ID   TPC12_HUMAN             Reviewed;         735 AA.
AC   Q8WVT3; B3KV01; D6W4Y2; Q8WVW1; Q9Y395;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   28-JAN-2026, entry version 181.
DE   RecName: Full=Trafficking protein particle complex subunit 12 {ECO:0000305};
DE   AltName: Full=Tetratricopeptide repeat protein 15 {ECO:0000303|PubMed:21525244};
DE            Short=TPR repeat protein 15 {ECO:0000303|PubMed:21525244};
DE            Short=TTC-15 {ECO:0000303|PubMed:21525244};
DE   AltName: Full=Trafficking of membranes and mitosis {ECO:0000303|PubMed:25918224};
GN   Name=TRAPPC12 {ECO:0000312|HGNC:HGNC:24284};
GN   Synonyms=TRAMM {ECO:0000303|PubMed:25918224}, TTC15
GN   {ECO:0000303|PubMed:21525244};
GN   ORFNames=CGI-87 {ECO:0000303|PubMed:10810093};
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 [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-301.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Muscle;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 356-735.
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP   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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   FUNCTION, IDENTIFICATION IN TRAPP COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=21525244; DOI=10.1091/mbc.e10-11-0873;
RA   Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT   "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early
RT   stage in ER-to-Golgi trafficking.";
RL   Mol. Biol. Cell 22:2083-2093(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP   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).
RN   [11]
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   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPE, AND
RP   PHOSPHORYLATION.
RX   PubMed=25918224; DOI=10.1083/jcb.201501090;
RA   Milev M.P., Hasaj B., Saint-Dic D., Snounou S., Zhao Q., Sacher M.;
RT   "TRAMM/TrappC12 plays a role in chromosome congression, kinetochore
RT   stability, and CENP-E recruitment.";
RL   J. Cell Biol. 209:221-234(2015).
RN   [13]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-717.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [14]
RP   INVOLVEMENT IN PEBAS, AND VARIANT PEBAS VAL-627.
RX   PubMed=28777934; DOI=10.1016/j.ajhg.2017.07.006;
RA   Milev M.P., Grout M.E., Saint-Dic D., Cheng Y.H., Glass I.A., Hale C.J.,
RA   Hanna D.S., Dorschner M.O., Prematilake K., Shaag A., Elpeleg O.,
RA   Sacher M., Doherty D., Edvardson S.;
RT   "Mutations in TRAPPC12 manifest in progressive childhood encephalopathy and
RT   Golgi dysfunction.";
RL   Am. J. Hum. Genet. 101:291-299(2017).
CC   -!- FUNCTION: Component of the TRAPP complex, which is involved in
CC       endoplasmic reticulum to Golgi apparatus trafficking at a very early
CC       stage (PubMed:21525244, PubMed:28777934). Also plays a role in
CC       chromosome congression, kinetochore assembly and stability and controls
CC       the recruitment of CENPE to the kinetochores (PubMed:25918224).
CC       {ECO:0000269|PubMed:21525244, ECO:0000269|PubMed:25918224,
CC       ECO:0000269|PubMed:28777934}.
CC   -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC       particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3,
CC       TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and
CC       TRAPPC12 (PubMed:21525244). Interacts with CENPE (PubMed:25918224).
CC       {ECO:0000269|PubMed:21525244, ECO:0000269|PubMed:25918224}.
CC   -!- INTERACTION:
CC       Q8WVT3; O00327-8: BMAL1; NbExp=3; IntAct=EBI-2819919, EBI-11991546;
CC       Q8WVT3; I6L957: HNRNPA2B1; NbExp=3; IntAct=EBI-2819919, EBI-1642515;
CC       Q8WVT3; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-2819919, EBI-821335;
CC       Q8WVT3; Q96LW2: RSKR; NbExp=3; IntAct=EBI-2819919, EBI-1054572;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment {ECO:0000269|PubMed:21525244}. Nucleus
CC       {ECO:0000269|PubMed:25918224}. Note=Mainly localizes to structures
CC       resembling the Golgi and a small amount is found in the nucleus.
CC       {ECO:0000269|PubMed:25918224}.
CC   -!- PTM: Phosphorylated as the cells enter mitosis but is dephosphorylated
CC       at or before the onset of anaphase. The phosphorylated form recruits
CC       CENPE to kinetochores more efficiently than the non-phosphorylated
CC       form. {ECO:0000269|PubMed:25918224}.
CC   -!- DISEASE: Encephalopathy, progressive, early-onset, with brain atrophy
CC       and spasticity (PEBAS) [MIM:617669]: An autosomal recessive,
CC       progressive encephalopathy characterized by central nervous system
CC       atrophy and dysfunction, spasticity, microcephaly, global developmental
CC       delay, and hearing loss. {ECO:0000269|PubMed:28777934}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry. Cells display a fragmented Golgi apparatus (PubMed:28777934).
CC       {ECO:0000269|PubMed:28777934}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD34082.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK098327; BAG53613.1; -; mRNA.
DR   EMBL; CH471053; EAX01067.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX01068.1; -; Genomic_DNA.
DR   EMBL; BC014164; AAH14164.2; -; mRNA.
DR   EMBL; BC017475; AAH17475.2; -; mRNA.
DR   EMBL; AF151845; AAD34082.1; ALT_INIT; mRNA.
DR   CCDS; CCDS1652.1; -.
DR   RefSeq; NP_001308031.1; NM_001321102.2.
DR   RefSeq; NP_057114.5; NM_016030.5.
DR   AlphaFoldDB; Q8WVT3; -.
DR   SMR; Q8WVT3; -.
DR   BioGRID; 119301; 101.
DR   ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant.
DR   ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant.
DR   CORUM; Q8WVT3; -.
DR   DIP; DIP-48283N; -.
DR   FunCoup; Q8WVT3; 3456.
DR   IntAct; Q8WVT3; 36.
DR   STRING; 9606.ENSP00000324318; -.
DR   GlyGen; Q8WVT3; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8WVT3; -.
DR   MetOSite; Q8WVT3; -.
DR   PhosphoSitePlus; Q8WVT3; -.
DR   BioMuta; TRAPPC12; -.
DR   DMDM; 116242834; -.
DR   jPOST; Q8WVT3; -.
DR   MassIVE; Q8WVT3; -.
DR   PaxDb; 9606-ENSP00000324318; -.
DR   PeptideAtlas; Q8WVT3; -.
DR   ProteomicsDB; 74819; -.
DR   Pumba; Q8WVT3; -.
DR   Antibodypedia; 26298; 69 antibodies from 14 providers.
DR   DNASU; 51112; -.
DR   Ensembl; ENST00000324266.10; ENSP00000324318.5; ENSG00000171853.17.
DR   Ensembl; ENST00000382110.6; ENSP00000371544.2; ENSG00000171853.17.
DR   GeneID; 51112; -.
DR   KEGG; hsa:51112; -.
DR   MANE-Select; ENST00000324266.10; ENSP00000324318.5; NM_016030.6; NP_057114.5.
DR   UCSC; uc002qxm.2; human.
DR   AGR; HGNC:24284; -.
DR   ClinPGx; PA134944710; -.
DR   CTD; 51112; -.
DR   DisGeNET; 51112; -.
DR   GeneCards; TRAPPC12; -.
DR   HGNC; HGNC:24284; TRAPPC12.
DR   HPA; ENSG00000171853; Tissue enhanced (testis).
DR   MalaCards; TRAPPC12; -.
DR   MIM; 614139; gene.
DR   MIM; 617669; phenotype.
DR   OpenTargets; ENSG00000171853; -.
DR   Orphanet; 500144; Early-onset progressive encephalopathy-hearing loss-pons hypoplasia-brain atrophy syndrome.
DR   VEuPathDB; HostDB:ENSG00000171853; -.
DR   eggNOG; KOG2796; Eukaryota.
DR   GeneTree; ENSGT00390000002448; -.
DR   HOGENOM; CLU_014917_0_0_1; -.
DR   InParanoid; Q8WVT3; -.
DR   OMA; MSNITQE; -.
DR   OrthoDB; 428342at2759; -.
DR   PAN-GO; Q8WVT3; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q8WVT3; -.
DR   PathwayCommons; Q8WVT3; -.
DR   Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   SignaLink; Q8WVT3; -.
DR   Agora; ENSG00000171853; -.
DR   BioGRID-ORCS; 51112; 35 hits in 1153 CRISPR screens.
DR   ChiTaRS; TRAPPC12; human.
DR   GenomeRNAi; 51112; -.
DR   Pharos; Q8WVT3; Tbio.
DR   PRO; PR:Q8WVT3; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8WVT3; protein.
DR   Bgee; ENSG00000171853; Expressed in left testis and 95 other cell types or tissues.
DR   ExpressionAtlas; Q8WVT3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030008; C:TRAPP complex; IDA:UniProtKB.
DR   GO; GO:1990072; C:TRAPPIII protein complex; NAS:ComplexPortal.
DR   GO; GO:0048208; P:COPII vesicle coating; NAS:ComplexPortal.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR   GO; GO:0051310; P:metaphase chromosome alignment; IMP:UniProtKB.
DR   GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IMP:UniProtKB.
DR   GO; GO:0090234; P:regulation of kinetochore assembly; IMP:UniProtKB.
DR   GO; GO:0099022; P:vesicle tethering; NAS:ComplexPortal.
DR   FunFam; 1.25.40.10:FF:000170; Trafficking protein particle complex subunit 12; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR21581:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF13174; TPR_6; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Deafness; Disease variant; ER-Golgi transport; Nucleus; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Repeat; TPR repeat;
KW   Transport.
FT   CHAIN           1..735
FT                   /note="Trafficking protein particle complex subunit 12"
FT                   /id="PRO_0000106401"
FT   REPEAT          545..578
FT                   /note="TPR 1"
FT   REPEAT          580..613
FT                   /note="TPR 2"
FT   REPEAT          620..653
FT                   /note="TPR 3"
FT   REPEAT          654..687
FT                   /note="TPR 4"
FT   REGION          1..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..22
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..50
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2L8"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         301
FT                   /note="S -> G (in dbSNP:rs11686212)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_028442"
FT   VARIANT         627
FT                   /note="A -> V (in PEBAS; uncertain significance;
FT                   dbSNP:rs768950892)"
FT                   /evidence="ECO:0000269|PubMed:28777934"
FT                   /id="VAR_080390"
FT   VARIANT         717
FT                   /note="E -> Q (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035869"
FT   CONFLICT        451
FT                   /note="F -> V (in Ref. 4; AAD34082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        486
FT                   /note="E -> D (in Ref. 4; AAD34082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="E -> D (in Ref. 3; AAH14164)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   735 AA;  79375 MW;  B844FB3749866E3F CRC64;
     MEDAGGGEET PAPEAPHPPQ LAPPEEQGLL FQEETIDLGG DEFGSEENET ASEGSSPLAD
     KLNEHMMESV LISDSPNSEG DAGDLGRVRD EAEPGGEGDP GPEPAGTPSP SGEADGDCAP
     EDAAPSSGGA PRQDAAREVP GSEAARPEQE PPVAEPVPVC TIFSQRAPPA SGDGFEPQMV
     KSPSFGGASE ASARTPPQVV QPSPSLSTFF GDTAASHSLA SDFFDSFTTS AFISVSNPGA
     GSPAPASPPP LAVPGTEGRP EPVAMRGPQA AAPPASPEPF AHIQAVFAGS DDPFATALSM
     SEMDRRNDAW LPGEATRGVL RAVATQQRGA VFVDKENLTM PGLRFDNIQG DAVKDLMLRF
     LGEKAAAKRQ VLNADSVEQS FVGLKQLISC RNWRAAVDLC GRLLTAHGQG YGKSGLLTSH
     TTDSLQLWFV RLALLVKLGL FQNAEMEFEP FGNLDQPDLY YEYYPHVYPG RRGSMVPFSM
     RILHAELQQY LGNPQESLDR LHKVKTVCSK ILANLEQGLA EDGGMSSVTQ EGRQASIRLW
     RSRLGRVMYS MANCLLLMKD YVLAVEAYHS VIKYYPEQEP QLLSGIGRIS LQIGDIKTAE
     KYFQDVEKVT QKLDGLQGKI MVLMNSAFLH LGQNNFAEAH RFFTEILRMD PRNAVANNNA
     AVCLLYLGKL KDSLRQLEAM VQQDPRHYLH ESVLFNLTTM YELESSRSMQ KKQALLEAVA
     GKEGDSFNTQ CLKLA
//