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DENN domain-containing protein 1A (Connecdenn 1) (Connecdenn) (Protein FAM31A)

 DEN1A_HUMAN             Reviewed;        1009 AA.
Q8TEH3; A8MZA3; B1AM80; B7Z3C8; B7Z669; D3PFD3; Q05C88; Q5VWF0;
Q6PJZ5; Q8IVD6; Q9H796;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
27-JUN-2006, sequence version 2.
22-NOV-2017, entry version 117.
RecName: Full=DENN domain-containing protein 1A {ECO:0000312|HGNC:HGNC:29324};
AltName: Full=Connecdenn 1 {ECO:0000303|PubMed:20154091};
Short=Connecdenn {ECO:0000303|PubMed:20154091};
AltName: Full=Protein FAM31A;
Name=DENND1A {ECO:0000312|HGNC:HGNC:29324};
Synonyms=FAM31A {ECO:0000312|HGNC:HGNC:29324}, KIAA1608;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 114-1009 (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 217-1009 (ISOFORM 7).
TISSUE=Artery smooth muscle, Fetal brain, Hippocampus, and Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-520; SER-523;
SER-536; SER-538 AND SER-546, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-546, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
IDENTIFICATION (ISOFORM 1), SUBCELLULAR LOCATION, FUNCTION, AND
INTERACTION WITH AP2A2; CLTC AND RAB35.
PubMed=20154091; DOI=10.1074/jbc.M109.050930;
Marat A.L., McPherson P.S.;
"The connecdenn family, Rab35 guanine nucleotide exchange factors
interfacing with the clathrin machinery.";
J. Biol. Chem. 285:10627-10637(2010).
[11]
FUNCTION, INTERACTION WITH CLATHRIN AND AP-2, AND SUBCELLULAR
LOCATION.
PubMed=20937701; DOI=10.1083/jcb.201008051;
Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
"Family-wide characterization of the DENN domain Rab GDP-GTP exchange
factors.";
J. Cell Biol. 191:367-381(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520; SER-523 AND
SER-592, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
POSSIBLE INVOLVEMENT IN PCOS.
PubMed=22180642; DOI=10.1136/jmedgenet-2011-100427;
Goodarzi M.O., Jones M.R., Li X., Chua A.K., Garcia O.A., Chen Y.D.,
Krauss R.M., Rotter J.I., Ankener W., Legro R.S., Azziz R.,
Strauss J.F. III, Dunaif A., Urbanek M.;
"Replication of association of DENND1A and THADA variants with
polycystic ovary syndrome in European cohorts.";
J. Med. Genet. 49:90-95(2012).
[15]
POSSIBLE INVOLVEMENT IN PCOS.
PubMed=23208300; DOI=10.1093/humrep/des424;
Cui L., Zhao H., Zhang B., Qu Z., Liu J., Liang X., Zhao X., Zhao J.,
Sun Y., Wang P., Li T., Shi Y., Chen Z.J.;
"Genotype-phenotype correlations of PCOS susceptibility SNPs
identified by GWAS in a large cohort of Han Chinese women.";
Hum. Reprod. 28:538-544(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-520; SER-523;
SER-546 AND SER-592, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
POSSIBLE INVOLVEMENT IN PCOS.
PubMed=24086769; DOI=10.1371/journal.pone.0077186;
Eriksen M.B., Nielsen M.F., Brusgaard K., Tan Q., Andersen M.S.,
Glintborg D., Gaster M.;
"Genetic alterations within the DENND1A gene in patients with
polycystic ovary syndrome (PCOS).";
PLoS ONE 8:E77186-E77186(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546 AND SER-749, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
POSSIBLE INVOLVEMENT IN PCOS.
PubMed=25626177; DOI=10.1016/j.gene.2015.01.034;
Gammoh E., Arekat M.R., Saldhana F.L., Madan S., Ebrahim B.H.,
Almawi W.Y.;
"DENND1A gene variants in Bahraini Arab women with polycystic ovary
syndrome.";
Gene 560:30-33(2015).
[20]
ENZYME REGULATION, INTERACTION WITH YWHAE, PHOSPHORYLATION AT SER-536
AND SER-538, AND MUTAGENESIS OF 536-SER--SER-538.
PubMed=26055712; DOI=10.1074/jbc.M115.636712;
Kulasekaran G., Nossova N., Marat A.L., Lund I., Cremer C.,
Ioannou M.S., McPherson P.S.;
"Phosphorylation-dependent regulation of Connecdenn/DENND1 guanine
nucleotide exchange factors.";
J. Biol. Chem. 290:17999-18008(2015).
-!- FUNCTION: Guanine nucleotide exchange factor (GEF) regulating
clathrin-mediated endocytosis through RAB35 activation. Promotes
the exchange of GDP to GTP, converting inactive GDP-bound RAB35
into its active GTP-bound form. Regulates clathrin-mediated
endocytosis of synaptic vesicles and mediates exit from early
endosomes (PubMed:20154091, PubMed:20937701). Binds
phosphatidylinositol-phosphates (PtdInsPs), with some preference
for PtdIns(3)P (By similarity). {ECO:0000250|UniProtKB:Q8K382,
ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701}.
-!- ENZYME REGULATION: The guanine nucleotide exchange factor (GEF)
activity is autoinhibited. Autoinhibition may be the result of
intramolecular interaction between the DENN domain and the C-
terminus, which is disrupted upon phosphorylation. Activation is
regulated by Akt activation. {ECO:0000269|PubMed:26055712}.
-!- SUBUNIT: Interacts with RAB35 (PubMed:20154091). Interacts with
clathrin and with the adapter protein complex 2, AP-2
(PubMed:20154091, PubMed:20937701). Interacts with ITSN1 AND
SH3GL2 (By similarity). Interacts (when phosphorylated) with YWHAE
(PubMed:26055712). {ECO:0000250|UniProtKB:Q8K382,
ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701,
ECO:0000269|PubMed:26055712}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
membrane {ECO:0000269|PubMed:20154091,
ECO:0000269|PubMed:20937701}; Peripheral membrane protein
{ECO:0000269|PubMed:20937701}. Cell junction, synapse, presynaptic
cell membrane {ECO:0000269|PubMed:20937701}. Note=Associates to
membranes via lipid-binding activity.
{ECO:0000250|UniProtKB:Q8K382}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=Q8TEH3-1; Sequence=Displayed;
Name=2;
IsoId=Q8TEH3-2; Sequence=VSP_019464, VSP_019465;
Name=3;
IsoId=Q8TEH3-3; Sequence=VSP_034513, VSP_034514;
Name=4;
IsoId=Q8TEH3-4; Sequence=VSP_034509, VSP_034512, VSP_034513,
VSP_034514;
Name=5;
IsoId=Q8TEH3-5; Sequence=VSP_034510, VSP_034511, VSP_019464,
VSP_019465;
Name=6;
IsoId=Q8TEH3-6; Sequence=VSP_034509, VSP_040666, VSP_040668;
Note=No experimental confirmation available.;
Name=7;
IsoId=Q8TEH3-7; Sequence=VSP_040667, VSP_040668;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated on serine and/or threonine in an Akt-dependent
manner. Phosphorylation probably regulates the guanine nucleotide
exchange factor (GEF) activity, possibly by disrupting an
intramolecular interaction between the DENN domain and the C-
terminus of the protein, thereby relieving the autoinhibition.
{ECO:0000269|PubMed:26055712}.
-!- DISEASE: Note=Genetic variants in DENND1A may play a role in
susceptibility to polycystic ovary syndrome (PCOS), the most
common endocrine disease among premenopausal women. PCOS is a
complex disorder characterized by infertility, hirsutism, obesity,
various menstrual disturbances, and enlarged ovaries studded with
atretic follicles. {ECO:0000269|PubMed:22180642,
ECO:0000269|PubMed:23208300, ECO:0000269|PubMed:24086769,
ECO:0000269|PubMed:25626177}.
-!- SEQUENCE CAUTION:
Sequence=AAH09616.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH28061.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAH13155.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK024782; BAB15002.1; -; mRNA.
EMBL; AK074151; BAB84977.1; -; mRNA.
EMBL; AK295710; BAH12164.1; -; mRNA.
EMBL; AK299867; BAH13155.1; ALT_INIT; mRNA.
EMBL; AL445489; CAI39791.1; -; Genomic_DNA.
EMBL; AL161790; CAI39791.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAI39791.1; JOINED; Genomic_DNA.
EMBL; AC006450; CAI39791.1; JOINED; Genomic_DNA.
EMBL; AL445489; CAI39792.1; -; Genomic_DNA.
EMBL; AC006450; CAI39792.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAI39792.1; JOINED; Genomic_DNA.
EMBL; AL161790; CAI39792.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAH73640.1; -; Genomic_DNA.
EMBL; AC006450; CAH73640.1; JOINED; Genomic_DNA.
EMBL; AL161790; CAH73640.1; JOINED; Genomic_DNA.
EMBL; AL445489; CAH73640.1; JOINED; Genomic_DNA.
EMBL; AL161790; CAI15705.1; -; Genomic_DNA.
EMBL; AC006450; CAI15705.1; JOINED; Genomic_DNA.
EMBL; AL445489; CAI15705.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAI15705.1; JOINED; Genomic_DNA.
EMBL; AL161790; CAI15706.1; -; Genomic_DNA.
EMBL; AC006450; CAI15706.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAI15706.1; JOINED; Genomic_DNA.
EMBL; AL445489; CAI15706.1; JOINED; Genomic_DNA.
EMBL; AL161790; CAI15707.1; -; Genomic_DNA.
EMBL; AC006450; CAI15707.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAI15707.1; JOINED; Genomic_DNA.
EMBL; AL445489; CAI15707.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAH73637.1; -; Genomic_DNA.
EMBL; AC006450; CAH73637.1; JOINED; Genomic_DNA.
EMBL; AL445489; CAH73637.1; JOINED; Genomic_DNA.
EMBL; AL161790; CAH73637.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAH73638.1; -; Genomic_DNA.
EMBL; AC006450; CAH73638.1; JOINED; Genomic_DNA.
EMBL; AL445489; CAH73638.1; JOINED; Genomic_DNA.
EMBL; AL161790; CAH73638.1; JOINED; Genomic_DNA.
EMBL; AL445489; CAI39794.1; -; Genomic_DNA.
EMBL; AC006450; CAI39794.1; JOINED; Genomic_DNA.
EMBL; AL161790; CAI39794.1; JOINED; Genomic_DNA.
EMBL; AL390774; CAI39794.1; JOINED; Genomic_DNA.
EMBL; CH471090; EAW87571.1; -; Genomic_DNA.
EMBL; CH471090; EAW87575.1; -; Genomic_DNA.
EMBL; BC009616; AAH09616.1; ALT_INIT; mRNA.
EMBL; BC028061; AAH28061.1; ALT_INIT; mRNA.
EMBL; BC039703; AAH39703.1; -; mRNA.
EMBL; BK006958; DAA12500.1; -; mRNA.
CCDS; CCDS35133.1; -. [Q8TEH3-1]
CCDS; CCDS35134.1; -. [Q8TEH3-2]
RefSeq; NP_065997.1; NM_020946.1. [Q8TEH3-1]
RefSeq; NP_079096.2; NM_024820.2. [Q8TEH3-2]
UniGene; Hs.744995; -.
ProteinModelPortal; Q8TEH3; -.
SMR; Q8TEH3; -.
BioGrid; 121730; 81.
IntAct; Q8TEH3; 14.
STRING; 9606.ENSP00000362727; -.
iPTMnet; Q8TEH3; -.
PhosphoSitePlus; Q8TEH3; -.
BioMuta; DENND1A; -.
DMDM; 109825594; -.
EPD; Q8TEH3; -.
MaxQB; Q8TEH3; -.
PaxDb; Q8TEH3; -.
PeptideAtlas; Q8TEH3; -.
PRIDE; Q8TEH3; -.
DNASU; 57706; -.
Ensembl; ENST00000373618; ENSP00000362720; ENSG00000119522. [Q8TEH3-4]
Ensembl; ENST00000373620; ENSP00000362722; ENSG00000119522. [Q8TEH3-2]
Ensembl; ENST00000373624; ENSP00000362727; ENSG00000119522. [Q8TEH3-1]
GeneID; 57706; -.
KEGG; hsa:57706; -.
UCSC; uc004bnz.2; human. [Q8TEH3-1]
CTD; 57706; -.
DisGeNET; 57706; -.
EuPathDB; HostDB:ENSG00000119522.15; -.
GeneCards; DENND1A; -.
H-InvDB; HIX0008366; -.
HGNC; HGNC:29324; DENND1A.
HPA; HPA020481; -.
MIM; 613633; gene.
neXtProt; NX_Q8TEH3; -.
OpenTargets; ENSG00000119522; -.
PharmGKB; PA134876117; -.
eggNOG; KOG3569; Eukaryota.
eggNOG; ENOG410XT3N; LUCA.
GeneTree; ENSGT00760000118819; -.
HOVERGEN; HBG059210; -.
InParanoid; Q8TEH3; -.
KO; K20160; -.
OMA; NPFVPSM; -.
OrthoDB; EOG091G083L; -.
PhylomeDB; Q8TEH3; -.
TreeFam; TF343037; -.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; DENND1A; human.
GeneWiki; DENND1A; -.
GenomeRNAi; 57706; -.
PRO; PR:Q8TEH3; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000119522; -.
CleanEx; HS_DENND1A; -.
ExpressionAtlas; Q8TEH3; baseline and differential.
Genevisible; Q8TEH3; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
GO; GO:0030665; C:clathrin-coated vesicle membrane; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0032483; P:regulation of Rab protein signal transduction; IDA:FlyBase.
GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
InterPro; IPR005112; dDENN_dom.
InterPro; IPR001194; DENN_dom.
InterPro; IPR005113; uDENN_dom.
Pfam; PF03455; dDENN; 1.
Pfam; PF02141; DENN; 1.
Pfam; PF03456; uDENN; 1.
SMART; SM00801; dDENN; 1.
SMART; SM00799; DENN; 1.
SMART; SM00800; uDENN; 1.
PROSITE; PS50211; DENN; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Cytoplasmic vesicle; Guanine-nucleotide releasing factor;
Lipid-binding; Membrane; Phosphoprotein; Protein transport;
Reference proteome; Synapse; Transport.
CHAIN 1 1009 DENN domain-containing protein 1A.
/FTId=PRO_0000242680.
DOMAIN 13 145 uDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
DOMAIN 162 298 cDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
DOMAIN 300 378 dDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
MOTIF 381 385 FXDXF motif.
{ECO:0000305|PubMed:20154091}.
MOTIF 569 578 Clathrin box.
{ECO:0000305|PubMed:20154091}.
COMPBIAS 649 995 Pro-rich.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 519 519 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 536 536 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:26055712}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:26055712}.
MOD_RES 546 546 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 592 592 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 749 749 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 32 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_034509.
VAR_SEQ 1 30 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034510.
VAR_SEQ 31 43 PEVQRQFPEDYSD -> MLKWPIPGQVALF (in
isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034511.
VAR_SEQ 33 60 VQRQFPEDYSDQEVLQTLTKFCFPFYVD -> MLKWPIPGQ
VALFQILRCRGNSRRTTVT (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034512.
VAR_SEQ 33 42 VQRQFPEDYS -> MRRPGDHGLQ (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040666.
VAR_SEQ 290 331 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040667.
VAR_SEQ 497 498 VR -> AL (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034513.
VAR_SEQ 499 1009 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034514.
VAR_SEQ 526 526 Q -> HLVKPLRHYAVFLSEDSSDDECQREEGPSSGFTESF
FFSAPFEW (in isoform 6 and isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040668.
VAR_SEQ 527 559 PQPYRTLRESDSAEGDEAESPEQQVRKSTGPVP -> NTIA
TPATLHILQKSITHFAAKFPTRGWTSSSH (in isoform
2 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_019464.
VAR_SEQ 560 1009 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_019465.
MUTAGEN 536 538 SDS->EDE: Phosphomimetic mutant;
abolishes the intramolecular interaction
between the DENN domain and the C-
terminus of the protein.
{ECO:0000269|PubMed:26055712}.
CONFLICT 456 456 E -> G (in Ref. 1; BAB15002).
{ECO:0000305}.
SEQUENCE 1009 AA; 110577 MW; ECEE79CFCD5E2D0C CRC64;
MGSRIKQNPE TTFEVYVEVA YPRTGGTLSD PEVQRQFPED YSDQEVLQTL TKFCFPFYVD
SLTVSQVGQN FTFVLTDIDS KQRFGFCRLS SGAKSCFCIL SYLPWFEVFY KLLNILADYT
TKRQENQWNE LLETLHKLPI PDPGVSVHLS VHSYFTVPDT RELPSIPENR NLTEYFVAVD
VNNMLHLYAS MLYERRILII CSKLSTLTAC IHGSAAMLYP MYWQHVYIPV LPPHLLDYCC
APMPYLIGIH LSLMEKVRNM ALDDVVILNV DTNTLETPFD DLQSLPNDVI SSLKNRLKKV
STTTGDGVAR AFLKAQAAFF GSYRNALKIE PEEPITFCEE AFVSHYRSGA MRQFLQNATQ
LQLFKQFIDG RLDLLNSGEG FSDVFEEEIN MGEYAGSDKL YHQWLSTVRK GSGAILNTVK
TKANPAMKTV YKFAKDHAKM GIKEVKNRLK QKDIAENGCA PTPEEQLPKT APSPLVEAKD
PKLREDRRPI TVHFGQVRPP RPHVVKRPKS NIAVEGRRTS VPSPEQPQPY RTLRESDSAE
GDEAESPEQQ VRKSTGPVPA PPDRAASIDL LEDVFSNLDM EAALQPLGQA KSLEDLRAPK
DLREQPGTFD YQRLDLGGSE RSRGVTVALK LTHPYNKLWS LGQDDMAIPS KPPAASPEKP
SALLGNSLAL PRRPQNRDSI LNPSDKEEVP TPTLGSITIP RPQGRKTPEL GIVPPPPIPR
PAKLQAAGAA LGDVSERLQT DRDRRAALSP GLLPGVVPQG PTELLQPLSP GPGAAGTSSD
ALLALLDPLS TAWSGSTLPS RPATPNVATP FTPQFSFPPA GTPTPFPQPP LNPFVPSMPA
APPTLPLVST PAGPFGAPPA SLGPAFASGL LLSSAGFCAP HRSQPNLSAL SMPNLFGQMP
MGTHTSPLQP LGPPAVAPSR IRTLPLARSS ARAAETKQGL ALRPGDPPLL PPRPPQGLEP
TLQPSAPQQA RDPFEDLLQK TKQDVSPSPA LAPAPDSVEQ LRKQWETFE


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