MYCPP_HUMAN
ID MYCPP_HUMAN Reviewed; 1863 AA.
AC Q7Z401; E7EPL3; Q14655; Q86T77; Q8IVX2; Q8NB93;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=C-myc promoter-binding protein;
DE AltName: Full=DENN domain-containing protein 4A;
GN Name=DENND4A; Synonyms=IRLB, MYCPBP;
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 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RX PubMed=12906859; DOI=10.1016/s0888-7543(03)00103-4;
RA Semova N., Kapanadze B., Corcoran M., Kutsenko A., Baranova A., Semov A.;
RT "Molecular cloning, structural analysis, and expression of a human IRLB,
RT MYC promoter-binding protein: new DENN domain-containing protein family
RT emerges.";
RL Genomics 82:343-354(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 33-1863 (ISOFORM 1).
RC TISSUE=Bone marrow, and Spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-284.
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-928 (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1673-1863 (ISOFORM 1), AND FUNCTION.
RX PubMed=8056341; DOI=10.1016/0378-1119(94)90018-3;
RA Stasiv Y.Z., Mashkova T.D., Chernov B.K., Sokolava I.V., Itkes A.V.,
RA Kisselev L.L.;
RT "Cloning of a cDNA encoding a human protein which binds a sequence in the
RT c-myc gene similar to the interferon-stimulated response element.";
RL Gene 145:267-272(1994).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-731 AND SER-1587, AND
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 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1035, 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 [11]
RP FUNCTION AS GUANYL-NUCLEOTIDE EXCHANGE FACTOR.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-731; SER-1015; SER-1035;
RP SER-1099; SER-1151; SER-1152; SER-1225; SER-1240; SER-1251; SER-1281;
RP SER-1508; SER-1587; SER-1589 AND SER-1591, AND IDENTIFICATION BY MASS
RP 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 [15]
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).
CC -!- FUNCTION: Probable guanine nucleotide exchange factor (GEF) which may
CC activate RAB10. Promotes the exchange of GDP to GTP, converting
CC inactive GDP-bound Rab proteins into their active GTP-bound form.
CC According to PubMed:8056341, it may bind to ISRE-like element
CC (interferon-stimulated response element) of MYC P2 promoter.
CC {ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:8056341}.
CC -!- INTERACTION:
CC Q7Z401; P63104: YWHAZ; NbExp=2; IntAct=EBI-1046479, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z401-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z401-2; Sequence=VSP_044630;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Highest expression in bone
CC marrow, medium in peripheral blood lymphocytes and lowest in spleen. In
CC brain, breast, and prostate, higher expression was seen in normal cells
CC than in tumor cells. Expression is regulated in a growth- and cell
CC cycle-dependent manner. {ECO:0000269|PubMed:12906859}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in fetal liver.
CC {ECO:0000269|PubMed:12906859}.
CC -!- INDUCTION: By serum in low-passage fibroblasts.
CC {ECO:0000269|PubMed:12906859}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AL833317; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF534403; AAQ10514.1; -; mRNA.
DR EMBL; AL832602; CAD89960.1; -; mRNA.
DR EMBL; AL833317; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC011939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041706; AAH41706.1; -; mRNA.
DR EMBL; AK091368; BAC03648.1; -; mRNA.
DR EMBL; X63417; CAA45013.1; -; mRNA.
DR CCDS; CCDS45285.1; -. [Q7Z401-1]
DR CCDS; CCDS53949.1; -. [Q7Z401-2]
DR PIR; I37904; I37904.
DR RefSeq; NP_001138295.1; NM_001144823.2. [Q7Z401-2]
DR RefSeq; NP_005839.3; NM_005848.4. [Q7Z401-1]
DR RefSeq; XP_005254178.1; XM_005254121.3.
DR RefSeq; XP_016877352.1; XM_017021863.1.
DR AlphaFoldDB; Q7Z401; -.
DR SMR; Q7Z401; -.
DR BioGRID; 115552; 70.
DR IntAct; Q7Z401; 23.
DR MINT; Q7Z401; -.
DR STRING; 9606.ENSP00000391167; -.
DR GlyGen; Q7Z401; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z401; -.
DR PhosphoSitePlus; Q7Z401; -.
DR BioMuta; DENND4A; -.
DR DMDM; 88909230; -.
DR EPD; Q7Z401; -.
DR jPOST; Q7Z401; -.
DR MassIVE; Q7Z401; -.
DR MaxQB; Q7Z401; -.
DR PaxDb; Q7Z401; -.
DR PeptideAtlas; Q7Z401; -.
DR PRIDE; Q7Z401; -.
DR ProteomicsDB; 17383; -.
DR ProteomicsDB; 69104; -. [Q7Z401-1]
DR Antibodypedia; 26036; 43 antibodies from 16 providers.
DR DNASU; 10260; -.
DR Ensembl; ENST00000431932.6; ENSP00000396830.2; ENSG00000174485.16. [Q7Z401-1]
DR GeneID; 10260; -.
DR KEGG; hsa:10260; -.
DR UCSC; uc002aph.4; human. [Q7Z401-1]
DR CTD; 10260; -.
DR DisGeNET; 10260; -.
DR GeneCards; DENND4A; -.
DR HGNC; HGNC:24321; DENND4A.
DR HPA; ENSG00000174485; Tissue enhanced (retina).
DR MIM; 600382; gene.
DR neXtProt; NX_Q7Z401; -.
DR OpenTargets; ENSG00000174485; -.
DR PharmGKB; PA134887513; -.
DR VEuPathDB; HostDB:ENSG00000174485; -.
DR eggNOG; KOG2127; Eukaryota.
DR GeneTree; ENSGT00940000155836; -.
DR HOGENOM; CLU_003074_0_0_1; -.
DR InParanoid; Q7Z401; -.
DR OrthoDB; 75304at2759; -.
DR PhylomeDB; Q7Z401; -.
DR TreeFam; TF313237; -.
DR PathwayCommons; Q7Z401; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q7Z401; -.
DR BioGRID-ORCS; 10260; 25 hits in 1078 CRISPR screens.
DR ChiTaRS; DENND4A; human.
DR GeneWiki; DENND4A; -.
DR GenomeRNAi; 10260; -.
DR Pharos; Q7Z401; Tbio.
DR PRO; PR:Q7Z401; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q7Z401; protein.
DR Bgee; ENSG00000174485; Expressed in calcaneal tendon and 155 other tissues.
DR ExpressionAtlas; Q7Z401; baseline and differential.
DR Genevisible; Q7Z401; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR023341; MABP.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR TIGRFAMs; TIGR00756; PPR; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS51498; MABP; 1.
DR PROSITE; PS51375; PPR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Guanine-nucleotide releasing factor;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1863
FT /note="C-myc promoter-binding protein"
FT /id="PRO_0000223952"
FT DOMAIN 42..200
FT /note="MABP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00831"
FT DOMAIN 192..364
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 385..521
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 523..641
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REPEAT 772..808
FT /note="PPR 1"
FT REPEAT 809..843
FT /note="PPR 2"
FT REGION 905..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 917..933
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 911..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 900
FT /note="S -> SDGSDLDAVSHGSMDSGHGTHTVEQAPFNTGLIKVYATDDRSST
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_044630"
FT VARIANT 284
FT /note="L -> P (in dbSNP:rs17854146)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025362"
FT CONFLICT 256
FT /note="S -> P (in Ref. 2; AL833317)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="S -> P (in Ref. 2; CAD89960)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="M -> MGK (in Ref. 1; AAQ10514)"
FT /evidence="ECO:0000305"
FT CONFLICT 1532
FT /note="T -> A (in Ref. 2; AL833317)"
FT /evidence="ECO:0000305"
FT CONFLICT 1726
FT /note="K -> Q (in Ref. 2; AL833317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1863 AA; 209244 MW; 7432EEC9DB9711E6 CRC64;
MIEDKGPRVA DYFVVAGLTD VSKPLEEEIH FNDACHKVAK PKEPITDVSV IIKSLGEEVP
QDYICIDVTP TGLSADLNNG SLVGPQIYLC YRRGRDKPPL TDLGVLYDWK ERLKQGCEII
QSTPYGRPAN ISGSTSSQRI YITYRRASEN MTQNTLAVTD ICIIIPSKGE SPPHTFCKVD
KNLNNSMWGS AVYLCYKKSV AKTNTVSYKA GLICRYPQED YESFSLPESV PLFCLPMGAT
IECWPSNSKY PLPVFSTFVL TGASAEKVYG AAIQFYEPYS EENLTEKQRL LLGLTSADGK
SDSSKTIHTN KCICLLSHWP FFDAFRKFLT FLYRYSISGP HVLPIEKHIS HFMHKVPFPS
PQRPRILVQL SPHDNLILSQ PVSSPLPLSG GKFSTLLQNL GPENAVTLLV FAVTEHKILI
HSLRPSVLTS VTEALVSMIF PFHWPCPYVP LCPLALADVL SAPCPFIVGI DSRYFDLYDP
PPDVSCVDVD TNTISQIGDK KNVAWKILPK KPCKNLMNTL NNLHQQLAKL QQRPRDDGLM
DLAINDYDFN SGKRLHMIDL EIQEAFLFFM ASILKGYRSY LRPITQAPSE TATDAASLFA
LQAFLRSRDR SHQKFYNMMT KTQMFIRFIE ECSFVSDKDA SLAFFDDCVD KVDMDKSGEV
RLIELDESFK SEHTVFVTPP EIPHLPNGEE PPLQYSYNGF PVLRNNLFER PEGFLQAKKN
KLPSKSSSPN SPLPMFRRTK QEIKSAHKIA KRYSSIPQMW SRCLLRHCYG LWFICLPAYV
KVCHSKVRAL KTAYDVLKKM QSKKMDPPDE VCYRILMQLC GQYDQPVLAV RVLFEMQKAG
IDPNAITYGY YNKAVLESTW PSRSRSGYFL WTKVRNVVLG VTQFKRALKK HAHLSQTTLS
GGQSDLGYNS LSKDEVRRGD TSTEDIQEEK DKKGSDCSSL SESESTKGSA DCLPKLSYQN
SSSIVRLTGT SNNSAGKISG ESMESTPELL LISSLEDTNE TRNIQSRCFR KRHKSDNETN
LQQQVVWGNR NRNLSGGVLM GFMLNRINQE ATPGDIVEKL GADAKILSNV ISKSTRPNTL
DIGKPPLRSK RDSLEKESSD DDTPFDGSNY LADKVDSPVI FDLEDLDSET DVSKAGCVAT
QNPKRIQRMN SSFSVKPFEK TDVATGFDPL SLLVAETEQQ QKEEEEEDED DSKSISTPSA
RRDLAEEIVM YMNNMSSPLT SRTPSIDLQR ACDDKLNKKS PPLVKACRRS SLPPNSPKPV
RLTKSKSYTK SEEKPRDRLW SSPAFSPTCP FREESQDTLT HSSPSFNLDT LLVPKLDVLR
NSMFTAGKGV AEKASKWYSR FTMYTTSSKD QSSDRTSLSS VGAQDSESTS LTDEDVCHEL
EGPISSQETS ATSGTKRIDL SRISLESSAS LEGSLSKFAL PGKSEVTSSF NASNTNIFQN
YAMEVLISSC SRCRTCDCLV HDEEIMAGWT ADDSNLNTTC PFCGNIFLPF LNIEIRDLRR
PGRYFLKSSP STENMHFPSS ISSQTRQSCI STSASGLDTS ALSVQGNFDL NSKSKLQENF
CTRSIQIPAN RSKTAMSKCP IFPMARSIST SGPLDKEDTG RQKLISTGSL PATLQGATDS
LGLEWHLPSP DPVTVPYLSP LVVWKELESL LENEGDHAIT VADFVDHHPI VFWNLVWYFR
RLDLPSNLPG LILSSEHCNK YSKIPRHCMS EDSKYVLIQM LWDNMKLHQD PGQPLYILWN
AHTQKYPMVH LLQKSDNSFN QELLKSMVKS IKMNDVYGPM SQILETLNKC PHFKRQRSLY
REILFLSLVA LGRENIDIDA FDKEYKMAYD RLTPSQVKST HNCDRPPSTG VMECRKTFGE
PYL
