DEN4C_HUMAN
ID DEN4C_HUMAN Reviewed; 1909 AA.
AC Q5VZ89; A2A3R1; A2A3R2; A2A3R3; A2A3R9; Q6AI48; Q6ZUB3; Q8NCY7; Q9H6N4;
AC Q9NUT1; Q9NWA5; Q9NWT3; R4GN35; R4GNB2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DENN domain-containing protein 4C;
GN Name=DENND4C; Synonyms=C9orf55, C9orf55B;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-1909 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 966-1909 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1272-1909 (ISOFORM 5).
RC TISSUE=Embryo, Hepatoma, Placenta, Signet-ring cell carcinoma, and Testis;
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 MRNA] OF 912-1909 (ISOFORM 1).
RC TISSUE=Fetal kidney, and Lymph node;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741; SER-965; SER-968;
RP SER-973; SER-989; SER-1003; SER-1046; SER-1099; SER-1126; SER-1225;
RP SER-1244; SER-1278; SER-1325; SER-1623 AND SER-1627, 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 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973; SER-989; SER-1278 AND
RP SER-1346, AND IDENTIFICATION BY 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1225 AND SER-1623,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-953 (ISOFORM 2), AND
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1184, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703; SER-737; SER-741;
RP SER-968; SER-973; SER-989; SER-996; SER-1061; SER-1099; SER-1184; SER-1225;
RP SER-1278; SER-1325; SER-1337; SER-1346; SER-1623 AND SER-1629, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965; SER-968; SER-973;
RP THR-975; SER-989; SER-1278 AND SER-1799, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-953 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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) activating RAB10.
CC Promotes the exchange of GDP to GTP, converting inactive GDP-bound
CC RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4
CC glucose transporter-enriched vesicles delivery to the plasma membrane
CC in response to insulin. {ECO:0000269|PubMed:20937701}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Cell membrane.
CC Cytoplasm, cytosol. Note=Associates with SLC2A4/GLUT4 storage vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5VZ89-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q5VZ89-3; Sequence=VSP_027384, VSP_027386;
CC Name=5;
CC IsoId=Q5VZ89-5; Sequence=VSP_027382, VSP_027383;
CC Name=2;
CC IsoId=Q5VZ89-7; Sequence=VSP_027379;
CC -!- PTM: Phosphorylated in response to insulin. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91294.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91478.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15221.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86313.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10466.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AL161909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58645.1; -; Genomic_DNA.
DR EMBL; AK000627; BAA91294.1; ALT_INIT; mRNA.
DR EMBL; AK001046; BAA91478.1; ALT_INIT; mRNA.
DR EMBL; AK002020; BAA92039.1; ALT_INIT; mRNA.
DR EMBL; AK025705; BAB15221.1; ALT_INIT; mRNA.
DR EMBL; AK125842; BAC86313.1; ALT_INIT; mRNA.
DR EMBL; AL834521; CAD39177.1; -; mRNA.
DR EMBL; CR627367; CAH10466.1; ALT_SEQ; mRNA.
DR CCDS; CCDS6491.3; -. [Q5VZ89-1]
DR CCDS; CCDS83349.1; -. [Q5VZ89-7]
DR RefSeq; NP_001317569.1; NM_001330640.1. [Q5VZ89-7]
DR RefSeq; NP_060395.5; NM_017925.6. [Q5VZ89-1]
DR AlphaFoldDB; Q5VZ89; -.
DR SMR; Q5VZ89; -.
DR BioGRID; 120799; 120.
DR IntAct; Q5VZ89; 26.
DR MINT; Q5VZ89; -.
DR STRING; 9606.ENSP00000473565; -.
DR iPTMnet; Q5VZ89; -.
DR PhosphoSitePlus; Q5VZ89; -.
DR BioMuta; DENND4C; -.
DR DMDM; 158937337; -.
DR EPD; Q5VZ89; -.
DR jPOST; Q5VZ89; -.
DR MassIVE; Q5VZ89; -.
DR MaxQB; Q5VZ89; -.
DR PaxDb; Q5VZ89; -.
DR PeptideAtlas; Q5VZ89; -.
DR PRIDE; Q5VZ89; -.
DR ProteomicsDB; 65680; -. [Q5VZ89-1]
DR ProteomicsDB; 65682; -. [Q5VZ89-3]
DR ProteomicsDB; 65684; -. [Q5VZ89-5]
DR Antibodypedia; 10280; 83 antibodies from 18 providers.
DR Ensembl; ENST00000434457.7; ENSP00000473469.1; ENSG00000137145.21. [Q5VZ89-7]
DR Ensembl; ENST00000602925.5; ENSP00000473565.1; ENSG00000137145.21. [Q5VZ89-1]
DR GeneID; 55667; -.
DR KEGG; hsa:55667; -.
DR MANE-Select; ENST00000434457.7; ENSP00000473469.1; NM_001330640.2; NP_001317569.1. [Q5VZ89-7]
DR UCSC; uc031tcw.2; human.
DR CTD; 55667; -.
DR GeneCards; DENND4C; -.
DR HGNC; HGNC:26079; DENND4C.
DR HPA; ENSG00000137145; Low tissue specificity.
DR neXtProt; NX_Q5VZ89; -.
DR OpenTargets; ENSG00000137145; -.
DR PharmGKB; PA134939495; -.
DR VEuPathDB; HostDB:ENSG00000137145; -.
DR eggNOG; KOG2127; Eukaryota.
DR GeneTree; ENSGT00940000158215; -.
DR InParanoid; Q5VZ89; -.
DR OMA; TWESEHR; -.
DR OrthoDB; 75304at2759; -.
DR PhylomeDB; Q5VZ89; -.
DR TreeFam; TF313237; -.
DR PathwayCommons; Q5VZ89; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q5VZ89; -.
DR BioGRID-ORCS; 55667; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; DENND4C; human.
DR GenomeRNAi; 55667; -.
DR Pharos; Q5VZ89; Tbio.
DR PRO; PR:Q5VZ89; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5VZ89; protein.
DR Bgee; ENSG00000137145; Expressed in jejunal mucosa and 201 other tissues.
DR ExpressionAtlas; Q5VZ89; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030904; C:retromer complex; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; IBA:GO_Central.
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; 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 PROSITE; PS50211; DENN; 1.
DR PROSITE; PS51498; MABP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1909
FT /note="DENN domain-containing protein 4C"
FT /id="PRO_0000089697"
FT DOMAIN 40..199
FT /note="MABP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00831"
FT DOMAIN 191..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 821..855
FT /note="PPR"
FT REGION 1243..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 975
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6H8H2"
FT MOD_RES 1278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6H8H2"
FT MOD_RES 1799
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 911
FT /note="S -> SALQNVTGGSDGDTVSHGSVDSSNDANNGEHTVFVRDLIRLESIDNH
FT SST (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027379"
FT VAR_SEQ 1606..1623
FT /note="SDEIKRASGDVQTMKISS -> RYQRVQRPLYVVINGVPL (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027382"
FT VAR_SEQ 1624..1909
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027383"
FT VAR_SEQ 1844..1845
FT /note="SL -> GI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027384"
FT VAR_SEQ 1846..1909
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027386"
FT VARIANT 1227
FT /note="V -> G (in dbSNP:rs34267952)"
FT /id="VAR_061640"
FT VARIANT 1266
FT /note="T -> A (in dbSNP:rs17818730)"
FT /id="VAR_022891"
FT VARIANT 1343
FT /note="N -> H (in dbSNP:rs6475322)"
FT /id="VAR_022892"
FT CONFLICT 683
FT /note="S -> G (in Ref. 3; BAC86313)"
FT /evidence="ECO:0000305"
FT CONFLICT 1297
FT /note="S -> P (in Ref. 3; BAA91294)"
FT /evidence="ECO:0000305"
FT CONFLICT 1656
FT /note="H -> R (in Ref. 3; BAA91478)"
FT /evidence="ECO:0000305"
FT CONFLICT 1769
FT /note="Q -> H (in Ref. 3; BAA92039)"
FT /evidence="ECO:0000305"
FT CONFLICT 1862
FT /note="I -> V (in Ref. 4; CAH10466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1868
FT /note="D -> G (in Ref. 4; CAH10466)"
FT /evidence="ECO:0000305"
FT CONFLICT 1893
FT /note="P -> A (in Ref. 4; CAD39177)"
FT /evidence="ECO:0000305"
FT CONFLICT 1897
FT /note="V -> A (in Ref. 4; CAH10466)"
FT /evidence="ECO:0000305"
FT MOD_RES Q5VZ89-7:953
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
SQ SEQUENCE 1909 AA; 212711 MW; 3AB522323299D990 CRC64;
MIEDKGPRVT DYFVVAGLTD TSTLLDQEIN RLDTKSTGPK APITDIAIII KSAGETVPEG
YTCVEATPSA LQANLNYGSL KSPELFLCYK RGRDKPPLTD IGVLYEGKER LIPGCEVILA
TPYGRCANVN NSSTTSQRIF ITYRRAPPVR PQNSLAVTDI CVIVTSKGET PPHTFCKVDK
NLNCGMWGSS VFLCYKKSVP ASNAIAYKAG LIFRYPEEDY ESFPLSESDV PLFCLPMGAT
IECWDPETKY PLPVFSTFVL TGSSAKKVYG AAIQFYEPYS RELLSEKQLM HLGLLTPVER
KMVSKSINTN KCICLLSHWP FFEAFRKFLM FIYKLSVSGP HPLPIEKHIS HFMQNIPFPS
PQRPRILVQL SVHDALILSQ PVSTPLPLSG ANFSTLLMNL GPENCATLLL FVLLESKILL
HSLRPAVLTG VAEAVVAMIF PFQWQCPYIP LCPLSLAAVL SAPLPFIVGV DSRYFDLHDP
PQDVVCIDLD TNMLYVSDEK KNMNWKQLPK KPCKNLLSTL KKLYPQLSSV HQKTQEGSAI
DMTPIEADFS WQKKMTQLEM EIQEAFLRFM ASILKGYRTY LRPITEAPSN KATAADSLFD
RQGFLKSRDR AYAKFYTLLS KTQIFIRFIE ECSFVSDKDT GLAFFDDCIE KLFPDKGTEK
TDKVDFDSAE DTRLIELDDS QKSEHTVFIM PPEPPPDDGK DLSPKYSYKY FPRLDLKLFD
RPQELKLCFS RHPTGNSITK SPPLMAKRTK QEIKTAHKLA KRCYTNPPQW AKCLFSHCYS
LWFICLPAYV RVSHPKVRAL QQAYDVLIKM RKTDVDPLDE VCYRVVMQLC GLWGHPVLAV
RVLFEMKTAR IKPNAITYGY YNKVVLESPW PSSTRSGIFL WTKVRNVVRG LAQFRQPLKK
TVQRSQVSSI SGGQSDQGYG SKDELIKDDA EIHVPEEQAA RELITKTKMQ TEEVCDASAI
VAKHSQPSPE PHSPTEPPAW GSSIVKVPSG IFDVNSRKSS TGSISNVLFS TQDPVEDAVF
GEATNLKKNG DRGEKRQKHF PERSCSFSSE SRAGMLLKKS SLDSNSSEMA IMMGADAKIL
TAALTCPKTS LLHIARTHSF ENVSCHLPDS RTCMSESTWN PEHRSSPVPE MLEESQELLE
PVVDDVPKTT ATVDTYESLL SDSNSNQSRD LKTVSKDLRN KRSSLYGIAK VVQREDVETG
LDPLSLLATE CTGGKTPDSE DKLFSPVIAR NLADEIESYM NLKSPLGSKS SSMELHREEN
RESGMTTAFI HALERRSSLP LDHGSPAQEN PESEKSSPAV SRSKTFTGRF KQQTPSRTHK
ERSTSLSALV RSSPHGSLGS VVNSLSGLKL DNILSGPKID VLKSGMKQAA TVASKMWVAV
ASAYSYSDDE EETNRDYSFP AGLEDHILGE NISPNTSISG LVPSELTQSN TSLGSSSSSG
DVGKLHYPTG EVPFPRGMKG QDFEKSDHGS SQNTSMSSIY QNCAMEVLMS SCSQCRACGA
LVYDEEIMAG WTADDSNLNT ACPFCKSNFL PLLNIEFKDL RGSASFFLKP STSGDSLQSG
SIPLANESLE HKPVSSLAEP DLINFMDFPK HNQIITEETG SAVEPSDEIK RASGDVQTMK
ISSVPNSLSK RNVSLTRSHS VGGPLQNIDF TQRPFHGIST VSLPNSLQEV VDPLGKRPNP
PPVSVPYLSP LVLRKELESL LENEGDQVIH TSSFINQHPI IFWNLVWYFR RLDLPSNLPG
LILTSEHCNE GVQLPLSSLS QDSKLVYIQL LWDNINLHQE PREPLYVSWR NFNSEKKSSL
LSEEQQETST LVETIRQSIQ HNNVLKPINL LSQQMKPGMK RQRSLYREIL FLSLVSLGRE
NIDIEAFDNE YGIAYNSLSS EILERLQKID APPSASVEWC RKCFGAPLI
