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Q9BZ29

- DOCK9_HUMAN

UniProt

Q9BZ29 - DOCK9_HUMAN

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Protein

Dedicator of cytokinesis protein 9

Gene

DOCK9

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

Functioni

Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation.2 Publications

GO - Molecular functioni

  1. Rho guanyl-nucleotide exchange factor activity Source: Ensembl

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Dedicator of cytokinesis protein 9
Alternative name(s):
Cdc42 guanine nucleotide exchange factor zizimin-1
Gene namesi
Name:DOCK9
Synonyms:KIAA1058
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:14132. DOCK9.

Subcellular locationi

Endomembrane system Curated
Note: Associated with membranes.Curated

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134877754.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20692069Dedicator of cytokinesis protein 9PRO_0000189999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine1 Publication
Modified residuei1235 – 12351Phosphoserine1 Publication
Modified residuei1241 – 12411Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BZ29.
PaxDbiQ9BZ29.
PRIDEiQ9BZ29.

PTM databases

PhosphoSiteiQ9BZ29.

Expressioni

Tissue specificityi

Widely expressed, with highest expression in heart and placenta. Expressed at intermediate level in kidney, brain, lung and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ9BZ29.
ExpressionAtlasiQ9BZ29. baseline and differential.
GenevestigatoriQ9BZ29.

Organism-specific databases

HPAiCAB034061.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts preferentially with nucleotide-depleted CDC42.2 PublicationsCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
NEBP209292EBI-2695893,EBI-1049657
SMAD2Q157963EBI-2695893,EBI-1040141
SMAD3P840223EBI-2695893,EBI-347161

Protein-protein interaction databases

BioGridi116930. 7 interactions.
IntActiQ9BZ29. 13 interactions.
MINTiMINT-4657670.

Structurei

Secondary structure

1
2069
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi178 – 1836Combined sources
Helixi190 – 1945Combined sources
Beta strandi198 – 2069Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi212 – 2209Combined sources
Beta strandi227 – 2304Combined sources
Turni232 – 2343Combined sources
Beta strandi248 – 2525Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi258 – 2625Combined sources
Helixi266 – 29126Combined sources
Helixi1610 – 162819Combined sources
Helixi1631 – 165121Combined sources
Beta strandi1677 – 16793Combined sources
Helixi1682 – 16854Combined sources
Turni1686 – 16883Combined sources
Helixi1690 – 16956Combined sources
Beta strandi1708 – 17103Combined sources
Helixi1711 – 172717Combined sources
Helixi1731 – 17333Combined sources
Helixi1734 – 17385Combined sources
Turni1739 – 17413Combined sources
Helixi1742 – 17476Combined sources
Helixi1751 – 177424Combined sources
Beta strandi1781 – 17888Combined sources
Helixi1804 – 18074Combined sources
Helixi1808 – 18103Combined sources
Beta strandi1814 – 18207Combined sources
Helixi1825 – 184016Combined sources
Helixi1842 – 18443Combined sources
Beta strandi1845 – 18484Combined sources
Helixi1856 – 18583Combined sources
Beta strandi1863 – 187311Combined sources
Helixi1877 – 18826Combined sources
Helixi1887 – 18893Combined sources
Beta strandi1890 – 190213Combined sources
Beta strandi1904 – 19096Combined sources
Turni1912 – 19143Combined sources
Beta strandi1916 – 192914Combined sources
Beta strandi1931 – 194515Combined sources
Helixi1947 – 196721Combined sources
Helixi1973 – 198412Combined sources
Beta strandi1987 – 19893Combined sources
Helixi1993 – 19997Combined sources
Helixi2013 – 203725Combined sources
Turni2041 – 20433Combined sources
Helixi2044 – 206421Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WG7NMR-A165-301[»]
2WM9X-ray2.20A1605-2067[»]
2WMNX-ray2.39A1605-2067[»]
2WMOX-ray2.20A1605-2067[»]
ProteinModelPortaliQ9BZ29.
SMRiQ9BZ29. Positions 171-307, 1609-2068.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZ29.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini174 – 281108PHPROSITE-ProRule annotationAdd
BLAST
Domaini640 – 818179DHR-1Add
BLAST
Domaini1605 – 2069465DHR-2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 13561Interaction with activated CDC42By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1948 – 198235Sequence AnalysisAdd
BLAST
Coiled coili2034 – 206734Sequence AnalysisAdd
BLAST

Domaini

The DHR-2 domain is necessary and sufficient for the GEF activity.

Sequence similaritiesi

Belongs to the DOCK family.Curated
Contains 1 DHR-1 domain.Curated
Contains 1 DHR-2 domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG242127.
GeneTreeiENSGT00760000119234.
HOVERGENiHBG107819.
InParanoidiQ9BZ29.
OMAiHKDLFGA.
PhylomeDBiQ9BZ29.
TreeFamiTF313629.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR021816. DOCK_C/D_N.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR23317. PTHR23317. 1 hit.
PfamiPF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF11878. DUF3398. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.
PROSITEiPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BZ29-1) [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
MSQPPLLPAS AETRKFTRAL SKPGTAAELR QSVSEVVRGS VLLAKPKLIE
60 70 80 90 100
PLDYENVIVQ KKTQILNDCL REMLLFPYDD FQTAILRRQG RYICSTVPAK
110 120 130 140 150
AEEEAQSLFV TECIKTYNSD WHLVNYKYED YSGEFRQLPN KVVKLDKLPV
160 170 180 190 200
HVYEVDEEVD KDEDAASLGS QKGGITKHGW LYKGNMNSAI SVTMRSFKRR
210 220 230 240 250
FFHLIQLGDG SYNLNFYKDE KISKEPKGSI FLDSCMGVVQ NNKVRRFAFE
260 270 280 290 300
LKMQDKSSYL LAADSEVEME EWITILNKIL QLNFEAAMQE KRNGDSHEDD
310 320 330 340 350
EQSKLEGSGS GLDSYLPELA KSAREAEIKL KSESRVKLFY LDPDAQKLDF
360 370 380 390 400
SSAEPEVKSF EEKFGKRILV KCNDLSFNLQ CCVAENEEGP TTNVEPFFVT
410 420 430 440 450
LSLFDIKYNR KISADFHVDL NHFSVRQMLA TTSPALMNGS GQSPSVLKGI
460 470 480 490 500
LHEAAMQYPK QGIFSVTCPH PDIFLVARIE KVLQGSITHC AEPYMKSSDS
510 520 530 540 550
SKVAQKVLKN AKQACQRLGQ YRMPFAWAAR TLFKDASGNL DKNARFSAIY
560 570 580 590 600
RQDSNKLSND DMLKLLADFR KPEKMAKLPV ILGNLDITID NVSSDFPNYV
610 620 630 640 650
NSSYIPTKQF ETCSKTPITF EVEEFVPCIP KHTQPYTIYT NHLYVYPKYL
660 670 680 690 700
KYDSQKSFAK ARNIAICIEF KDSDEEDSQP LKCIYGRPGG PVFTRSAFAA
710 720 730 740 750
VLHHHQNPEF YDEIKIELPT QLHEKHHLLL TFFHVSCDNS SKGSTKKRDV
760 770 780 790 800
VETQVGYSWL PLLKDGRVVT SEQHIPVSAN LPSGYLGYQE LGMGRHYGPE
810 820 830 840 850
IKWVDGGKPL LKISTHLVST VYTQDQHLHN FFQYCQKTES GAQALGNELV
860 870 880 890 900
KYLKSLHAME GHVMIAFLPT ILNQLFRVLT RATQEEVAVN VTRVIIHVVA
910 920 930 940 950
QCHEEGLESH LRSYVKYAYK AEPYVASEYK TVHEELTKSM TTILKPSADF
960 970 980 990 1000
LTSNKLLKYS WFFFDVLIKS MAQHLIENSK VKLLRNQRFP ASYHHAVETV
1010 1020 1030 1040 1050
VNMLMPHITQ KFRDNPEASK NANHSLAVFI KRCFTFMDRG FVFKQINNYI
1060 1070 1080 1090 1100
SCFAPGDPKT LFEYKFEFLR VVCNHEHYIP LNLPMPFGKG RIQRYQDLQL
1110 1120 1130 1140 1150
DYSLTDEFCR NHFLVGLLLR EVGTALQEFR EVRLIAISVL KNLLIKHSFD
1160 1170 1180 1190 1200
DRYASRSHQA RIATLYLPLF GLLIENVQRI NVRDVSPFPV NAGMTVKDES
1210 1220 1230 1240 1250
LALPAVNPLV TPQKGSTLDN SLHKDLLGAI SGIASPYTTS TPNINSVRNA
1260 1270 1280 1290 1300
DSRGSLISTD SGNSLPERNS EKSNSLDKHQ QSSTLGNSVV RCDKLDQSEI
1310 1320 1330 1340 1350
KSLLMCFLYI LKSMSDDALF TYWNKASTSE LMDFFTISEV CLHQFQYMGK
1360 1370 1380 1390 1400
RYIARTGMMH ARLQQLGSLD NSLTFNHSYG HSDADVLHQS LLEANIATEV
1410 1420 1430 1440 1450
CLTALDTLSL FTLAFKNQLL ADHGHNPLMK KVFDVYLCFL QKHQSETALK
1460 1470 1480 1490 1500
NVFTALRSLI YKFPSTFYEG RADMCAALCY EILKCCNSKL SSIRTEASQL
1510 1520 1530 1540 1550
LYFLMRNNFD YTGKKSFVRT HLQVIISVSQ LIADVVGIGG TRFQQSLSII
1560 1570 1580 1590 1600
NNCANSDRLI KHTSFSSDVK DLTKRIRTVL MATAQMKEHE NDPEMLVDLQ
1610 1620 1630 1640 1650
YSLAKSYAST PELRKTWLDS MARIHVKNGD LSEAAMCYVH VTALVAEYLT
1660 1670 1680 1690 1700
RKEAVQWEPP LLPHSHSACL RRSRGGVFRQ GCTAFRVITP NIDEEASMME
1710 1720 1730 1740 1750
DVGMQDVHFN EDVLMELLEQ CADGLWKAER YELIADIYKL IIPIYEKRRD
1760 1770 1780 1790 1800
FERLAHLYDT LHRAYSKVTE VMHSGRRLLG TYFRVAFFGQ AAQYQFTDSE
1810 1820 1830 1840 1850
TDVEGFFEDE DGKEYIYKEP KLTPLSEISQ RLLKLYSDKF GSENVKMIQD
1860 1870 1880 1890 1900
SGKVNPKDLD SKYAYIQVTH VIPFFDEKEL QERKTEFERS HNIRRFMFEM
1910 1920 1930 1940 1950
PFTQTGKRQG GVEEQCKRRT ILTAIHCFPY VKKRIPVMYQ HHTDLNPIEV
1960 1970 1980 1990 2000
AIDEMSKKVA ELRQLCSSAE VDMIKLQLKL QGSVSVQVNA GPLAYARAFL
2010 2020 2030 2040 2050
DDTNTKRYPD NKVKLLKEVF RQFVEACGQA LAVNERLIKE DQLEYQEEMK
2060
ANYREMAKEL SEIMHEQLG
Length:2,069
Mass (Da):236,446
Last modified:October 19, 2002 - v2
Checksum:i95073CD751745AAE
GO
Isoform 2 (identifier: Q9BZ29-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MSQPPLLPAS...SEVVRGSVLL → MQADKCRTSS...VEAESPGPVP

Show »
Length:2,068
Mass (Da):236,425
Checksum:iC2654DB8162F26F1
GO
Isoform 3 (identifier: Q9BZ29-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1355-1378: RTGMMHARLQQLGSLDNSLTFNHS → SVRKISSVLGISVDNG

Note: No experimental confirmation available.

Show »
Length:2,061
Mass (Da):235,361
Checksum:iDEB17F98C3573D68
GO
Isoform 4 (identifier: Q9BZ29-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1791-1804: Missing.
     2068-2069: LG → ICPLEEKTSVLPNSLHIFNAISGTPTSTMVHGMTSSSSVV

Note: Produced by exon skipping that results in a frameshift. No experimental confirmation available.

Show »
Length:2,093
Mass (Da):238,846
Checksum:iA540EC1EDDCFFDB5
GO
Isoform 5 (identifier: Q9BZ29-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MSQPPLLPAS...SEVVRGSVLL → MQADKCRTSS...VEAESPGPVP
     1234-1254: ASPYTTSTPNINSVRNADSRG → GNAPCSCGLLSTITLKVSWSQ
     1255-2069: Missing.

Note: No experimental confirmation available.

Show »
Length:1,253
Mass (Da):142,650
Checksum:i7BA871F8ACA17693
GO

Sequence cautioni

The sequence BAA83010.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701S → P in BAG54337. (PubMed:14702039)Curated
Sequence conflicti296 – 2961S → P in BAG54337. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti455 – 4551A → T.
Corresponds to variant rs56010605 [ dbSNP | Ensembl ].
VAR_062000
Natural varianti1416 – 14161K → E.
Corresponds to variant rs16955934 [ dbSNP | Ensembl ].
VAR_053067

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343MSQPP…GSVLL → MQADKCRTSSRSVKKELVIE SPLQYKDAAQGEVEAESPGP VP in isoform 2 and isoform 5. 2 PublicationsVSP_017128Add
BLAST
Alternative sequencei1234 – 125421ASPYT…ADSRG → GNAPCSCGLLSTITLKVSWS Q in isoform 5. 1 PublicationVSP_045683Add
BLAST
Alternative sequencei1255 – 2069815Missing in isoform 5. 1 PublicationVSP_045684Add
BLAST
Alternative sequencei1355 – 137824RTGMM…TFNHS → SVRKISSVLGISVDNG in isoform 3. CuratedVSP_004024Add
BLAST
Alternative sequencei1791 – 180414Missing in isoform 4. 1 PublicationVSP_007709Add
BLAST
Alternative sequencei2068 – 20692LG → ICPLEEKTSVLPNSLHIFNA ISGTPTSTMVHGMTSSSSVV in isoform 4. 1 PublicationVSP_007710

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF527605 mRNA. Translation: AAM90306.1.
AB028981 mRNA. Translation: BAA83010.2. Different initiation.
AK126492 mRNA. Translation: BAG54337.1.
AL139084, AL161420 Genomic DNA. Translation: CAI13370.1.
AL139084, AL161420, AL391122 Genomic DNA. Translation: CAI13372.1.
AL161420, AL139084 Genomic DNA. Translation: CAI39569.1.
AL161420 Genomic DNA. Translation: CAI39570.1.
AL161420, AL139084, AL391122 Genomic DNA. Translation: CAI39574.1.
AL161420 Genomic DNA. Translation: CAI39577.1.
AL391122, AL139084, AL161420 Genomic DNA. Translation: CAI11061.1.
BC043506 mRNA. Translation: AAH43506.1.
CCDSiCCDS45062.1. [Q9BZ29-5]
RefSeqiNP_001123520.1. NM_001130048.1. [Q9BZ29-5]
NP_001123521.1. NM_001130049.1.
NP_001123522.1. NM_001130050.1. [Q9BZ29-6]
NP_056111.1. NM_015296.2. [Q9BZ29-1]
UniGeneiHs.596105.

Genome annotation databases

EnsembliENST00000376460; ENSP00000365643; ENSG00000088387. [Q9BZ29-5]
GeneIDi23348.
KEGGihsa:23348.
UCSCiuc001vnt.2. human. [Q9BZ29-1]
uc001vnw.2. human. [Q9BZ29-5]

Polymorphism databases

DMDMi24212635.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF527605 mRNA. Translation: AAM90306.1 .
AB028981 mRNA. Translation: BAA83010.2 . Different initiation.
AK126492 mRNA. Translation: BAG54337.1 .
AL139084 , AL161420 Genomic DNA. Translation: CAI13370.1 .
AL139084 , AL161420 , AL391122 Genomic DNA. Translation: CAI13372.1 .
AL161420 , AL139084 Genomic DNA. Translation: CAI39569.1 .
AL161420 Genomic DNA. Translation: CAI39570.1 .
AL161420 , AL139084 , AL391122 Genomic DNA. Translation: CAI39574.1 .
AL161420 Genomic DNA. Translation: CAI39577.1 .
AL391122 , AL139084 , AL161420 Genomic DNA. Translation: CAI11061.1 .
BC043506 mRNA. Translation: AAH43506.1 .
CCDSi CCDS45062.1. [Q9BZ29-5 ]
RefSeqi NP_001123520.1. NM_001130048.1. [Q9BZ29-5 ]
NP_001123521.1. NM_001130049.1.
NP_001123522.1. NM_001130050.1. [Q9BZ29-6 ]
NP_056111.1. NM_015296.2. [Q9BZ29-1 ]
UniGenei Hs.596105.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WG7 NMR - A 165-301 [» ]
2WM9 X-ray 2.20 A 1605-2067 [» ]
2WMN X-ray 2.39 A 1605-2067 [» ]
2WMO X-ray 2.20 A 1605-2067 [» ]
ProteinModelPortali Q9BZ29.
SMRi Q9BZ29. Positions 171-307, 1609-2068.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116930. 7 interactions.
IntActi Q9BZ29. 13 interactions.
MINTi MINT-4657670.

PTM databases

PhosphoSitei Q9BZ29.

Polymorphism databases

DMDMi 24212635.

Proteomic databases

MaxQBi Q9BZ29.
PaxDbi Q9BZ29.
PRIDEi Q9BZ29.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376460 ; ENSP00000365643 ; ENSG00000088387 . [Q9BZ29-5 ]
GeneIDi 23348.
KEGGi hsa:23348.
UCSCi uc001vnt.2. human. [Q9BZ29-1 ]
uc001vnw.2. human. [Q9BZ29-5 ]

Organism-specific databases

CTDi 23348.
GeneCardsi GC13M099445.
HGNCi HGNC:14132. DOCK9.
HPAi CAB034061.
MIMi 607325. gene.
neXtProti NX_Q9BZ29.
PharmGKBi PA134877754.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG242127.
GeneTreei ENSGT00760000119234.
HOVERGENi HBG107819.
InParanoidi Q9BZ29.
OMAi HKDLFGA.
PhylomeDBi Q9BZ29.
TreeFami TF313629.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi DOCK9. human.
EvolutionaryTracei Q9BZ29.
GeneWikii Dock9.
GenomeRNAii 23348.
NextBioi 45323.
PROi Q9BZ29.
SOURCEi Search...

Gene expression databases

Bgeei Q9BZ29.
ExpressionAtlasi Q9BZ29. baseline and differential.
Genevestigatori Q9BZ29.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR021816. DOCK_C/D_N.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
PANTHERi PTHR23317. PTHR23317. 1 hit.
Pfami PF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF11878. DUF3398. 1 hit.
PF00169. PH. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 5 hits.
PROSITEi PS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins."
    Meller N., Irani-Tehrani M., Kiosses W.B., Del Pozo M.A., Schwartz M.A.
    Nat. Cell Biol. 4:639-647(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, INTERACTION WITH CDC42, GEF ACTIVITY, TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "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 5).
    Tissue: Uterus.
  5. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4).
  6. "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 1551-2069 (ISOFORM 4).
    Tissue: Eye.
  7. "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, GEF ACTIVITY.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-1235 AND THR-1241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Solution structure of pleckstrin homology domain from human KIAA1058 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 165-301.
  13. "Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor."
    Yang J., Zhang Z., Roe S.M., Marshall C.J., Barford D.
    Science 325:1398-1402(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1605-2069 IN COMPLEX WITH CDC42, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiDOCK9_HUMAN
AccessioniPrimary (citable) accession number: Q9BZ29
Secondary accession number(s): B3KX25
, E9PFM9, Q5JUD4, Q5JUD6, Q5T2Q1, Q5TAN8, Q9BZ25, Q9BZ26, Q9BZ27, Q9BZ28, Q9UPU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: November 26, 2014
This is version 126 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

Miscellaneous

'Zizim' means 'spike' in Hebrew.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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

External Data

Dasty 3