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DENN domain-containing protein 1B (Connecdenn 2) (Protein FAM31B)

 DEN1B_HUMAN             Reviewed;         775 AA.
Q6P3S1; B5MD89; D3PFD5; Q5T3B8; Q5T3B9; Q5T3C1; Q5TAI8; Q6B0I8;
Q8NDT1; Q8TBE6; Q9H774; Q9NXU2;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
16-MAR-2016, sequence version 2.
22-NOV-2017, entry version 118.
RecName: Full=DENN domain-containing protein 1B {ECO:0000312|HGNC:HGNC:28404};
AltName: Full=Connecdenn 2 {ECO:0000303|PubMed:20154091};
AltName: Full=Protein FAM31B {ECO:0000312|HGNC:HGNC:28404};
Name=DENND1B {ECO:0000312|HGNC:HGNC:28404};
Synonyms=C1orf218 {ECO:0000312|HGNC:HGNC:28404},
FAM31B {ECO:0000312|HGNC:HGNC:28404};
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 GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[2]
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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 427-775 (ISOFORM 5).
TISSUE=Brain, and Testis;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-775 (ISOFORM 3).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-775 (ISOFORM 5).
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, 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).
[9]
IDENTIFICATION (ISOFORM 5), SUBCELLULAR LOCATION, FUNCTION,
INTERACTION WITH AP2A2; AP2B1; CLTC AND RAB35, AND MUTAGENESIS OF
LYS-489; LYS-500; ARG-501; LYS-502; ARG-507 AND LYS-509.
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).
[10]
FUNCTION.
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).
[11]
INVOLVEMENT IN ASTHMA, AND TISSUE SPECIFICITY.
PubMed=20032318; DOI=10.1056/NEJMoa0901867;
Sleiman P.M., Flory J., Imielinski M., Bradfield J.P., Annaiah K.,
Willis-Owen S.A., Wang K., Rafaels N.M., Michel S., Bonnelykke K.,
Zhang H., Kim C.E., Frackelton E.C., Glessner J.T., Hou C.,
Otieno F.G., Santa E., Thomas K., Smith R.M., Glaberson W.R.,
Garris M., Chiavacci R.M., Beaty T.H., Ruczinski I., Orange J.M.,
Allen J., Spergel J.M., Grundmeier R., Mathias R.A., Christie J.D.,
von Mutius E., Cookson W.O., Kabesch M., Moffatt M.F., Grunstein M.M.,
Barnes K.C., Devoto M., Magnusson M., Li H., Grant S.F., Bisgaard H.,
Hakonarson H.;
"Variants of DENND1B associated with asthma in children.";
N. Engl. J. Med. 362:36-44(2010).
[12]
FUNCTION, AND INTERACTION WITH RAB35.
PubMed=24520163; DOI=10.7554/eLife.01623;
Langemeyer L., Nunes Bastos R., Cai Y., Itzen A., Reinisch K.M.,
Barr F.A.;
"Diversity and plasticity in Rab GTPase nucleotide release mechanism
has consequences for Rab activation and inactivation.";
Elife 3:E01623-E01623(2014).
[13]
PHOSPHORYLATION.
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).
[14]
FUNCTION, AND INVOLVEMENT IN ASTHMA.
PubMed=26774822; DOI=10.1016/j.cell.2015.11.052;
Yang C.W., Hojer C.D., Zhou M., Wu X., Wuster A., Lee W.P.,
Yaspan B.L., Chan A.C.;
"Regulation of T cell receptor signaling by DENND1B in TH2 cells and
allergic disease.";
Cell 164:141-155(2016).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-410 IN COMPLEX WITH RAB35.
PubMed=22065758; DOI=10.1073/pnas.1110415108;
Wu X., Bradley M.J., Cai Y., Kummel D., De La Cruz E.M., Barr F.A.,
Reinisch K.M.;
"Insights regarding guanine nucleotide exchange from the structure of
a DENN-domain protein complexed with its Rab GTPase substrate.";
Proc. Natl. Acad. Sci. U.S.A. 108:18672-18677(2011).
-!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB35 that
acts as a regulator of T-cell receptor (TCR) internalization in
TH2 cells (PubMed:20154091, PubMed:20937701, PubMed:24520163,
PubMed:26774822). Acts by promoting the exchange of GDP to GTP,
converting inactive GDP-bound RAB35 into its active GTP-bound form
(PubMed:20154091, PubMed:20937701). Plays a role in clathrin-
mediated endocytosis (PubMed:20154091). Controls cytokine
production in TH2 lymphocytes by controlling the rate of TCR
internalization and routing to endosomes: acts by mediating
clathrin-mediated endocytosis of TCR via its interaction with the
adapter protein complex 2 (AP-2) and GEF activity
(PubMed:26774822). Dysregulation leads to impaired TCR down-
modulation and recycling, affecting cytokine production in TH2
cells (PubMed:26774822). {ECO:0000269|PubMed:20154091,
ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:24520163,
ECO:0000269|PubMed:26774822}.
-!- SUBUNIT: Interacts with RAB35 (PubMed:24520163, PubMed:22065758).
Interacts with clathrin heavy chain/CLTC (PubMed:20154091).
Interacts with components of the adapter protein complex 2 (AP-2)
AP2A2 and AP2B1 (PubMed:20154091). Interacts with CD3E (By
similarity). {ECO:0000250|UniProtKB:Q3U1T9,
ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:22065758,
ECO:0000269|PubMed:24520163}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:20154091}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000269|PubMed:20154091}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=5;
IsoId=Q6P3S1-1; Sequence=Displayed;
Name=2;
IsoId=Q6P3S1-2; Sequence=VSP_028083, VSP_034515;
Name=3;
IsoId=Q6P3S1-3; Sequence=VSP_028083, VSP_028084, VSP_028085;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q6P3S1-4; Sequence=VSP_028082, VSP_028083, VSP_034515;
Note=No experimental confirmation available.;
Name=1; Synonyms=DENND1B-S;
IsoId=Q6P3S1-5; Sequence=VSP_034515;
-!- TISSUE SPECIFICITY: Highly expressed in dendritic and natural
killer cells and at lower levels in other myeloid lineage cells
and in pituitary. Significantly up-regulated in effector memory T-
cells as compared with naive T-cells.
{ECO:0000269|PubMed:20032318}.
-!- DOMAIN: The FXDXF motif mediates interaction the AP-2 complex.
{ECO:0000250|UniProtKB:Q3U1T9}.
-!- DOMAIN: The clathrin box motif mediates interaction with clathrin.
{ECO:0000250|UniProtKB:Q3U1T9}.
-!- PTM: Phosphorylated on serine and/or threonine, possibly
regulating the guanine nucleotide exchange factor (GEF) activity.
{ECO:0000269|PubMed:26055712}.
-!- DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic
disease affecting children and young adults. It is a complex
genetic disorder with a heterogeneous phenotype, largely
attributed to the interactions among many genes and between these
genes and the environment. It is characterized by recurrent
attacks of paroxysmal dyspnea, with wheezing due to spasmodic
contraction of the bronchi. {ECO:0000269|PubMed:20032318,
ECO:0000269|PubMed:26774822}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Asthma susceptibility is probably caused by decreased TCR
down-modulation and recycling in TH2 cells, causing prolonged TCR
signaling and increased cytokine production in TH2 lymphocytes
(PubMed:26774822). {ECO:0000269|PubMed:26774822}.
-!- SEQUENCE CAUTION:
Sequence=AAH74735.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA90918.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15024.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=EAW91280.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AL139136; CAI15312.2; -; Genomic_DNA.
EMBL; AL139136; CAI15313.2; -; Genomic_DNA.
EMBL; AL365258; CAI15313.2; JOINED; Genomic_DNA.
EMBL; AL139136; CAI15314.1; -; Genomic_DNA.
EMBL; AL365258; CAI15314.1; JOINED; Genomic_DNA.
EMBL; AL139136; CAI15315.1; -; Genomic_DNA.
EMBL; AL365258; CAI15315.1; JOINED; Genomic_DNA.
EMBL; AL365258; CAI14212.2; -; Genomic_DNA.
EMBL; AL139136; CAI14212.2; JOINED; Genomic_DNA.
EMBL; AL365258; CAI14213.1; -; Genomic_DNA.
EMBL; AL139136; CAI14213.1; JOINED; Genomic_DNA.
EMBL; AL365258; CAI14214.1; -; Genomic_DNA.
EMBL; AL139136; CAI14214.1; JOINED; Genomic_DNA.
EMBL; CH471067; EAW91280.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471067; EAW91281.1; -; Genomic_DNA.
EMBL; CH471067; EAW91285.1; -; Genomic_DNA.
EMBL; BC022561; AAH22561.1; -; mRNA.
EMBL; BC063877; AAH63877.1; -; mRNA.
EMBL; BC074735; AAH74735.2; ALT_INIT; mRNA.
EMBL; AL831839; CAD38548.1; -; mRNA.
EMBL; AK000061; BAA90918.1; ALT_INIT; mRNA.
EMBL; AK024832; BAB15024.1; ALT_INIT; mRNA.
EMBL; BK006960; DAA12502.1; -; mRNA.
CCDS; CCDS41452.2; -. [Q6P3S1-5]
CCDS; CCDS72996.1; -. [Q6P3S1-4]
CCDS; CCDS72997.1; -. [Q6P3S1-1]
RefSeq; NP_001182144.1; NM_001195215.1. [Q6P3S1-1]
RefSeq; NP_001182145.1; NM_001195216.1.
RefSeq; NP_001287787.1; NM_001300858.1. [Q6P3S1-4]
RefSeq; NP_659414.2; NM_144977.4. [Q6P3S1-5]
UniGene; Hs.125056; -.
UniGene; Hs.745032; -.
PDB; 3TW8; X-ray; 2.10 A; A/C=1-410.
PDBsum; 3TW8; -.
ProteinModelPortal; Q6P3S1; -.
SMR; Q6P3S1; -.
BioGrid; 127867; 2.
IntAct; Q6P3S1; 2.
STRING; 9606.ENSP00000356366; -.
iPTMnet; Q6P3S1; -.
PhosphoSitePlus; Q6P3S1; -.
BioMuta; DENND1B; -.
DMDM; 74749089; -.
MaxQB; Q6P3S1; -.
PaxDb; Q6P3S1; -.
PeptideAtlas; Q6P3S1; -.
PRIDE; Q6P3S1; -.
DNASU; 163486; -.
Ensembl; ENST00000235453; ENSP00000235453; ENSG00000213047. [Q6P3S1-4]
Ensembl; ENST00000367396; ENSP00000356366; ENSG00000213047. [Q6P3S1-5]
Ensembl; ENST00000620048; ENSP00000479816; ENSG00000213047. [Q6P3S1-1]
GeneID; 163486; -.
KEGG; hsa:163486; -.
UCSC; uc001gue.4; human. [Q6P3S1-1]
CTD; 163486; -.
DisGeNET; 163486; -.
EuPathDB; HostDB:ENSG00000213047.11; -.
GeneCards; DENND1B; -.
HGNC; HGNC:28404; DENND1B.
HPA; HPA042586; -.
MIM; 600807; phenotype.
MIM; 613292; gene.
neXtProt; NX_Q6P3S1; -.
OpenTargets; ENSG00000213047; -.
PharmGKB; PA134951951; -.
eggNOG; KOG3569; Eukaryota.
eggNOG; ENOG410XT3N; LUCA.
GeneTree; ENSGT00760000118819; -.
HOVERGEN; HBG059209; -.
InParanoid; Q6P3S1; -.
KO; K20160; -.
OMA; FAKSHAR; -.
OrthoDB; EOG091G083L; -.
TreeFam; TF320336; -.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
GenomeRNAi; 163486; -.
PRO; PR:Q6P3S1; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000213047; -.
CleanEx; HS_DENND1B; -.
ExpressionAtlas; Q6P3S1; baseline and differential.
Genevisible; Q6P3S1; HS.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0032456; P:endocytic recycling; ISS: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:0050776; P:regulation of immune response; ISS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0035745; P:T-helper 2 cell cytokine production; IMP:UniProtKB.
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;
3D-structure; Alternative splicing; Asthma; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Guanine-nucleotide releasing factor;
Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
Transport.
CHAIN 1 775 DENN domain-containing protein 1B.
/FTId=PRO_0000304674.
DOMAIN 14 143 uDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
DOMAIN 180 316 cDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
DOMAIN 318 395 dDENN. {ECO:0000255|PROSITE-
ProRule:PRU00304}.
MOTIF 398 402 FXDXF motif.
{ECO:0000305|PubMed:20154091}.
MOTIF 566 575 Clathrin box.
{ECO:0000305|PubMed:20154091}.
MOD_RES 520 520 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q3U1T9}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U1T9}.
MOD_RES 536 536 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U1T9}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U1T9}.
MOD_RES 552 552 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U1T9}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U1T9}.
VAR_SEQ 1 28 MDCRTKANPDRTFDLVLKVKCHASENED -> MAAAPREEK
RWPQPVFSN (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028082.
VAR_SEQ 150 169 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_028083.
VAR_SEQ 310 315 ALKNKL -> MKAIQW (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_028084.
VAR_SEQ 316 775 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_028085.
VAR_SEQ 415 775 NPRSYQQWVHTVKKGGALFNTAMTKATPAVRTAYKFAKNHA
KLGLKEVKSKLKHKENEEDYGTCSSSVQYTPVYKLHNEKGG
NSEKRKLAQARLKRPLKSLDGALYDDEDDDDIERASKLSSE
DGEEASAYLYESDDSVETRVKTPYSGEMDLLGEILDTLSTH
SSDQGKLAAAKSLDFFRSMDDIDYKPTNKSNAPSENNLAFL
CGGSGDQAEWNLGQDDSALHGKHLPPSPRKRVSSSGLTDSL
FILKEENSNKHLGADNVSDPTSGLDFQLTSPEVSQTDKGKT
EKRETLSQISDDLLIPGLGRHSSTFVPWEKEGKEAKETSED
IGLLHEVVSLCHMTSDFQQSLNISDKNTNGNQT -> KDKL
QYDYPFSQ (in isoform 4, isoform 2 and
isoform 1). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_034515.
VARIANT 216 216 V -> M (in dbSNP:rs7546381).
/FTId=VAR_035055.
MUTAGEN 489 489 K->A: Causes only a slight reduction in
AP2B1-binding.
{ECO:0000269|PubMed:20154091}.
MUTAGEN 500 500 K->A: Greatly reduce AP2B1-binding.
{ECO:0000269|PubMed:20154091}.
MUTAGEN 501 501 R->A: No effect.
{ECO:0000269|PubMed:20154091}.
MUTAGEN 502 502 K->A: Almost completely abolishes AP2B1-
binding. {ECO:0000269|PubMed:20154091}.
MUTAGEN 507 507 R->A: No effect.
{ECO:0000269|PubMed:20154091}.
MUTAGEN 509 509 K->A: Greatly reduce AP2B1-binding.
{ECO:0000269|PubMed:20154091}.
CONFLICT 340 340 S -> Y (in Ref. 3; AAH22561).
{ECO:0000305}.
STRAND 10 12 {ECO:0000244|PDB:3TW8}.
STRAND 14 20 {ECO:0000244|PDB:3TW8}.
STRAND 30 36 {ECO:0000244|PDB:3TW8}.
HELIX 42 52 {ECO:0000244|PDB:3TW8}.
HELIX 57 60 {ECO:0000244|PDB:3TW8}.
HELIX 61 63 {ECO:0000244|PDB:3TW8}.
STRAND 66 74 {ECO:0000244|PDB:3TW8}.
STRAND 80 87 {ECO:0000244|PDB:3TW8}.
STRAND 91 101 {ECO:0000244|PDB:3TW8}.
HELIX 104 119 {ECO:0000244|PDB:3TW8}.
HELIX 123 135 {ECO:0000244|PDB:3TW8}.
HELIX 188 196 {ECO:0000244|PDB:3TW8}.
HELIX 199 209 {ECO:0000244|PDB:3TW8}.
TURN 210 212 {ECO:0000244|PDB:3TW8}.
STRAND 214 220 {ECO:0000244|PDB:3TW8}.
HELIX 222 234 {ECO:0000244|PDB:3TW8}.
TURN 235 238 {ECO:0000244|PDB:3TW8}.
STRAND 243 248 {ECO:0000244|PDB:3TW8}.
HELIX 251 258 {ECO:0000244|PDB:3TW8}.
STRAND 263 268 {ECO:0000244|PDB:3TW8}.
TURN 269 271 {ECO:0000244|PDB:3TW8}.
HELIX 272 276 {ECO:0000244|PDB:3TW8}.
STRAND 284 287 {ECO:0000244|PDB:3TW8}.
TURN 288 291 {ECO:0000244|PDB:3TW8}.
STRAND 292 294 {ECO:0000244|PDB:3TW8}.
HELIX 300 302 {ECO:0000244|PDB:3TW8}.
HELIX 305 315 {ECO:0000244|PDB:3TW8}.
HELIX 318 321 {ECO:0000244|PDB:3TW8}.
HELIX 325 338 {ECO:0000244|PDB:3TW8}.
HELIX 339 341 {ECO:0000244|PDB:3TW8}.
HELIX 357 360 {ECO:0000244|PDB:3TW8}.
HELIX 366 375 {ECO:0000244|PDB:3TW8}.
HELIX 379 391 {ECO:0000244|PDB:3TW8}.
SEQUENCE 775 AA; 86552 MW; ED44D8F693DF3983 CRC64;
MDCRTKANPD RTFDLVLKVK CHASENEDPV VLWKFPEDFG DQEILQSVPK FCFPFDVERV
SQNQVGQHFT FVLTDIESKQ RFGFCRLTSG GTICLCILSY LPWFEVYYKL LNTLADYLAK
ELENDLNETL RSLYNHPVPK ANTPVNLSVN QEIFIACEQV LKDQPALVPH SYFIAPDVTG
LPTIPESRNL TEYFVAVDVN NMLQLYASML HERRIVIISS KLSTLTACIH GSAALLYPMY
WQHIYIPVLP PHLLDYCCAP MPYLIGIHSS LIERVKNKSL EDVVMLNVDT NTLESPFSDL
NNLPSDVVSA LKNKLKKQST ATGDGVARAF LRAQAALFGS YRDALRYKPG EPITFCEESF
VKHRSSVMKQ FLETAINLQL FKQFIDGRLA KLNAGRGFSD VFEEEITSGG FCGGNPRSYQ
QWVHTVKKGG ALFNTAMTKA TPAVRTAYKF AKNHAKLGLK EVKSKLKHKE NEEDYGTCSS
SVQYTPVYKL HNEKGGNSEK RKLAQARLKR PLKSLDGALY DDEDDDDIER ASKLSSEDGE
EASAYLYESD DSVETRVKTP YSGEMDLLGE ILDTLSTHSS DQGKLAAAKS LDFFRSMDDI
DYKPTNKSNA PSENNLAFLC GGSGDQAEWN LGQDDSALHG KHLPPSPRKR VSSSGLTDSL
FILKEENSNK HLGADNVSDP TSGLDFQLTS PEVSQTDKGK TEKRETLSQI SDDLLIPGLG
RHSSTFVPWE KEGKEAKETS EDIGLLHEVV SLCHMTSDFQ QSLNISDKNT NGNQT


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