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Q9BZ29 (DOCK9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dedicator of cytokinesis protein 9
Alternative name(s):
Cdc42 guanine nucleotide exchange factor zizimin-1
Gene names
Name:DOCK9
Synonyms:KIAA1058
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2069 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation. Ref.1 Ref.13

Subunit structure

Homodimer Probable. Interacts preferentially with nucleotide-depleted CDC42. Ref.1 Ref.13

Subcellular location

Endomembrane system Probable. Note: Associated with membranes Probable.

Tissue specificity

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

Domain

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

Miscellaneous

'Zizim' means 'spike' in Hebrew.

Sequence similarities

Belongs to the DOCK family.

Contains 1 DHR-1 domain.

Contains 1 DHR-2 domain.

Contains 1 PH domain.

Sequence caution

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

Ontologies

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BZ29-1)

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.
Isoform 2 (identifier: Q9BZ29-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MSQPPLLPAS...SEVVRGSVLL → MQADKCRTSS...VEAESPGPVP
Isoform 3 (identifier: Q9BZ29-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1355-1378: RTGMMHARLQQLGSLDNSLTFNHS → SVRKISSVLGISVDNG
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9BZ29-4)

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.
Isoform 5 (identifier: Q9BZ29-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20692069Dedicator of cytokinesis protein 9
PRO_0000189999

Regions

Domain174 – 281108PH
Domain640 – 818179DHR-1
Domain1605 – 2069465DHR-2
Region75 – 13561Interaction with activated CDC42 By similarity
Coiled coil1948 – 198235 Potential
Coiled coil2034 – 206734 Potential

Amino acid modifications

Modified residue211Phosphoserine Ref.9
Modified residue12351Phosphoserine Ref.10
Modified residue12411Phosphothreonine Ref.8 Ref.10

Natural variations

Alternative sequence1 – 4343MSQPP…GSVLL → MQADKCRTSSRSVKKELVIE SPLQYKDAAQGEVEAESPGP VP in isoform 2 and isoform 5.
VSP_017128
Alternative sequence1234 – 125421ASPYT…ADSRG → GNAPCSCGLLSTITLKVSWS Q in isoform 5.
VSP_045683
Alternative sequence1255 – 2069815Missing in isoform 5.
VSP_045684
Alternative sequence1355 – 137824RTGMM…TFNHS → SVRKISSVLGISVDNG in isoform 3.
VSP_004024
Alternative sequence1791 – 180414Missing in isoform 4.
VSP_007709
Alternative sequence2068 – 20692LG → ICPLEEKTSVLPNSLHIFNA ISGTPTSTMVHGMTSSSSVV in isoform 4.
VSP_007710
Natural variant4551A → T.
Corresponds to variant rs56010605 [ dbSNP | Ensembl ].
VAR_062000
Natural variant14161K → E.
Corresponds to variant rs16955934 [ dbSNP | Ensembl ].
VAR_053067

Experimental info

Sequence conflict1701S → P in BAG54337. Ref.4
Sequence conflict2961S → P in BAG54337. Ref.4

Secondary structure

...................................................................................... 2069
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 19, 2002. Version 2.
Checksum: 95073CD751745AAE

FASTA2,069236,446
        10         20         30         40         50         60 
MSQPPLLPAS AETRKFTRAL SKPGTAAELR QSVSEVVRGS VLLAKPKLIE PLDYENVIVQ 

        70         80         90        100        110        120 
KKTQILNDCL REMLLFPYDD FQTAILRRQG RYICSTVPAK AEEEAQSLFV TECIKTYNSD 

       130        140        150        160        170        180 
WHLVNYKYED YSGEFRQLPN KVVKLDKLPV HVYEVDEEVD KDEDAASLGS QKGGITKHGW 

       190        200        210        220        230        240 
LYKGNMNSAI SVTMRSFKRR FFHLIQLGDG SYNLNFYKDE KISKEPKGSI FLDSCMGVVQ 

       250        260        270        280        290        300 
NNKVRRFAFE LKMQDKSSYL LAADSEVEME EWITILNKIL QLNFEAAMQE KRNGDSHEDD 

       310        320        330        340        350        360 
EQSKLEGSGS GLDSYLPELA KSAREAEIKL KSESRVKLFY LDPDAQKLDF SSAEPEVKSF 

       370        380        390        400        410        420 
EEKFGKRILV KCNDLSFNLQ CCVAENEEGP TTNVEPFFVT LSLFDIKYNR KISADFHVDL 

       430        440        450        460        470        480 
NHFSVRQMLA TTSPALMNGS GQSPSVLKGI LHEAAMQYPK QGIFSVTCPH PDIFLVARIE 

       490        500        510        520        530        540 
KVLQGSITHC AEPYMKSSDS SKVAQKVLKN AKQACQRLGQ YRMPFAWAAR TLFKDASGNL 

       550        560        570        580        590        600 
DKNARFSAIY RQDSNKLSND DMLKLLADFR KPEKMAKLPV ILGNLDITID NVSSDFPNYV 

       610        620        630        640        650        660 
NSSYIPTKQF ETCSKTPITF EVEEFVPCIP KHTQPYTIYT NHLYVYPKYL KYDSQKSFAK 

       670        680        690        700        710        720 
ARNIAICIEF KDSDEEDSQP LKCIYGRPGG PVFTRSAFAA VLHHHQNPEF YDEIKIELPT 

       730        740        750        760        770        780 
QLHEKHHLLL TFFHVSCDNS SKGSTKKRDV VETQVGYSWL PLLKDGRVVT SEQHIPVSAN 

       790        800        810        820        830        840 
LPSGYLGYQE LGMGRHYGPE IKWVDGGKPL LKISTHLVST VYTQDQHLHN FFQYCQKTES 

       850        860        870        880        890        900 
GAQALGNELV KYLKSLHAME GHVMIAFLPT ILNQLFRVLT RATQEEVAVN VTRVIIHVVA 

       910        920        930        940        950        960 
QCHEEGLESH LRSYVKYAYK AEPYVASEYK TVHEELTKSM TTILKPSADF LTSNKLLKYS 

       970        980        990       1000       1010       1020 
WFFFDVLIKS MAQHLIENSK VKLLRNQRFP ASYHHAVETV VNMLMPHITQ KFRDNPEASK 

      1030       1040       1050       1060       1070       1080 
NANHSLAVFI KRCFTFMDRG FVFKQINNYI SCFAPGDPKT LFEYKFEFLR VVCNHEHYIP 

      1090       1100       1110       1120       1130       1140 
LNLPMPFGKG RIQRYQDLQL DYSLTDEFCR NHFLVGLLLR EVGTALQEFR EVRLIAISVL 

      1150       1160       1170       1180       1190       1200 
KNLLIKHSFD DRYASRSHQA RIATLYLPLF GLLIENVQRI NVRDVSPFPV NAGMTVKDES 

      1210       1220       1230       1240       1250       1260 
LALPAVNPLV TPQKGSTLDN SLHKDLLGAI SGIASPYTTS TPNINSVRNA DSRGSLISTD 

      1270       1280       1290       1300       1310       1320 
SGNSLPERNS EKSNSLDKHQ QSSTLGNSVV RCDKLDQSEI KSLLMCFLYI LKSMSDDALF 

      1330       1340       1350       1360       1370       1380 
TYWNKASTSE LMDFFTISEV CLHQFQYMGK RYIARTGMMH ARLQQLGSLD NSLTFNHSYG 

      1390       1400       1410       1420       1430       1440 
HSDADVLHQS LLEANIATEV CLTALDTLSL FTLAFKNQLL ADHGHNPLMK KVFDVYLCFL 

      1450       1460       1470       1480       1490       1500 
QKHQSETALK NVFTALRSLI YKFPSTFYEG RADMCAALCY EILKCCNSKL SSIRTEASQL 

      1510       1520       1530       1540       1550       1560 
LYFLMRNNFD YTGKKSFVRT HLQVIISVSQ LIADVVGIGG TRFQQSLSII NNCANSDRLI 

      1570       1580       1590       1600       1610       1620 
KHTSFSSDVK DLTKRIRTVL MATAQMKEHE NDPEMLVDLQ YSLAKSYAST PELRKTWLDS 

      1630       1640       1650       1660       1670       1680 
MARIHVKNGD LSEAAMCYVH VTALVAEYLT RKEAVQWEPP LLPHSHSACL RRSRGGVFRQ 

      1690       1700       1710       1720       1730       1740 
GCTAFRVITP NIDEEASMME DVGMQDVHFN EDVLMELLEQ CADGLWKAER YELIADIYKL 

      1750       1760       1770       1780       1790       1800 
IIPIYEKRRD FERLAHLYDT LHRAYSKVTE VMHSGRRLLG TYFRVAFFGQ AAQYQFTDSE 

      1810       1820       1830       1840       1850       1860 
TDVEGFFEDE DGKEYIYKEP KLTPLSEISQ RLLKLYSDKF GSENVKMIQD SGKVNPKDLD 

      1870       1880       1890       1900       1910       1920 
SKYAYIQVTH VIPFFDEKEL QERKTEFERS HNIRRFMFEM PFTQTGKRQG GVEEQCKRRT 

      1930       1940       1950       1960       1970       1980 
ILTAIHCFPY VKKRIPVMYQ HHTDLNPIEV AIDEMSKKVA ELRQLCSSAE VDMIKLQLKL 

      1990       2000       2010       2020       2030       2040 
QGSVSVQVNA GPLAYARAFL DDTNTKRYPD NKVKLLKEVF RQFVEACGQA LAVNERLIKE 

      2050       2060 
DQLEYQEEMK ANYREMAKEL SEIMHEQLG 

« Hide

Isoform 2 [UniParc].

Checksum: C2654DB8162F26F1
Show »

FASTA2,068236,425
Isoform 3 [UniParc].

Checksum: DEB17F98C3573D68
Show »

FASTA2,061235,361
Isoform 4 [UniParc].

Checksum: A540EC1EDDCFFDB5
Show »

FASTA2,093238,846
Isoform 5 [UniParc].

Checksum: 7BA871F8ACA17693
Show »

FASTA1,253142,650

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001123520.1. NM_001130048.1.
NP_001123521.1. NM_001130049.1.
NP_001123522.1. NM_001130050.1.
NP_056111.1. NM_015296.2.
UniGeneHs.596105.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WG7NMR-A165-301[»]
2WM9X-ray2.20A1605-2069[»]
2WMNX-ray2.39A1605-2069[»]
2WMOX-ray2.20A1605-2069[»]
ProteinModelPortalQ9BZ29.
SMRQ9BZ29. Positions 171-307, 1609-2068.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116930. 7 interactions.
IntActQ9BZ29. 13 interactions.
MINTMINT-4657670.

PTM databases

PhosphoSiteQ9BZ29.

Polymorphism databases

DMDM24212635.

Proteomic databases

PaxDbQ9BZ29.
PRIDEQ9BZ29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339416; ENSP00000341086; ENSG00000088387. [Q9BZ29-4]
ENST00000376460; ENSP00000365643; ENSG00000088387. [Q9BZ29-5]
ENST00000442173; ENSP00000406883; ENSG00000088387. [Q9BZ29-6]
GeneID23348.
KEGGhsa:23348.
UCSCuc001vnt.2. human. [Q9BZ29-1]
uc001vnw.2. human. [Q9BZ29-5]

Organism-specific databases

CTD23348.
GeneCardsGC13M099445.
HGNCHGNC:14132. DOCK9.
HPACAB034061.
MIM607325. gene.
neXtProtNX_Q9BZ29.
PharmGKBPA134877754.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242127.
HOVERGENHBG107819.
InParanoidQ9BZ29.
OMAHKDLFGA.
PhylomeDBQ9BZ29.
TreeFamTF313629.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9BZ29.
BgeeQ9BZ29.
GenevestigatorQ9BZ29.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR021816. DOCK_C/D_N.
IPR026796. DOCK_D.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PANTHERPTHR23317. PTHR23317. 1 hit.
PTHR23317:SF26. PTHR23317:SF26. 1 hit.
PfamPF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF11878. DUF3398. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
PROSITEPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDOCK9. human.
EvolutionaryTraceQ9BZ29.
GeneWikiDock9.
GenomeRNAi23348.
NextBio45323.
PROQ9BZ29.
SOURCESearch...

Entry information

Entry nameDOCK9_HUMAN
AccessionPrimary (citable) accession number: Q9BZ29
Secondary accession number(s): B3KX25 expand/collapse secondary AC list , E9PFM9, Q5JUD4, Q5JUD6, Q5T2Q1, Q5TAN8, Q9BZ25, Q9BZ26, Q9BZ27, Q9BZ28, Q9UPU4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

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