Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96N67

- DOCK7_HUMAN

UniProt

Q96N67 - DOCK7_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dedicator of cytokinesis protein 7

Gene

DOCK7

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

Functioni

Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization (PubMed:16982419). Has a role in pigmentation (By similarity). Involved in the regulation of cortical neurogenesis through the control of radial glial cells (RGCs) proliferation versus differentiation; negatively regulates the basal-to-apical interkinetic nuclear migration of RGCs by antagonizing the microtubule growth-promoting function of TACC3 (By similarity).By similarity1 Publication

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW
  2. Rac GTPase binding Source: BHF-UCL

GO - Biological processi

  1. activation of Rac GTPase activity Source: BHF-UCL
  2. axonogenesis Source: BHF-UCL
  3. establishment of neuroblast polarity Source: BHF-UCL
  4. hematopoietic progenitor cell differentiation Source: Ensembl
  5. interkinetic nuclear migration Source: UniProtKB
  6. microtubule cytoskeleton organization Source: BHF-UCL
  7. neuron projection development Source: BHF-UCL
  8. pigmentation Source: Ensembl
  9. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  10. regulation of neurogenesis Source: UniProtKB
  11. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Guanine-nucleotide releasing factor

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Dedicator of cytokinesis protein 7
Gene namesi
Name:DOCK7
Synonyms:KIAA1771
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:19190. DOCK7.

Subcellular locationi

Cell projectionaxon 1 Publication
Note: Enriched in the developing axons of hippocampal neurons.

GO - Cellular componenti

  1. axon Source: BHF-UCL
  2. basal part of cell Source: BHF-UCL
  3. focal adhesion Source: UniProtKB
  4. growth cone Source: BHF-UCL
  5. neuron projection Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Involvement in diseasei

Epileptic encephalopathy, early infantile, 23 (EIEE23) [MIM:615859]: A severe disease characterized by early-onset intractable epilepsy, dysmorphic features, intellectual disability, and cortical blindness. Brain imaging shows an abnormally marked pontobulbar sulcus with mild pontine hypoplasia, white matter abnormalities, and atrophy in the occipital lobe.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Epilepsy

Organism-specific databases

MIMi615859. phenotype.
PharmGKBiPA134872825.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21402140Dedicator of cytokinesis protein 7PRO_0000189995Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei30 – 301Phosphoserine2 Publications
Modified residuei180 – 1801Phosphoserine3 Publications
Modified residuei182 – 1821Phosphoserine2 Publications
Modified residuei882 – 8821Phosphoserine1 Publication
Modified residuei888 – 8881Phosphoserine1 Publication
Modified residuei896 – 8961Phosphoserine1 Publication
Modified residuei900 – 9001Phosphoserine2 Publications
Modified residuei905 – 9051Phosphoserine1 Publication
Modified residuei907 – 9071Phosphothreonine2 Publications
Modified residuei909 – 9091Phosphothreonine1 Publication
Modified residuei910 – 9101Phosphoserine2 Publications
Modified residuei1383 – 13831Phosphoserine2 Publications
Modified residuei1430 – 14301Phosphoserine1 Publication
Modified residuei1432 – 14321Phosphoserine1 Publication
Modified residuei1438 – 14381Phosphoserine1 Publication
Modified residuei1962 – 19621N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96N67.
PaxDbiQ96N67.
PRIDEiQ96N67.

PTM databases

PhosphoSiteiQ96N67.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ96N67.
CleanExiHS_DOCK7.
ExpressionAtlasiQ96N67. baseline and differential.
GenevestigatoriQ96N67.

Organism-specific databases

HPAiHPA008607.

Interactioni

Subunit structurei

Interacts with TSC1. Interacts with nucleotide-free RAC1 and RAC3. Interacts with TACC3 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi124527. 46 interactions.
IntActiQ96N67. 30 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ96N67.
SMRiQ96N67. Positions 1839-2111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini561 – 727167DHR-1Add
BLAST
Domaini1678 – 2114437DHR-2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili365 – 39531Sequence AnalysisAdd
BLAST
Coiled coili2086 – 211227Sequence AnalysisAdd
BLAST

Domaini

The DHR-2 domain mediates GEF activity.

Sequence similaritiesi

Belongs to the DOCK family.Curated
Contains 1 DHR-1 domain.Curated
Contains 1 DHR-2 domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG242127.
GeneTreeiENSGT00760000119234.
HOVERGENiHBG051390.
InParanoidiQ96N67.
OMAiYIHYVFR.
PhylomeDBiQ96N67.
TreeFamiTF313629.

Family and domain databases

InterProiIPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR021816. DOCK_C/D_N.
[Graphical view]
PANTHERiPTHR23317. PTHR23317. 1 hit.
PfamiPF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF11878. DUF3398. 1 hit.
[Graphical view]
PROSITEiPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96N67-1) [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
MAERRAFAQK ISRTVAAEVR KQISGQYSGS PQLLKNLNIV GNISHHTTVP
60 70 80 90 100
LTEAVDPVDL EDYLITHPLA VDSGPLRDLI EFPPDDIEVV YSPRDCRTLV
110 120 130 140 150
SAVPEESEMD PHVRDCIRSY TEDWAIVIRK YHKLGTGFNP NTLDKQKERQ
160 170 180 190 200
KGLPKQVFES DEAPDGNSYQ DDQDDLKRRS MSIDDTPRGS WACSIFDLKN
210 220 230 240 250
SLPDALLPNL LDRTPNEEID RQNDDQRKSN RHKELFALHP SPDEEEPIER
260 270 280 290 300
LSVPDIPKEH FGQRLLVKCL SLKFEIEIEP IFASLALYDV KEKKKISENF
310 320 330 340 350
YFDLNSEQMK GLLRPHVPPA AITTLARSAI FSITYPSQDV FLVIKLEKVL
360 370 380 390 400
QQGDIGECAE PYMIFKEADA TKNKEKLEKL KSQADQFCQR LGKYRMPFAW
410 420 430 440 450
TAIHLMNIVS SAGSLERDST EVEISTGERK GSWSERRNSS IVGRRSLERT
460 470 480 490 500
TSGDDACNLT SFRPATLTVT NFFKQEGDRL SDEDLYKFLA DMRRPSSVLR
510 520 530 540 550
RLRPITAQLK IDISPAPENP HYCLTPELLQ VKLYPDSRVR PTREILEFPA
560 570 580 590 600
RDVYVPNTTY RNLLYIYPQS LNFANRQGSA RNITVKVQFM YGEDPSNAMP
610 620 630 640 650
VIFGKSSCSE FSKEAYTAVV YHNRSPDFHE EIKVKLPATL TDHHHLLFTF
660 670 680 690 700
YHVSCQQKQN TPLETPVGYT WIPMLQNGRL KTGQFCLPVS LEKPPQAYSV
710 720 730 740 750
LSPEVPLPGM KWVDNHKGVF NVEVVAVSSI HTQDPYLDKF FALVNALDEH
760 770 780 790 800
LFPVRIGDMR IMENNLENEL KSSISALNSS QLEPVVRFLH LLLDKLILLV
810 820 830 840 850
IRPPVIAGQI VNLGQASFEA MASIINRLHK NLEGNHDQHG RNSLLASYIH
860 870 880 890 900
YVFRLPNTYP NSSSPGPGGL GGSVHYATMA RSAVRPASLN LNRSRSLSNS
910 920 930 940 950
NPDISGTPTS PDDEVRSIIG SKGLDRSNSW VNTGGPKAAP WGSNPSPSAE
960 970 980 990 1000
STQAMDRSCN RMSSHTETSS FLQTLTGRLP TKKLFHEELA LQWVVCSGSV
1010 1020 1030 1040 1050
RESALQQAWF FFELMVKSMV HHLYFNDKLE APRKSRFPER FMDDIAALVS
1060 1070 1080 1090 1100
TIASDIVSRF QKDTEMVERL NTSLAFFLND LLSVMDRGFV FSLIKSCYKQ
1110 1120 1130 1140 1150
VSSKLYSLPN PSVLVSLRLD FLRIICSHEH YVTLNLPCSL LTPPASPSPS
1160 1170 1180 1190 1200
VSSATSQSSG FSTNVQDQKI ANMFELSVPF RQQHYLAGLV LTELAVILDP
1210 1220 1230 1240 1250
DAEGLFGLHK KVINMVHNLL SSHDSDPRYS DPQIKARVAM LYLPLIGIIM
1260 1270 1280 1290 1300
ETVPQLYDFT ETHNQRGRPI CIATDDYESE SGSMISQTVA MAIAGTSVPQ
1310 1320 1330 1340 1350
LTRPGSFLLT STSGRQHTTF SAESSRSLLI CLLWVLKNAD ETVLQKWFTD
1360 1370 1380 1390 1400
LSVLQLNRLL DLLYLCVSCF EYKGKKVFER MNSLTFKKSK DMRAKLEEAI
1410 1420 1430 1440 1450
LGSIGARQEM VRRSRGQLGT YTIASPPERS PSGSAFGSQE NLRWRKDMTH
1460 1470 1480 1490 1500
WRQNTEKLDK SRAEIEHEAL IDGNLATEAN LIILDTLEIV VQTVSVTESK
1510 1520 1530 1540 1550
ESILGGVLKV LLHSMACNQS AVYLQHCFAT QRALVSKFPE LLFEEETEQC
1560 1570 1580 1590 1600
ADLCLRLLRH CSSSIGTIRS HASASLYLLM RQNFEIGNNF ARVKMQVTMS
1610 1620 1630 1640 1650
LSSLVGTSQN FNEEFLRRSL KTILTYAEED LELRETTFPD QVQDLVFNLH
1660 1670 1680 1690 1700
MILSDTVKMK EHQEDPEMLI DLMYRIAKGY QTSPDLRLTW LQNMAGKHSE
1710 1720 1730 1740 1750
RSNHAEAAQC LVHSAALVAE YLSMLEDRKY LPVGCVTFQN ISSNVLEESA
1760 1770 1780 1790 1800
VSDDVVSPDE EGICSGKYFT ESGLVGLLEQ AAASFSMAGM YEAVNEVYKV
1810 1820 1830 1840 1850
LIPIHEANRD AKKLSTIHGK LQEAFSKIVH QSTGWERMFG TYFRVGFYGT
1860 1870 1880 1890 1900
KFGDLDEQEF VYKEPAITKL AEISHRLEGF YGERFGEDVV EVIKDSNPVD
1910 1920 1930 1940 1950
KCKLDPNKAY IQITYVEPYF DTYEMKDRIT YFDKNYNLRR FMYCTPFTLD
1960 1970 1980 1990 2000
GRAHGELHEQ FKRKTILTTS HAFPYIKTRV NVTHKEEIIL TPIEVAIEDM
2010 2020 2030 2040 2050
QKKTQELAFA THQDPADPKM LQMVLQGSVG TTVNQGPLEV AQVFLSEIPS
2060 2070 2080 2090 2100
DPKLFRHHNK LRLCFKDFTK RCEDALRKNK SLIGPDQKEY QRELERNYHR
2110 2120 2130 2140
LKEALQPLIN RKIPQLYKAV LPVTCHRDSF SRMSLRKMDL
Length:2,140
Mass (Da):242,561
Last modified:January 9, 2007 - v4
Checksum:iA14857DCB9C3AE6E
GO
Isoform 2 (identifier: Q96N67-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1419-1427: Missing.
     1832-1836: STGWE → DGK

Note: Contains a phosphoserine at position 1429. Contains a phosphoserine at position 1421. Contains a phosphoserine at position 1425.

Show »
Length:2,129
Mass (Da):241,412
Checksum:i56C741287C8296C4
GO
Isoform 3 (identifier: Q96N67-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     923-953: Missing.
     1419-1427: Missing.

Note: Contains a phosphoserine at position 1398. Contains a phosphoserine at position 1390. Contains a phosphoserine at position 1394.

Show »
Length:2,100
Mass (Da):238,534
Checksum:i4A44093C2074BD4B
GO
Isoform 4 (identifier: Q96N67-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     923-953: Missing.
     1419-1427: Missing.
     1832-1836: STGWE → DGK

Note: Contains a phosphoserine at position 1398. Contains a phosphoserine at position 1390. Contains a phosphoserine at position 1394.

Show »
Length:2,098
Mass (Da):238,274
Checksum:iA768EB92CB1CDB3D
GO
Isoform 5 (identifier: Q96N67-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     923-953: Missing.

Show »
Length:2,109
Mass (Da):239,422
Checksum:i0171AA19EEB3B57F
GO
Isoform 6 (identifier: Q96N67-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1419-1427: Missing.

Note: Contains a phosphoserine at position 1429. Contains a phosphoserine at position 1421. Contains a phosphoserine at position 1425.

Show »
Length:2,131
Mass (Da):241,673
Checksum:i2C21C8938ACE0AD5
GO
Isoform 7 (identifier: Q96N67-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     601-632: VIFGKSSCSEFSKEAYTAVVYHNRSPDFHEEI → SPSCTHPIPTVRPLPLWCYHSIFSLLSWDFIT
     633-2140: Missing.

Note: No experimental confirmation available.

Show »
Length:632
Mass (Da):72,236
Checksum:i5CD59D3E484D8F1F
GO

Sequence cautioni

The sequence AAH16392.2 differs from that shown. Reason: Frameshift at position 1337.
The sequence ABC33725.1 differs from that shown. Reason: Frameshift at position 911.
The sequence BAB71042.1 differs from that shown. Reason: Frameshift at position 1792.
The sequence BAB70933.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC86032.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti750 – 7501H → R in BAC86032. (PubMed:14702039)Curated
Sequence conflicti1440 – 14401E → G in BAC86032. (PubMed:14702039)Curated
Sequence conflicti1520 – 15201S → N in BAB70933. (PubMed:14702039)Curated
Sequence conflicti1521 – 15211A → V in BAC86032. (PubMed:14702039)Curated
Sequence conflicti1639 – 16391P → L in BAC86032. (PubMed:14702039)Curated
Sequence conflicti1859 – 18591E → K in BAB70933. (PubMed:14702039)Curated
Sequence conflicti1908 – 19081K → T in BAB71042. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti824 – 8241I → T.
Corresponds to variant rs35400360 [ dbSNP | Ensembl ].
VAR_057524

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei601 – 63232VIFGK…FHEEI → SPSCTHPIPTVRPLPLWCYH SIFSLLSWDFIT in isoform 7. 1 PublicationVSP_054534Add
BLAST
Alternative sequencei633 – 21401508Missing in isoform 7. 1 PublicationVSP_054535Add
BLAST
Alternative sequencei923 – 95331Missing in isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_012440Add
BLAST
Alternative sequencei1419 – 14279Missing in isoform 2, isoform 3, isoform 4 and isoform 6. 4 PublicationsVSP_022240
Alternative sequencei1832 – 18365STGWE → DGK in isoform 2 and isoform 4. 4 PublicationsVSP_007707

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ341187 mRNA. Translation: ABC68221.1.
AK055401 mRNA. Translation: BAB70917.1.
AK055493 mRNA. Translation: BAB70933.1. Different initiation.
AK055905 mRNA. Translation: BAB71042.1. Frameshift.
AK125049 mRNA. Translation: BAC86032.1. Different initiation.
AK292640 mRNA. Translation: BAF85329.1.
AL451044
, AC096946, AC103923, AL138847 Genomic DNA. Translation: CAI13104.1.
AL451044, AC096946 Genomic DNA. Translation: CAI13105.1.
AL138847
, AC096946, AC103923, AL451044 Genomic DNA. Translation: CAI22995.1.
CH471059 Genomic DNA. Translation: EAX06582.1.
DQ309763 mRNA. Translation: ABC33725.1. Frameshift.
DQ118679 mRNA. Translation: AAZ38451.1.
DQ118680 mRNA. Translation: AAZ38452.1.
AB051558 mRNA. Translation: BAB21862.1.
BC016392 mRNA. Translation: AAH16392.2. Frameshift.
CCDSiCCDS30734.1. [Q96N67-5]
CCDS60156.1. [Q96N67-2]
CCDS60157.1. [Q96N67-7]
RefSeqiNP_001258928.1. NM_001271999.1. [Q96N67-2]
NP_001258929.1. NM_001272000.1. [Q96N67-3]
NP_001258930.1. NM_001272001.1. [Q96N67-4]
NP_001258931.1. NM_001272002.1. [Q96N67-7]
NP_212132.2. NM_033407.3. [Q96N67-5]
XP_005271349.1. XM_005271292.1. [Q96N67-6]
UniGeneiHs.744927.

Genome annotation databases

EnsembliENST00000251157; ENSP00000251157; ENSG00000116641. [Q96N67-2]
ENST00000340370; ENSP00000340742; ENSG00000116641. [Q96N67-5]
ENST00000404627; ENSP00000384446; ENSG00000116641. [Q96N67-7]
ENST00000614472; ENSP00000483062; ENSG00000116641.
GeneIDi85440.
KEGGihsa:85440.
UCSCiuc001dam.3. human. [Q96N67-6]
uc001dan.4. human. [Q96N67-3]
uc001dao.4. human. [Q96N67-4]
uc001dap.4. human. [Q96N67-5]
uc001daq.4. human. [Q96N67-2]
uc009wah.2. human.

Polymorphism databases

DMDMi122065170.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ341187 mRNA. Translation: ABC68221.1 .
AK055401 mRNA. Translation: BAB70917.1 .
AK055493 mRNA. Translation: BAB70933.1 . Different initiation.
AK055905 mRNA. Translation: BAB71042.1 . Frameshift.
AK125049 mRNA. Translation: BAC86032.1 . Different initiation.
AK292640 mRNA. Translation: BAF85329.1 .
AL451044
, AC096946 , AC103923 , AL138847 Genomic DNA. Translation: CAI13104.1 .
AL451044 , AC096946 Genomic DNA. Translation: CAI13105.1 .
AL138847
, AC096946 , AC103923 , AL451044 Genomic DNA. Translation: CAI22995.1 .
CH471059 Genomic DNA. Translation: EAX06582.1 .
DQ309763 mRNA. Translation: ABC33725.1 . Frameshift.
DQ118679 mRNA. Translation: AAZ38451.1 .
DQ118680 mRNA. Translation: AAZ38452.1 .
AB051558 mRNA. Translation: BAB21862.1 .
BC016392 mRNA. Translation: AAH16392.2 . Frameshift.
CCDSi CCDS30734.1. [Q96N67-5 ]
CCDS60156.1. [Q96N67-2 ]
CCDS60157.1. [Q96N67-7 ]
RefSeqi NP_001258928.1. NM_001271999.1. [Q96N67-2 ]
NP_001258929.1. NM_001272000.1. [Q96N67-3 ]
NP_001258930.1. NM_001272001.1. [Q96N67-4 ]
NP_001258931.1. NM_001272002.1. [Q96N67-7 ]
NP_212132.2. NM_033407.3. [Q96N67-5 ]
XP_005271349.1. XM_005271292.1. [Q96N67-6 ]
UniGenei Hs.744927.

3D structure databases

ProteinModelPortali Q96N67.
SMRi Q96N67. Positions 1839-2111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124527. 46 interactions.
IntActi Q96N67. 30 interactions.

PTM databases

PhosphoSitei Q96N67.

Polymorphism databases

DMDMi 122065170.

Proteomic databases

MaxQBi Q96N67.
PaxDbi Q96N67.
PRIDEi Q96N67.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251157 ; ENSP00000251157 ; ENSG00000116641 . [Q96N67-2 ]
ENST00000340370 ; ENSP00000340742 ; ENSG00000116641 . [Q96N67-5 ]
ENST00000404627 ; ENSP00000384446 ; ENSG00000116641 . [Q96N67-7 ]
ENST00000614472 ; ENSP00000483062 ; ENSG00000116641 .
GeneIDi 85440.
KEGGi hsa:85440.
UCSCi uc001dam.3. human. [Q96N67-6 ]
uc001dan.4. human. [Q96N67-3 ]
uc001dao.4. human. [Q96N67-4 ]
uc001dap.4. human. [Q96N67-5 ]
uc001daq.4. human. [Q96N67-2 ]
uc009wah.2. human.

Organism-specific databases

CTDi 85440.
GeneCardsi GC01M062920.
HGNCi HGNC:19190. DOCK7.
HPAi HPA008607.
MIMi 615730. gene.
615859. phenotype.
neXtProti NX_Q96N67.
PharmGKBi PA134872825.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG242127.
GeneTreei ENSGT00760000119234.
HOVERGENi HBG051390.
InParanoidi Q96N67.
OMAi YIHYVFR.
PhylomeDBi Q96N67.
TreeFami TF313629.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi DOCK7. human.
GeneWikii Dock7.
GenomeRNAii 85440.
NextBioi 76016.
PROi Q96N67.
SOURCEi Search...

Gene expression databases

Bgeei Q96N67.
CleanExi HS_DOCK7.
ExpressionAtlasi Q96N67. baseline and differential.
Genevestigatori Q96N67.

Family and domain databases

InterProi IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR021816. DOCK_C/D_N.
[Graphical view ]
PANTHERi PTHR23317. PTHR23317. 1 hit.
Pfami PF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF11878. DUF3398. 1 hit.
[Graphical view ]
PROSITEi PS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18."
    Watabe-Uchida M., John K.A., Janas J.A., Newey S.E., Van Aelst L.
    Neuron 51:727-739(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RAC1 AND RAC3, FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Fetal brain.
  2. "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] (ISOFORM 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 830-2140 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1156-2140 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 585-2140 (ISOFORM 3).
    Tissue: Brain, Mesangial cell, Thalamus and Thymus.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Molecular characterization of human Dock7."
    Yamauchi J., Miyamoto Y., Takashima S., Tanoue A.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-2140 (ISOFORMS 3 AND 4).
    Tissue: Brain.
  6. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 830-2140 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  7. "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] OF 1332-2140 (ISOFORM 2).
    Tissue: Ovary.
  8. "Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity."
    Cote J.-F., Vuori K.
    J. Cell Sci. 115:4901-4913(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  9. Cited for: INTERACTION WITH TSC1, IDENTIFICATION BY MASS SPECTROMETRY.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1429 (ISOFORMS 2 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1398 (ISOFORMS 3 AND 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-180; SER-182; SER-882; SER-888; SER-900; THR-907; SER-910; SER-1383 AND SER-1432, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1421; SER-1425 AND SER-1429 (ISOFORMS 2 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1390; SER-1394 AND SER-1398 (ISOFORMS 3 AND 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-180; SER-896; SER-900; SER-905; THR-907; THR-909; SER-910 AND SER-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1962, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-30; SER-180; SER-182 AND SER-1430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: INVOLVEMENT IN EIEE23.

Entry informationi

Entry nameiDOCK7_HUMAN
AccessioniPrimary (citable) accession number: Q96N67
Secondary accession number(s): Q00M63
, Q2PPY7, Q45RE8, Q45RE9, Q5T1B9, Q5T1C0, Q6ZV32, Q8TB82, Q96NG6, Q96NI0, Q9C092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: January 9, 2007
Last modified: October 29, 2014
This is version 113 of the entry and version 4 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3