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Protein

DENN domain-containing protein 1B

Gene

DENND1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).4 Publications

GO - Molecular functioni

  • Rab guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

  • endocytic recycling Source: UniProtKB
  • positive regulation of GTPase activity Source: GOC
  • protein transport Source: UniProtKB-KW
  • regulation of immune response Source: UniProtKB
  • T cell receptor signaling pathway Source: UniProtKB
  • T-helper 2 cell cytokine production Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
DENN domain-containing protein 1BImported
Alternative name(s):
Connecdenn 21 Publication
Protein FAM31BImported
Gene namesi
Name:DENND1BImported
Synonyms:C1orf218Imported, FAM31BImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28404. DENND1B.

Subcellular locationi

  • Cytoplasmcytosol 1 Publication
  • Cytoplasmic vesicleclathrin-coated vesicle 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle

Pathology & Biotechi

Involvement in diseasei

Asthma (ASTHMA)2 Publications
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).1 Publication
Disease descriptionThe 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.
See also OMIM:600807

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi489 – 4891K → A: Causes only a slight reduction in AP2B1-binding. 1 Publication
Mutagenesisi500 – 5001K → A: Greatly reduce AP2B1-binding. 1 Publication
Mutagenesisi501 – 5011R → A: No effect. 1 Publication
Mutagenesisi502 – 5021K → A: Almost completely abolishes AP2B1-binding. 1 Publication
Mutagenesisi507 – 5071R → A: No effect. 1 Publication
Mutagenesisi509 – 5091K → A: Greatly reduce AP2B1-binding. 1 Publication

Keywords - Diseasei

Asthma

Organism-specific databases

MIMi600807. phenotype.
PharmGKBiPA134951951.

Polymorphism and mutation databases

BioMutaiDENND1B.
DMDMi74749089.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 775775DENN domain-containing protein 1BPRO_0000304674Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei652 – 6521PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on serine and/or threonine, possibly regulating the guanine nucleotide exchange factor (GEF) activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6P3S1.
PaxDbiQ6P3S1.
PRIDEiQ6P3S1.

PTM databases

iPTMnetiQ6P3S1.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ6P3S1.
CleanExiHS_DENND1B.
ExpressionAtlasiQ6P3S1. baseline and differential.
GenevisibleiQ6P3S1. HS.

Organism-specific databases

HPAiHPA042586.
HPA045494.

Interactioni

Subunit structurei

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).By similarity3 Publications

Protein-protein interaction databases

BioGridi127867. 2 interactions.
IntActiQ6P3S1. 1 interaction.
STRINGi9606.ENSP00000356366.

Structurei

Secondary structure

1
775
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Beta strandi14 – 207Combined sources
Beta strandi30 – 367Combined sources
Helixi42 – 5211Combined sources
Helixi57 – 604Combined sources
Helixi61 – 633Combined sources
Beta strandi66 – 749Combined sources
Beta strandi80 – 878Combined sources
Beta strandi91 – 10111Combined sources
Helixi104 – 11916Combined sources
Helixi123 – 13513Combined sources
Helixi188 – 1969Combined sources
Helixi199 – 20911Combined sources
Turni210 – 2123Combined sources
Beta strandi214 – 2207Combined sources
Helixi222 – 23413Combined sources
Turni235 – 2384Combined sources
Beta strandi243 – 2486Combined sources
Helixi251 – 2588Combined sources
Beta strandi263 – 2686Combined sources
Turni269 – 2713Combined sources
Helixi272 – 2765Combined sources
Beta strandi284 – 2874Combined sources
Turni288 – 2914Combined sources
Beta strandi292 – 2943Combined sources
Helixi300 – 3023Combined sources
Helixi305 – 31511Combined sources
Helixi318 – 3214Combined sources
Helixi325 – 33814Combined sources
Helixi339 – 3413Combined sources
Helixi357 – 3604Combined sources
Helixi366 – 37510Combined sources
Helixi379 – 39113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TW8X-ray2.10A/C1-410[»]
ProteinModelPortaliQ6P3S1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 8968UDENNAdd
BLAST
Domaini90 – 291202DENNPROSITE-ProRule annotationAdd
BLAST
Domaini322 – 38867dDENNPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi398 – 4025FXDXF motif1 Publication
Motifi566 – 57510Clathrin box1 Publication

Domaini

The FXDXF motif mediates interaction the AP-2 complex.By similarity
The clathrin box motif mediates interaction with clathrin.By similarity

Sequence similaritiesi

Contains 1 dDENN domain.PROSITE-ProRule annotation
Contains 1 DENN domain.PROSITE-ProRule annotation
Contains 1 uDENN domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3569. Eukaryota.
ENOG410XT3N. LUCA.
GeneTreeiENSGT00760000118819.
HOVERGENiHBG059209.
InParanoidiQ6P3S1.
OMAiFAKSHAR.
OrthoDBiEOG73Z2SH.
TreeFamiTF320336.

Family and domain databases

InterProiIPR005112. dDENN_dom.
IPR001194. DENN_dom.
IPR005113. uDENN_dom.
[Graphical view]
PfamiPF03455. dDENN. 1 hit.
PF02141. DENN. 1 hit.
PF03456. uDENN. 1 hit.
[Graphical view]
SMARTiSM00801. dDENN. 1 hit.
SM00799. DENN. 1 hit.
SM00800. uDENN. 1 hit.
[Graphical view]
PROSITEiPS50947. DDENN. 1 hit.
PS50211. DENN. 1 hit.
PS50946. UDENN. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 5 (identifier: Q6P3S1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDCRTKANPD RTFDLVLKVK CHASENEDPV VLWKFPEDFG DQEILQSVPK
60 70 80 90 100
FCFPFDVERV SQNQVGQHFT FVLTDIESKQ RFGFCRLTSG GTICLCILSY
110 120 130 140 150
LPWFEVYYKL LNTLADYLAK ELENDLNETL RSLYNHPVPK ANTPVNLSVN
160 170 180 190 200
QEIFIACEQV LKDQPALVPH SYFIAPDVTG LPTIPESRNL TEYFVAVDVN
210 220 230 240 250
NMLQLYASML HERRIVIISS KLSTLTACIH GSAALLYPMY WQHIYIPVLP
260 270 280 290 300
PHLLDYCCAP MPYLIGIHSS LIERVKNKSL EDVVMLNVDT NTLESPFSDL
310 320 330 340 350
NNLPSDVVSA LKNKLKKQST ATGDGVARAF LRAQAALFGS YRDALRYKPG
360 370 380 390 400
EPITFCEESF VKHRSSVMKQ FLETAINLQL FKQFIDGRLA KLNAGRGFSD
410 420 430 440 450
VFEEEITSGG FCGGNPRSYQ QWVHTVKKGG ALFNTAMTKA TPAVRTAYKF
460 470 480 490 500
AKNHAKLGLK EVKSKLKHKE NEEDYGTCSS SVQYTPVYKL HNEKGGNSEK
510 520 530 540 550
RKLAQARLKR PLKSLDGALY DDEDDDDIER ASKLSSEDGE EASAYLYESD
560 570 580 590 600
DSVETRVKTP YSGEMDLLGE ILDTLSTHSS DQGKLAAAKS LDFFRSMDDI
610 620 630 640 650
DYKPTNKSNA PSENNLAFLC GGSGDQAEWN LGQDDSALHG KHLPPSPRKR
660 670 680 690 700
VSSSGLTDSL FILKEENSNK HLGADNVSDP TSGLDFQLTS PEVSQTDKGK
710 720 730 740 750
TEKRETLSQI SDDLLIPGLG RHSSTFVPWE KEGKEAKETS EDIGLLHEVV
760 770
SLCHMTSDFQ QSLNISDKNT NGNQT
Length:775
Mass (Da):86,552
Last modified:March 16, 2016 - v2
Checksum:iED44D8F693DF3983
GO
Isoform 2 (identifier: Q6P3S1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-169: Missing.
     415-775: NPRSYQQWVH...SDKNTNGNQT → KDKLQYDYPFSQ

Show »
Length:406
Mass (Da):46,023
Checksum:iF447B1AC261D9D1C
GO
Isoform 3 (identifier: Q6P3S1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-169: Missing.
     310-315: ALKNKL → MKAIQW
     316-775: Missing.

Note: No experimental confirmation available.
Show »
Length:295
Mass (Da):33,701
Checksum:iAEE0F8F8B6791EF4
GO
Isoform 4 (identifier: Q6P3S1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: MDCRTKANPDRTFDLVLKVKCHASENED → MAAAPREEKRWPQPVFSN
     150-169: Missing.
     415-775: NPRSYQQWVH...SDKNTNGNQT → KDKLQYDYPFSQ

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):44,901
Checksum:iEE50301A6487BABF
GO
Isoform 1 (identifier: Q6P3S1-5) [UniParc]FASTAAdd to basket

Also known as: DENND1B-S

The sequence of this isoform differs from the canonical sequence as follows:
     415-775: NPRSYQQWVH...SDKNTNGNQT → KDKLQYDYPFSQ

Show »
Length:426
Mass (Da):48,260
Checksum:i811670F3F2F6897F
GO

Sequence cautioni

The sequence AAH74735.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA90918.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15024.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW91280.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti340 – 3401S → Y in AAH22561 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti216 – 2161V → M.
Corresponds to variant rs7546381 [ dbSNP | Ensembl ].
VAR_035055

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828MDCRT…SENED → MAAAPREEKRWPQPVFSN in isoform 4. 1 PublicationVSP_028082Add
BLAST
Alternative sequencei150 – 16920Missing in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_028083Add
BLAST
Alternative sequencei310 – 3156ALKNKL → MKAIQW in isoform 3. 1 PublicationVSP_028084
Alternative sequencei316 – 775460Missing in isoform 3. 1 PublicationVSP_028085Add
BLAST
Alternative sequencei415 – 775361NPRSY…NGNQT → KDKLQYDYPFSQ in isoform 4, isoform 2 and isoform 1. 2 PublicationsVSP_034515Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL139136 Genomic DNA. Translation: CAI15312.2.
AL139136, AL365258 Genomic DNA. Translation: CAI15313.2.
AL139136, AL365258 Genomic DNA. Translation: CAI15314.1.
AL139136, AL365258 Genomic DNA. Translation: CAI15315.1.
AL365258, AL139136 Genomic DNA. Translation: CAI14212.2.
AL365258, AL139136 Genomic DNA. Translation: CAI14213.1.
AL365258, AL139136 Genomic DNA. Translation: CAI14214.1.
CH471067 Genomic DNA. Translation: EAW91280.1. Sequence problems.
CH471067 Genomic DNA. Translation: EAW91281.1.
CH471067 Genomic DNA. Translation: EAW91285.1.
BC022561 mRNA. Translation: AAH22561.1.
BC063877 mRNA. Translation: AAH63877.1.
BC074735 mRNA. Translation: AAH74735.2. Different initiation.
AL831839 mRNA. Translation: CAD38548.1.
AK000061 mRNA. Translation: BAA90918.1. Different initiation.
AK024832 mRNA. Translation: BAB15024.1. Different initiation.
BK006960 mRNA. Translation: DAA12502.1.
CCDSiCCDS41452.2. [Q6P3S1-5]
CCDS72996.1. [Q6P3S1-4]
CCDS72997.1. [Q6P3S1-1]
RefSeqiNP_001182144.1. NM_001195215.1. [Q6P3S1-1]
NP_001182145.1. NM_001195216.1.
NP_001287787.1. NM_001300858.1. [Q6P3S1-4]
NP_659414.2. NM_144977.4. [Q6P3S1-5]
UniGeneiHs.125056.
Hs.745032.

Genome annotation databases

EnsembliENST00000235453; ENSP00000235453; ENSG00000213047. [Q6P3S1-4]
ENST00000367396; ENSP00000356366; ENSG00000213047. [Q6P3S1-5]
ENST00000620048; ENSP00000479816; ENSG00000213047. [Q6P3S1-1]
GeneIDi163486.
KEGGihsa:163486.
UCSCiuc001gue.4. human. [Q6P3S1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL139136 Genomic DNA. Translation: CAI15312.2.
AL139136, AL365258 Genomic DNA. Translation: CAI15313.2.
AL139136, AL365258 Genomic DNA. Translation: CAI15314.1.
AL139136, AL365258 Genomic DNA. Translation: CAI15315.1.
AL365258, AL139136 Genomic DNA. Translation: CAI14212.2.
AL365258, AL139136 Genomic DNA. Translation: CAI14213.1.
AL365258, AL139136 Genomic DNA. Translation: CAI14214.1.
CH471067 Genomic DNA. Translation: EAW91280.1. Sequence problems.
CH471067 Genomic DNA. Translation: EAW91281.1.
CH471067 Genomic DNA. Translation: EAW91285.1.
BC022561 mRNA. Translation: AAH22561.1.
BC063877 mRNA. Translation: AAH63877.1.
BC074735 mRNA. Translation: AAH74735.2. Different initiation.
AL831839 mRNA. Translation: CAD38548.1.
AK000061 mRNA. Translation: BAA90918.1. Different initiation.
AK024832 mRNA. Translation: BAB15024.1. Different initiation.
BK006960 mRNA. Translation: DAA12502.1.
CCDSiCCDS41452.2. [Q6P3S1-5]
CCDS72996.1. [Q6P3S1-4]
CCDS72997.1. [Q6P3S1-1]
RefSeqiNP_001182144.1. NM_001195215.1. [Q6P3S1-1]
NP_001182145.1. NM_001195216.1.
NP_001287787.1. NM_001300858.1. [Q6P3S1-4]
NP_659414.2. NM_144977.4. [Q6P3S1-5]
UniGeneiHs.125056.
Hs.745032.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TW8X-ray2.10A/C1-410[»]
ProteinModelPortaliQ6P3S1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127867. 2 interactions.
IntActiQ6P3S1. 1 interaction.
STRINGi9606.ENSP00000356366.

PTM databases

iPTMnetiQ6P3S1.

Polymorphism and mutation databases

BioMutaiDENND1B.
DMDMi74749089.

Proteomic databases

MaxQBiQ6P3S1.
PaxDbiQ6P3S1.
PRIDEiQ6P3S1.

Protocols and materials databases

DNASUi163486.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000235453; ENSP00000235453; ENSG00000213047. [Q6P3S1-4]
ENST00000367396; ENSP00000356366; ENSG00000213047. [Q6P3S1-5]
ENST00000620048; ENSP00000479816; ENSG00000213047. [Q6P3S1-1]
GeneIDi163486.
KEGGihsa:163486.
UCSCiuc001gue.4. human. [Q6P3S1-1]

Organism-specific databases

CTDi163486.
GeneCardsiDENND1B.
HGNCiHGNC:28404. DENND1B.
HPAiHPA042586.
HPA045494.
MIMi600807. phenotype.
613292. gene.
neXtProtiNX_Q6P3S1.
PharmGKBiPA134951951.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3569. Eukaryota.
ENOG410XT3N. LUCA.
GeneTreeiENSGT00760000118819.
HOVERGENiHBG059209.
InParanoidiQ6P3S1.
OMAiFAKSHAR.
OrthoDBiEOG73Z2SH.
TreeFamiTF320336.

Miscellaneous databases

GenomeRNAii163486.
PROiQ6P3S1.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P3S1.
CleanExiHS_DENND1B.
ExpressionAtlasiQ6P3S1. baseline and differential.
GenevisibleiQ6P3S1. HS.

Family and domain databases

InterProiIPR005112. dDENN_dom.
IPR001194. DENN_dom.
IPR005113. uDENN_dom.
[Graphical view]
PfamiPF03455. dDENN. 1 hit.
PF02141. DENN. 1 hit.
PF03456. uDENN. 1 hit.
[Graphical view]
SMARTiSM00801. dDENN. 1 hit.
SM00799. DENN. 1 hit.
SM00800. uDENN. 1 hit.
[Graphical view]
PROSITEiPS50947. DDENN. 1 hit.
PS50211. DENN. 1 hit.
PS50946. UDENN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 427-775 (ISOFORM 5).
    Tissue: Brain and Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-775 (ISOFORM 3).
    Tissue: Brain.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-775 (ISOFORM 5).
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    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.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery."
    Marat A.L., McPherson P.S.
    J. Biol. Chem. 285:10627-10637(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM 5), SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH AP2A2; AP2B1; CLTC AND RAB35, MUTAGENESIS OF LYS-489; LYS-500; ARG-501; LYS-502; ARG-507 AND LYS-509.
  10. "Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors."
    Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.
    J. Cell Biol. 191:367-381(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: INVOLVEMENT IN ASTHMA, TISSUE SPECIFICITY.
  12. "Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation."
    Langemeyer L., Nunes Bastos R., Cai Y., Itzen A., Reinisch K.M., Barr F.A.
    Elife 3:E01623-E01623(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB35.
  13. "Phosphorylation-dependent regulation of Connecdenn/DENND1 guanine nucleotide exchange factors."
    Kulasekaran G., Nossova N., Marat A.L., Lund I., Cremer C., Ioannou M.S., McPherson P.S.
    J. Biol. Chem. 290:17999-18008(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  14. "Regulation of T cell receptor signaling by DENND1B in TH2 cells and allergic disease."
    Yang C.W., Hojer C.D., Zhou M., Wu X., Wuster A., Lee W.P., Yaspan B.L., Chan A.C.
    Cell 164:141-155(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INVOLVEMENT IN ASTHMA.
  15. "Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate."
    Wu X., Bradley M.J., Cai Y., Kummel D., De La Cruz E.M., Barr F.A., Reinisch K.M.
    Proc. Natl. Acad. Sci. U.S.A. 108:18672-18677(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-410 IN COMPLEX WITH RAB35.

Entry informationi

Entry nameiDEN1B_HUMAN
AccessioniPrimary (citable) accession number: Q6P3S1
Secondary accession number(s): B5MD89
, D3PFD5, Q5T3B8, Q5T3B9, Q5T3C1, Q5TAI8, Q6B0I8, Q8NDT1, Q8TBE6, Q9H774, Q9NXU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 16, 2016
Last modified: June 8, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.