DEN5B_HUMAN
ID DEN5B_HUMAN Reviewed; 1274 AA.
AC Q6ZUT9; B5ME75; Q59FW8; Q68CZ7; Q6NUJ0; Q7Z3F9; Q8N973; Q8WUC8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=DENN domain-containing protein 5B;
DE AltName: Full=Rab6IP1-like protein;
GN Name=DENND5B;
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] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 336-1274 (ISOFORM 1), AND VARIANTS LYS-52 AND
RP ASN-487.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Testis;
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 396-1274 (ISOFORM 1), AND VARIANT
RP ASN-487.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-1274 (ISOFORM 1).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-822 AND SER-1076, 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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076, AND IDENTIFICATION BY
RP 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: Guanine nucleotide exchange factor (GEF) which may activate
CC RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP, converting
CC inactive GDP-bound Rab proteins into their active GTP-bound form.
CC {ECO:0000269|PubMed:20937701}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZUT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZUT9-2; Sequence=VSP_032673;
CC Name=3;
CC IsoId=Q6ZUT9-3; Sequence=VSP_032672, VSP_032675, VSP_032676;
CC Name=4;
CC IsoId=Q6ZUT9-4; Sequence=VSP_032674, VSP_032677, VSP_032678;
CC -!- SIMILARITY: Belongs to the RAB6IP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04583.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK095598; BAC04583.1; ALT_INIT; mRNA.
DR EMBL; AK125323; BAC86129.1; -; mRNA.
DR EMBL; AC022080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88553.1; -; Genomic_DNA.
DR EMBL; BC020855; AAH20855.1; -; mRNA.
DR EMBL; BC068580; AAH68580.1; -; mRNA.
DR EMBL; AB209341; BAD92578.1; -; mRNA.
DR EMBL; BX537924; CAD97905.1; -; mRNA.
DR EMBL; CR749639; CAH18433.1; -; mRNA.
DR CCDS; CCDS44857.1; -. [Q6ZUT9-1]
DR CCDS; CCDS76542.1; -. [Q6ZUT9-2]
DR RefSeq; NP_001295268.1; NM_001308339.1.
DR RefSeq; NP_659410.3; NM_144973.3. [Q6ZUT9-1]
DR AlphaFoldDB; Q6ZUT9; -.
DR SMR; Q6ZUT9; -.
DR BioGRID; 127761; 17.
DR IntAct; Q6ZUT9; 2.
DR STRING; 9606.ENSP00000373734; -.
DR GlyGen; Q6ZUT9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZUT9; -.
DR PhosphoSitePlus; Q6ZUT9; -.
DR BioMuta; DENND5B; -.
DR DMDM; 182676608; -.
DR EPD; Q6ZUT9; -.
DR jPOST; Q6ZUT9; -.
DR MassIVE; Q6ZUT9; -.
DR MaxQB; Q6ZUT9; -.
DR PaxDb; Q6ZUT9; -.
DR PeptideAtlas; Q6ZUT9; -.
DR PRIDE; Q6ZUT9; -.
DR ProteomicsDB; 68365; -. [Q6ZUT9-1]
DR ProteomicsDB; 68366; -. [Q6ZUT9-2]
DR ProteomicsDB; 68367; -. [Q6ZUT9-3]
DR ProteomicsDB; 68368; -. [Q6ZUT9-4]
DR Antibodypedia; 55109; 74 antibodies from 15 providers.
DR DNASU; 160518; -.
DR Ensembl; ENST00000354285.8; ENSP00000346238.4; ENSG00000170456.16. [Q6ZUT9-4]
DR Ensembl; ENST00000389082.10; ENSP00000373734.5; ENSG00000170456.16. [Q6ZUT9-1]
DR GeneID; 160518; -.
DR KEGG; hsa:160518; -.
DR MANE-Select; ENST00000389082.10; ENSP00000373734.5; NM_144973.4; NP_659410.3.
DR UCSC; uc001rki.2; human. [Q6ZUT9-1]
DR CTD; 160518; -.
DR DisGeNET; 160518; -.
DR GeneCards; DENND5B; -.
DR HGNC; HGNC:28338; DENND5B.
DR HPA; ENSG00000170456; Low tissue specificity.
DR MIM; 617279; gene.
DR neXtProt; NX_Q6ZUT9; -.
DR OpenTargets; ENSG00000170456; -.
DR PharmGKB; PA164718788; -.
DR VEuPathDB; HostDB:ENSG00000170456; -.
DR eggNOG; KOG2080; Eukaryota.
DR GeneTree; ENSGT00940000153678; -.
DR HOGENOM; CLU_004201_2_0_1; -.
DR InParanoid; Q6ZUT9; -.
DR OMA; NTIHMYE; -.
DR OrthoDB; 53600at2759; -.
DR PhylomeDB; Q6ZUT9; -.
DR TreeFam; TF313237; -.
DR PathwayCommons; Q6ZUT9; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q6ZUT9; -.
DR BioGRID-ORCS; 160518; 13 hits in 1070 CRISPR screens.
DR ChiTaRS; DENND5B; human.
DR GenomeRNAi; 160518; -.
DR Pharos; Q6ZUT9; Tbio.
DR PRO; PR:Q6ZUT9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6ZUT9; protein.
DR Bgee; ENSG00000170456; Expressed in lateral nuclear group of thalamus and 190 other tissues.
DR ExpressionAtlas; Q6ZUT9; baseline and differential.
DR Genevisible; Q6ZUT9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; IEA:Ensembl.
DR Gene3D; 1.20.58.900; -; 3.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF02759; RUN; 2.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00593; RUN; 2.
DR SMART; SM00800; uDENN; 1.
DR SUPFAM; SSF140741; SSF140741; 2.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS50826; RUN; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Guanine-nucleotide releasing factor;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1274
FT /note="DENN domain-containing protein 5B"
FT /id="PRO_0000326531"
FT TRANSMEM 916..936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 39..244
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 263..399
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 401..581
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 772..932
FT /note="RUN 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 936..1044
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 1118..1267
FT /note="RUN 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2RSQ0"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2RSQ0"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1062
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL8"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL8"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ26"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032672"
FT VAR_SEQ 1..42
FT /note="MSGSCAAPGPGSGSSPAACRFAHYFVLCGIDADSGLEPDELA -> MGTHHH
FT AQLIFVFLVEMRFHRVDQAGLELLTSGNSPASASRSAEITVVSQHAQPGFLYQWLEADR
FT HGKSQGAANTTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032673"
FT VAR_SEQ 42
FT /note="A -> AVLYQWLEADRHGKSQGAANTTS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032674"
FT VAR_SEQ 544..585
FT /note="ASFLSDQPEPYLPFLSRFIETQMFATFIDNKIMSQWEEKDPL -> VKRTIV
FT FLLWLLVALLLILTFLNFLFFCAYAYPYIIDFVNLF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032675"
FT VAR_SEQ 586..1274
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032676"
FT VAR_SEQ 703..716
FT /note="KYMQEARSLGKNLR -> VCGLPSWGASQQAP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032677"
FT VAR_SEQ 717..1274
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032678"
FT VARIANT 52
FT /note="R -> K (in dbSNP:rs4930979)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_040076"
FT VARIANT 487
FT /note="H -> N (in dbSNP:rs1056320)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_040077"
FT CONFLICT 434
FT /note="N -> D (in Ref. 4; AAH68580)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="K -> R (in Ref. 1; BAC04583)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="M -> T (in Ref. 1; BAC04583)"
FT /evidence="ECO:0000305"
FT CONFLICT 1144
FT /note="I -> T (in Ref. 1; BAC04583)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="V -> A (in Ref. 1; BAC04583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1274 AA; 145020 MW; 712F41E50EEE910A CRC64;
MSGSCAAPGP GSGSSPAACR FAHYFVLCGI DADSGLEPDE LAGENFDQSP LRRTFKSKVL
AHYPQNIEWN PFDQDAVNML CMPKGLSFRT QTDNKDPQFH SFIITREDGS RTYGFVLTFY
EEVTSKQICT AMQTLYQMHN AEHYSSVYAS SSCSMDSLAS SLDEGDTTSL LKLQRYNSYD
ISRDTLYVSK SICLITPLPF MQACKKFLIQ LYKAVTSQQP PPLPLESYIH NILYEVPLPP
PGRSLKFYGV YEPVICQRPG PSELPLSDYP LREAFELLGL ENLVQVFTCV LLEMQILLYS
QDYQRLMTVA EGITTLLFPF QWQHVYVPIL PASLLHFLDA PVPYLMGLQS KEGTDRSKLE
LPQEANLCFV DIDNHFIELP EEFPQFPNKV DFIQELSEVL VQFGIPPEGS LHCSESTSKL
KNMVLKDLVN DKKNGNVCTN NISMYELLKG NETIARLQAL AKRTGVAVEK MDLSASLGEK
DKDLKLHCEE AELRDYQLNV QLREVFANRF TQMFADYEAF VIQTAQDMES WLTNREQMQN
FDKASFLSDQ PEPYLPFLSR FIETQMFATF IDNKIMSQWE EKDPLLRVFD TRIDKIRLYN
VRAPTLRTSI YQKCSTLKEA AQSIEQRLMK MDHTAIHPHL LDMKIGQGKY EQGFFPKLQS
DVLATGPTSN NRWVSRSATA QRRKERLRQH SEHVGLDNDL REKYMQEARS LGKNLRQPKL
SDLSPAVIAQ TNCKFVEGLL KECRMKTKRM LVEKMGHEAV ELGHGEANIT GLEENTLIAS
LCDLLERIWS HGLQVKQGKS ALWSHLIQFQ DREEKQEHLA ESPVALGPER RKSDSGVMLP
TLRVSLIQDM RHIQNMSEIK TDVGRARAWI RLSLEKKLLS QHLKQLLSNQ PLTKKLYKRY
AFLRCEEERE QFLYHLLSLN AVDYFCFTSV FTTIMIPYRS VIIPIKKLSN AIITSNPWIC
VSGELGDTGV MQIPKNLLEM TFECQNLGKL TTVQIGHDNS GLLAKWLVDC VMVRNEITGH
TYRFPCGRWL GKGIDDGSLE RILIGELMTS ASDEDLVKQC RTPPQQKSPT TARRLSITSL
TGKNNKPNAG QIQEGIGEAV NNIVKHFHKP EKERGSLTVL LCGENGLVAA LEQVFHHGFK
SARIFHKNVF IWDFIEKVVA YFETTDQILD NEDDVLIQKS SCKTFCHYVN AINTAPRNIG
KDGKFQILVC LGTRDRLLPQ WIPLLAECPA ITRMYEESAL LRDRMTVNSL IRILQTIQDF
TIVLEGSLIK GVDV
