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E3 ubiquitin-protein ligase TRIM32 (EC 2.3.2.27) (72 kDa Tat-interacting protein) (RING-type E3 ubiquitin transferase TRIM32) (Tripartite motif-containing protein 32) (Zinc finger protein HT2A)

 TRI32_HUMAN             Reviewed;         653 AA.
Q13049; Q9NQP8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
25-OCT-2017, entry version 191.
RecName: Full=E3 ubiquitin-protein ligase TRIM32;
EC=2.3.2.27;
AltName: Full=72 kDa Tat-interacting protein;
AltName: Full=RING-type E3 ubiquitin transferase TRIM32 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 32;
AltName: Full=Zinc finger protein HT2A;
Name=TRIM32; Synonyms=HT2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7778269; DOI=10.1006/viro.1995.1266;
Fridell R.A., Harding L.S., Bogerd H.P., Cullen B.R.;
"Identification of a novel human zinc finger protein that specifically
interacts with the activation domain of lentiviral Tat proteins.";
Virology 209:347-357(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-15; 51-60; 70-101; 205-238; 248-282; 345-359;
467-500; 587-596 AND 605-613, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, UBIQUITINATION,
SELF-ASSOCIATION, AND INTERACTION WITH DTNBP1.
PubMed=19349376; DOI=10.1093/hmg/ddp167;
Locke M., Tinsley C.L., Benson M.A., Blake D.J.;
"TRIM32 is an E3 ubiquitin ligase for dysbindin.";
Hum. Mol. Genet. 18:2344-2358(2009).
[7]
FUNCTION.
PubMed=22500027; DOI=10.1074/jbc.M112.341487;
Zhang Q., Yu D., Seo S., Stone E.M., Sheffield V.C.;
"Intrinsic protein-protein interaction-mediated and chaperonin-
assisted sequential assembly of stable Bardet-Biedl syndrome protein
complex, the BBSome.";
J. Biol. Chem. 287:20625-20635(2012).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-339, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
STRUCTURE BY NMR OF 10-84.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RING domain of the tripartite motif protein
32.";
Submitted (NOV-2005) to the PDB data bank.
[10]
VARIANT LGMD2H ASN-487, AND TISSUE SPECIFICITY.
PubMed=11822024; DOI=10.1086/339083;
Frosk P., Weiler T., Nylen E., Sudha T., Greenberg C.R., Morgan K.,
Fujiwara T.M., Wrogemann K.;
"Limb-girdle muscular dystrophy type 2H associated with mutation in
TRIM32, a putative E3-ubiquitin-ligase gene.";
Am. J. Hum. Genet. 70:663-672(2002).
[11]
VARIANT BBS11 SER-130.
PubMed=16606853; DOI=10.1073/pnas.0600158103;
Chiang A.P., Beck J.S., Yen H.-J., Tayeh M.K., Scheetz T.E.,
Swiderski R.E., Nishimura D.Y., Braun T.A., Kim K.-Y.A., Huang J.,
Elbedour K., Carmi R., Slusarski D.C., Casavant T.L., Stone E.M.,
Sheffield V.C.;
"Homozygosity mapping with SNP arrays identifies TRIM32, an E3
ubiquitin ligase, as a Bardet-Biedl syndrome gene (BBS11).";
Proc. Natl. Acad. Sci. U.S.A. 103:6287-6292(2006).
[12]
VARIANTS LGMD2H HIS-394 AND ASP-588 DEL.
PubMed=17994549; DOI=10.1002/humu.20633;
Saccone V., Palmieri M., Passamano L., Piluso G., Meroni G.,
Politano L., Nigro V.;
"Mutations that impair interaction properties of TRIM32 associated
with limb-girdle muscular dystrophy 2H.";
Hum. Mutat. 29:240-247(2008).
[13]
VARIANT GLN-299.
PubMed=21344540; DOI=10.1002/humu.21480;
Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R.,
Vincent A., Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I.,
Fishman G.A., Chitayat D., Knueppel T., Millan J.M., Munier F.L.,
Kennedy D., Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K.,
Heon E.;
"BBS genotype-phenotype assessment of a multiethnic patient cohort
calls for a revision of the disease definition.";
Hum. Mutat. 32:610-619(2011).
-!- FUNCTION: Has an E3 ubiquitin ligase activity. Ubiquitinates
DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate
BBS2. May play a significant role in mediating the biological
activity of the HIV-1 Tat protein in vivo. Binds specifically to
the activation domain of HIV-1 Tat and can also interact with the
HIV-2 and EIAV Tat proteins in vivo. {ECO:0000269|PubMed:19349376,
ECO:0000269|PubMed:22500027}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with DTNBP1. It self-associates.
{ECO:0000269|PubMed:19349376}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-742790, EBI-742790;
B3KPU6:-; NbExp=3; IntAct=EBI-742790, EBI-10175879;
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-742790, EBI-743598;
Q9NYB9-2:ABI2; NbExp=6; IntAct=EBI-742790, EBI-11096309;
P54253:ATXN1; NbExp=2; IntAct=EBI-742790, EBI-930964;
Q8N3C7:CLIP4; NbExp=5; IntAct=EBI-742790, EBI-5655540;
Q99J34:Irak1 (xeno); NbExp=2; IntAct=EBI-742790, EBI-6117042;
Q7L273:KCTD9; NbExp=5; IntAct=EBI-742790, EBI-4397613;
O76083:PDE9A; NbExp=6; IntAct=EBI-742790, EBI-742764;
O76083-2:PDE9A; NbExp=8; IntAct=EBI-742790, EBI-11524542;
Q9HAT8:PELI2; NbExp=4; IntAct=EBI-742790, EBI-448407;
Q06124:PTPN11; NbExp=3; IntAct=EBI-742790, EBI-297779;
Q9UI14:RABAC1; NbExp=9; IntAct=EBI-742790, EBI-712367;
P11684:SCGB1A1; NbExp=6; IntAct=EBI-742790, EBI-7797649;
O00560:SDCBP; NbExp=5; IntAct=EBI-742790, EBI-727004;
Q5T7P8-2:SYT6; NbExp=5; IntAct=EBI-742790, EBI-10246152;
Q9C035:TRIM5; NbExp=2; IntAct=EBI-742790, EBI-924214;
P61088:UBE2N; NbExp=3; IntAct=EBI-742790, EBI-1052908;
Q5VVX9:UBE2U; NbExp=4; IntAct=EBI-742790, EBI-2130181;
Q13404:UBE2V1; NbExp=3; IntAct=EBI-742790, EBI-1050671;
Q9UMX0:UBQLN1; NbExp=8; IntAct=EBI-742790, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-742790, EBI-10173939;
Q9UHD9:UBQLN2; NbExp=4; IntAct=EBI-742790, EBI-947187;
Q9NRR5:UBQLN4; NbExp=3; IntAct=EBI-742790, EBI-711226;
-!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic
bodies, often located around the nucleus.
-!- TISSUE SPECIFICITY: Spleen, thymus, prostate, testis, ovary,
intestine, colon and skeletal muscle.
{ECO:0000269|PubMed:11822024}.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:19349376}.
-!- DISEASE: Limb-girdle muscular dystrophy 2H (LGMD2H) [MIM:254110]:
An autosomal recessive degenerative myopathy characterized by
pelvic girdle, shoulder girdle and quadriceps muscle weakness.
Clinical phenotype and severity are highly variable. Disease
progression is slow and most patients remain ambulatory into the
sixth decade of life. {ECO:0000269|PubMed:11822024,
ECO:0000269|PubMed:17994549}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Bardet-Biedl syndrome 11 (BBS11) [MIM:615988]: A syndrome
characterized by usually severe pigmentary retinopathy, early-
onset obesity, polydactyly, hypogenitalism, renal malformation and
mental retardation. Secondary features include diabetes mellitus,
hypertension and congenital heart disease. Bardet-Biedl syndrome
inheritance is autosomal recessive, but three mutated alleles (two
at one locus, and a third at a second locus) may be required for
clinical manifestation of some forms of the disease.
{ECO:0000269|PubMed:16606853}. Note=The disease is caused by
mutations affecting the gene represented in this entry. It has
been suggested that TRIM32 might be the E3 ubiquitin ligase for
BBS2, a component of the BBSome complex involved in ciliogenesis,
that is ubiquitinated and degraded by the proteasome
(PubMed:22500027). {ECO:0000269|PubMed:22500027}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Leiden Muscular Dystrophy pages; Note=TRIM32;
URL="http://www.dmd.nl/trim32_home.html";
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EMBL; U18543; AAA86474.1; -; mRNA.
EMBL; AL133284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003154; AAH03154.1; -; mRNA.
CCDS; CCDS6817.1; -.
RefSeq; NP_001093149.1; NM_001099679.1.
RefSeq; NP_036342.2; NM_012210.3.
RefSeq; XP_005251870.1; XM_005251813.3.
RefSeq; XP_011516700.1; XM_011518398.2.
RefSeq; XP_016869975.1; XM_017014486.1.
UniGene; Hs.591910; -.
PDB; 2CT2; NMR; -; A=10-84.
PDB; 5FEY; X-ray; 2.23 A; A/B=7-93.
PDBsum; 2CT2; -.
PDBsum; 5FEY; -.
ProteinModelPortal; Q13049; -.
SMR; Q13049; -.
BioGrid; 116608; 88.
CORUM; Q13049; -.
IntAct; Q13049; 51.
MINT; MINT-2854880; -.
STRING; 9606.ENSP00000363095; -.
iPTMnet; Q13049; -.
PhosphoSitePlus; Q13049; -.
BioMuta; TRIM32; -.
DMDM; 20178303; -.
EPD; Q13049; -.
MaxQB; Q13049; -.
PaxDb; Q13049; -.
PeptideAtlas; Q13049; -.
PRIDE; Q13049; -.
DNASU; 22954; -.
Ensembl; ENST00000373983; ENSP00000363095; ENSG00000119401.
Ensembl; ENST00000450136; ENSP00000408292; ENSG00000119401.
GeneID; 22954; -.
KEGG; hsa:22954; -.
UCSC; uc004bjw.3; human.
CTD; 22954; -.
DisGeNET; 22954; -.
EuPathDB; HostDB:ENSG00000119401.10; -.
GeneCards; TRIM32; -.
GeneReviews; TRIM32; -.
HGNC; HGNC:16380; TRIM32.
HPA; HPA050060; -.
MalaCards; TRIM32; -.
MIM; 254110; phenotype.
MIM; 602290; gene.
MIM; 615988; phenotype.
neXtProt; NX_Q13049; -.
OpenTargets; ENSG00000119401; -.
Orphanet; 1878; Autosomal recessive limb-girdle muscular dystrophy type 2H.
Orphanet; 110; Bardet-Biedl syndrome.
PharmGKB; PA38130; -.
eggNOG; ENOG410ITFD; Eukaryota.
eggNOG; ENOG410XRCH; LUCA.
GeneTree; ENSGT00900000141088; -.
HOGENOM; HOG000120114; -.
HOVERGEN; HBG060344; -.
InParanoid; Q13049; -.
KO; K10607; -.
OMA; CITGMCV; -.
OrthoDB; EOG091G0KUF; -.
PhylomeDB; Q13049; -.
TreeFam; TF331018; -.
Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q13049; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q13049; -.
GeneWiki; TRIM32; -.
GenomeRNAi; 22954; -.
PRO; PR:Q13049; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000119401; -.
CleanEx; HS_TRIM32; -.
ExpressionAtlas; Q13049; baseline and differential.
Genevisible; Q13049; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0005863; C:striated muscle myosin thick filament; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0017022; F:myosin binding; ISS:BHF-UCL.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; ISS:BHF-UCL.
GO; GO:0030957; F:Tat protein binding; TAS:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0031369; F:translation initiation factor binding; ISS:BHF-UCL.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007014; P:actin ubiquitination; IEA:Ensembl.
GO; GO:0061564; P:axon development; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IDA:BHF-UCL.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; IDA:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IDA:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:2000147; P:positive regulation of cell motility; ISS:BHF-UCL.
GO; GO:1903886; P:positive regulation of chemokine (C-C motif) ligand 20 production; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:1903883; P:positive regulation of interleukin-17-mediated signaling pathway; IEA:Ensembl.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:BHF-UCL.
GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:BHF-UCL.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IEA:Ensembl.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL.
GO; GO:0016567; P:protein ubiquitination; IDA:BHF-UCL.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
GO; GO:0034612; P:response to tumor necrosis factor; ISS:BHF-UCL.
GO; GO:0009411; P:response to UV; ISS:BHF-UCL.
GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
CDD; cd00021; BBOX; 1.
Gene3D; 2.120.10.30; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR001258; NHL_repeat.
InterPro; IPR013017; NHL_repeat_subgr.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF01436; NHL; 3.
Pfam; PF13445; zf-RING_UBOX; 1.
SMART; SM00336; BBOX; 1.
SMART; SM00184; RING; 1.
PROSITE; PS51125; NHL; 5.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Bardet-Biedl syndrome; Ciliopathy;
Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Limb-girdle muscular dystrophy; Mental retardation;
Metal-binding; Obesity; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.4}.
CHAIN 2 653 E3 ubiquitin-protein ligase TRIM32.
/FTId=PRO_0000056246.
REPEAT 358 401 NHL 1.
REPEAT 415 458 NHL 2.
REPEAT 459 499 NHL 3.
REPEAT 562 605 NHL 4.
REPEAT 606 646 NHL 5.
ZN_FING 20 65 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 103 133 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 138 197 {ECO:0000255}.
COMPBIAS 2 6 Poly-Ala.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.4}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CH72}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 130 130 P -> S (in BBS11; dbSNP:rs111033571).
{ECO:0000269|PubMed:16606853}.
/FTId=VAR_038807.
VARIANT 257 257 T -> R (in dbSNP:rs3747834).
/FTId=VAR_038808.
VARIANT 299 299 R -> Q (in a patient with Bardet-Biedl
syndrome; unknown pathological
significance; dbSNP:rs766439806).
{ECO:0000269|PubMed:21344540}.
/FTId=VAR_066295.
VARIANT 394 394 R -> H (in LGMD2H; dbSNP:rs121434447).
{ECO:0000269|PubMed:17994549}.
/FTId=VAR_042939.
VARIANT 408 408 R -> C (in dbSNP:rs3747835).
/FTId=VAR_038809.
VARIANT 487 487 D -> N (in LGMD2H; dbSNP:rs111033570).
{ECO:0000269|PubMed:11822024}.
/FTId=VAR_018725.
VARIANT 588 588 Missing (in LGMD2H).
{ECO:0000269|PubMed:17994549}.
/FTId=VAR_042940.
CONFLICT 27 27 F -> I (in Ref. 1; AAA86474).
{ECO:0000305}.
HELIX 11 16 {ECO:0000244|PDB:5FEY}.
TURN 21 23 {ECO:0000244|PDB:5FEY}.
STRAND 34 36 {ECO:0000244|PDB:5FEY}.
STRAND 38 40 {ECO:0000244|PDB:2CT2}.
STRAND 42 44 {ECO:0000244|PDB:5FEY}.
HELIX 45 51 {ECO:0000244|PDB:5FEY}.
STRAND 62 64 {ECO:0000244|PDB:5FEY}.
TURN 73 75 {ECO:0000244|PDB:2CT2}.
STRAND 76 78 {ECO:0000244|PDB:2CT2}.
HELIX 80 85 {ECO:0000244|PDB:5FEY}.
SEQUENCE 653 AA; 71989 MW; D83B1595CA8378FD CRC64;
MAAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK LLASSINGVR
CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC RSCGRRLPRQ FCRSCGLVLC
EPCREADHQP PGHCTLPVKE AAEERRRDFG EKLTRLRELM GELQRRKAAL EGVSKDLQAR
YKAVLQEYGH EERRVQDELA RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD
YFLAKIKQAD VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT
VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS NIQQCLFLKK
MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR KGFLKEIRRS PSGIDSFVLS
FLGADLPNLT PLSVAMNCQG LIGVTDSYDN SLKVYTLDGH CVACHRSQLS KPWGITALPS
GQFVVTDVEG GKLWCFTVDR GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR
QNEHHLEGGF SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL
HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY STP


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