TRIM3_HUMAN
ID TRIM3_HUMAN Reviewed; 744 AA.
AC O75382; B7Z5E6; F5H2Q8; Q4V9L4; Q9C038; Q9C039;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Tripartite motif-containing protein 3;
DE AltName: Full=Brain-expressed RING finger protein;
DE AltName: Full=RING finger protein 22;
DE AltName: Full=RING finger protein 97;
GN Name=TRIM3; Synonyms=BERP, RNF22, RNF97;
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 ALPHA).
RC TISSUE=Brain;
RX PubMed=11170753; DOI=10.1006/geno.2000.6452;
RA El-Husseini A.E.-D., Fretier P., Vincent S.R.;
RT "Cloning and characterization of a gene (RNF22) encoding a novel brain
RT expressed ring finger protein (BERP) that maps to human chromosome
RT 11p15.5.";
RL Genomics 71:363-367(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND 4).
RC TISSUE=Brain;
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=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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Cervix;
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 [7]
RP IDENTIFICATION IN THE CART COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=15772161; DOI=10.1091/mbc.e04-11-1014;
RA Yan Q., Sun W., Kujala P., Lotfi Y., Vida T.A., Bean A.J.;
RT "CART: an Hrs/actinin-4/BERP/myosin V protein complex required for
RT efficient receptor recycling.";
RL Mol. Biol. Cell 16:2470-2482(2005).
RN [8]
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP INTERACTION WITH ZFYVE28.
RX PubMed=19460345; DOI=10.1016/j.devcel.2009.03.015;
RA Mosesson Y., Chetrit D., Schley L., Berghoff J., Ziv T., Carvalho S.,
RA Milanezi F., Admon A., Schmitt F., Ehrlich M., Yarden Y.;
RT "Monoubiquitinylation regulates endosomal localization of Lst2, a negative
RT regulator of EGF receptor signaling.";
RL Dev. Cell 16:687-698(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-427, 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).
CC -!- FUNCTION: Probably involved in vesicular trafficking via its
CC association with the CART complex (PubMed:15772161). The CART complex
CC is necessary for efficient transferrin receptor recycling but not for
CC EGFR degradation (PubMed:15772161). Positively regulates motility of
CC microtubule-dependent motor protein KIF21B (By similarity).
CC {ECO:0000250|UniProtKB:Q9R1R2, ECO:0000269|PubMed:15772161}.
CC -!- SUBUNIT: Associates with myosin-Vb (MYO5B) and alpha-actinin-4 (ACTN4)
CC (By similarity). Component of the CART complex, at least composed of
CC ACTN4, HGS/HRS, MYO5B and TRIM3 (PubMed:15772161). Interacts with
CC ZFYVE28/LST2 (PubMed:19460345). Interacts with KIF21B (By similarity).
CC {ECO:0000250|UniProtKB:O70277, ECO:0000250|UniProtKB:Q9R1R2,
CC ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:19460345}.
CC -!- INTERACTION:
CC O75382; P04424: ASL; NbExp=3; IntAct=EBI-2129889, EBI-750131;
CC O75382; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2129889, EBI-739624;
CC O75382; P48730: CSNK1D; NbExp=3; IntAct=EBI-2129889, EBI-751621;
CC O75382; P49674: CSNK1E; NbExp=3; IntAct=EBI-2129889, EBI-749343;
CC O75382; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-2129889, EBI-11954971;
CC O75382; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2129889, EBI-739832;
CC O75382; Q6NSJ5: LRRC8E; NbExp=3; IntAct=EBI-2129889, EBI-8647013;
CC O75382; Q9ULV0-2: MYO5B; NbExp=3; IntAct=EBI-2129889, EBI-14093244;
CC O75382; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-2129889, EBI-1378139;
CC O75382; P28347-2: TEAD1; NbExp=3; IntAct=EBI-2129889, EBI-12151837;
CC O75382; Q15562-2: TEAD2; NbExp=3; IntAct=EBI-2129889, EBI-9370956;
CC O75382; Q9C040: TRIM2; NbExp=4; IntAct=EBI-2129889, EBI-749840;
CC O75382; P19474: TRIM21; NbExp=3; IntAct=EBI-2129889, EBI-81290;
CC O75382; O75382: TRIM3; NbExp=3; IntAct=EBI-2129889, EBI-2129889;
CC O75382; P51668: UBE2D1; NbExp=3; IntAct=EBI-2129889, EBI-743540;
CC O75382; Q96LR5: UBE2E2; NbExp=3; IntAct=EBI-2129889, EBI-2129763;
CC O75382; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-2129889, EBI-10180829;
CC O75382; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-2129889, EBI-720977;
CC O75382; Q8NFA0-2: USP32; NbExp=3; IntAct=EBI-2129889, EBI-12220239;
CC O75382; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-2129889, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC {ECO:0000269|PubMed:15772161}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9R1R2}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9R1R2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Alpha;
CC IsoId=O75382-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O75382-2; Sequence=VSP_005758;
CC Name=Gamma;
CC IsoId=O75382-3; Sequence=VSP_005759;
CC Name=4;
CC IsoId=O75382-4; Sequence=VSP_044780, VSP_044781;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, uterus and testis.
CC -!- DOMAIN: The interaction with MYO5B is dependent upon its NHL repeats,
CC which form a beta-propeller (NHL) domain containing six blades.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF045239; AAC24809.1; -; mRNA.
DR EMBL; AF220020; AAG53474.1; -; mRNA.
DR EMBL; AF220021; AAG53475.1; -; mRNA.
DR EMBL; AF220022; AAG53476.1; -; mRNA.
DR EMBL; AK291396; BAF84085.1; -; mRNA.
DR EMBL; AK298843; BAH12882.1; -; mRNA.
DR EMBL; AC084337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68709.1; -; Genomic_DNA.
DR EMBL; BC096827; AAH96827.1; -; mRNA.
DR CCDS; CCDS58115.1; -. [O75382-4]
DR CCDS; CCDS7764.1; -. [O75382-1]
DR RefSeq; NP_001234935.1; NM_001248006.1. [O75382-1]
DR RefSeq; NP_001234936.1; NM_001248007.1. [O75382-4]
DR RefSeq; NP_006449.2; NM_006458.3. [O75382-1]
DR RefSeq; NP_150594.2; NM_033278.3. [O75382-1]
DR RefSeq; XP_011518146.1; XM_011519844.1.
DR RefSeq; XP_011518147.1; XM_011519845.2. [O75382-4]
DR RefSeq; XP_016872587.1; XM_017017098.1. [O75382-1]
DR RefSeq; XP_016872588.1; XM_017017099.1.
DR PDB; 7O0B; X-ray; 2.13 A; A=318-420.
DR PDBsum; 7O0B; -.
DR AlphaFoldDB; O75382; -.
DR SMR; O75382; -.
DR BioGRID; 115858; 69.
DR CORUM; O75382; -.
DR IntAct; O75382; 29.
DR MINT; O75382; -.
DR STRING; 9606.ENSP00000433102; -.
DR iPTMnet; O75382; -.
DR PhosphoSitePlus; O75382; -.
DR BioMuta; TRIM3; -.
DR EPD; O75382; -.
DR jPOST; O75382; -.
DR MassIVE; O75382; -.
DR MaxQB; O75382; -.
DR PaxDb; O75382; -.
DR PeptideAtlas; O75382; -.
DR PRIDE; O75382; -.
DR ProteomicsDB; 26042; -.
DR ProteomicsDB; 49955; -. [O75382-1]
DR ProteomicsDB; 49956; -. [O75382-2]
DR ProteomicsDB; 49957; -. [O75382-3]
DR Antibodypedia; 11249; 268 antibodies from 33 providers.
DR DNASU; 10612; -.
DR Ensembl; ENST00000345851.8; ENSP00000340797.3; ENSG00000110171.21. [O75382-1]
DR Ensembl; ENST00000359518.7; ENSP00000352508.3; ENSG00000110171.21. [O75382-1]
DR Ensembl; ENST00000525074.5; ENSP00000433102.1; ENSG00000110171.21. [O75382-1]
DR Ensembl; ENST00000536344.5; ENSP00000445460.1; ENSG00000110171.21. [O75382-4]
DR GeneID; 10612; -.
DR KEGG; hsa:10612; -.
DR MANE-Select; ENST00000345851.8; ENSP00000340797.3; NM_033278.4; NP_150594.2.
DR UCSC; uc001mdh.4; human. [O75382-1]
DR CTD; 10612; -.
DR DisGeNET; 10612; -.
DR GeneCards; TRIM3; -.
DR HGNC; HGNC:10064; TRIM3.
DR HPA; ENSG00000110171; Low tissue specificity.
DR MIM; 605493; gene.
DR neXtProt; NX_O75382; -.
DR OpenTargets; ENSG00000110171; -.
DR PharmGKB; PA35534; -.
DR VEuPathDB; HostDB:ENSG00000110171; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158173; -.
DR HOGENOM; CLU_008645_5_0_1; -.
DR InParanoid; O75382; -.
DR OMA; EPCETAM; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; O75382; -.
DR TreeFam; TF331018; -.
DR PathwayCommons; O75382; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; O75382; -.
DR BioGRID-ORCS; 10612; 7 hits in 1120 CRISPR screens.
DR ChiTaRS; TRIM3; human.
DR GeneWiki; TRIM3; -.
DR GenomeRNAi; 10612; -.
DR Pharos; O75382; Tbio.
DR PRO; PR:O75382; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O75382; protein.
DR Bgee; ENSG00000110171; Expressed in cerebellar hemisphere and 156 other tissues.
DR ExpressionAtlas; O75382; baseline and differential.
DR Genevisible; O75382; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Acetylation; Alternative splicing; Cell projection;
KW Coiled coil; Cytoplasm; Endosome; Golgi apparatus; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..744
FT /note="Tripartite motif-containing protein 3"
FT /id="PRO_0000056197"
FT REPEAT 317..418
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 22..63
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 110..151
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 2..290
FT /note="Interaction with KIF21B"
FT /evidence="ECO:0000250|UniProtKB:Q9R1R2"
FT REGION 419..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..224
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044780"
FT VAR_SEQ 120
FT /note="G -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044781"
FT VAR_SEQ 146..156
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005758"
FT VAR_SEQ 224..302
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005759"
FT VARIANT 298
FT /note="L -> R (in dbSNP:rs10128723)"
FT /id="VAR_052124"
FT CONFLICT 113
FT /note="L -> F (in Ref. 1; AAC24809 and 2; AAG53474/
FT AAG53475/AAG53476)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="S -> T (in Ref. 1; AAC24809 and 2; AAG53474/
FT AAG53475)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="T -> A (in Ref. 1; AAC24809 and 2; AAG53474/
FT AAG53475/AAG53476)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="V -> L (in Ref. 3; BAH12882)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="N -> S (in Ref. 1; AAC24809 and 2; AAG53474/
FT AAG53475/AAG53476)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="I -> V (in Ref. 1; AAC24809 and 2; AAG53474/
FT AAG53475/AAG53476)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="V -> E (in Ref. 1; AAC24809 and 2; AAG53474/
FT AAG53475/AAG53476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 80830 MW; FF9829CB52314DD2 CRC64;
MAKREDSPGP EVQPMDKQFL VCSICLDRYQ CPKVLPCLHT FCERCLQNYI PAQSLTLSCP
VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPDGAHDPE DPHPLSVVAG RPLSCPNHEG
KTMEFYCEAC ETAMCGECRA GEHREHGTVL LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI
ALVGGISQQL QERKAEALAQ ISAAFEDLEQ ALQQRKQALV SDLETICGAK QKVLQSQLDT
LRQGQEHIGS SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL
EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK DGRLVRTGSA
ELRAEITGPD GTRLPVPVVD HKNGTYELVY TARTEGELLL SVLLYGQPVR GSPFRVRALR
PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV RRPSSMYSTG GKRKDNPIED ELVFRVGSRG
REKGEFTNLQ GVSAASSGRI VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA
VDTNGDIIVA DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF
TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS ADGEFLFKFG
SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG SFLSYINTSA EPLYGPQGLA
LTSDGHVVVA DAGNHCFKAY RYLQ
