
FIVETEGLKK SIHNLGTILT TNAVASETVA TGEGLRQTII GQPMSVTITT KDKDGELCKT
GNAYLTAELS TPDGSVADGE ILDNKNGTYE FLYTVQKEGD FTLSLRLYDQ HIRGSPFKLK
VIRSADVSPT TEGVKRRVKS PGSGHVKQKA VKRPASMYST GKRKENPIED DLIFRVGTKG
RNKGEFTNLQ GVAASTNGKI LIADSNNQCV QIFSNDGQFK SRFGIRGRSP GQLQRPTGVA
VHPSGDIIIA DYDNKWVSIF SSDGKFKTKI GSGKLMGPKG VSVDRNGHII VVDNKACCVF
IFQPNGKIVT RFGSRGNGDR QFAGPHFAAV NSNNEIIITD FHNHSVKVFN QEGEFMLKFG
SNGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDGSG SFLSYINTSA DPLYGPQGLA
LTSDGHVVVA DSGNHCFKVY RYLQ
