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Protein

Dedicator of cytokinesis protein 5

Gene

DOCK5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP.

GO - Molecular functioni

GO - Biological processi

  • negative regulation of vascular smooth muscle contraction Source: BHF-UCL
  • positive regulation of smooth muscle cell migration Source: BHF-UCL
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Dedicator of cytokinesis protein 5
Gene namesi
Name:DOCK5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:23476. DOCK5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134932307.

Polymorphism and mutation databases

BioMutaiDOCK5.
DMDMi119370380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18701870Dedicator of cytokinesis protein 5PRO_0000189992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei365 – 3651PhosphoserineCombined sources
Modified residuei758 – 7581N6-acetyllysineBy similarity
Modified residuei818 – 8181N6-acetyllysineCombined sources
Modified residuei1766 – 17661PhosphoserineCombined sources
Modified residuei1789 – 17891PhosphoserineCombined sources
Modified residuei1794 – 17941PhosphothreonineCombined sources
Modified residuei1814 – 18141PhosphothreonineCombined sources
Modified residuei1834 – 18341PhosphoserineCombined sources
Modified residuei1869 – 18691PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H7D0.
MaxQBiQ9H7D0.
PaxDbiQ9H7D0.
PRIDEiQ9H7D0.

PTM databases

iPTMnetiQ9H7D0.
PhosphoSiteiQ9H7D0.

Expressioni

Gene expression databases

BgeeiQ9H7D0.
CleanExiHS_DOCK5.
ExpressionAtlasiQ9H7D0. baseline and differential.
GenevisibleiQ9H7D0. HS.

Organism-specific databases

HPAiHPA017719.
HPA056837.

Interactioni

Protein-protein interaction databases

BioGridi123062. 55 interactions.
IntActiQ9H7D0. 23 interactions.
MINTiMINT-7944979.
STRINGi9606.ENSP00000276440.

Structurei

3D structure databases

ProteinModelPortaliQ9H7D0.
SMRiQ9H7D0. Positions 1-72, 443-629, 1216-1639.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 6962SH3PROSITE-ProRule annotationAdd
BLAST
Domaini443 – 627185DHR-1Add
BLAST
Domaini1231 – 1642412DHR-2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1782 – 185574Pro-richAdd
BLAST

Domaini

The DHR-2 domain may mediate some GEF activity.By similarity

Sequence similaritiesi

Belongs to the DOCK family.Curated
Contains 1 DHR-1 domain.Curated
Contains 1 DHR-2 domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG1998. Eukaryota.
ENOG410XQH7. LUCA.
GeneTreeiENSGT00610000085806.
HOGENOMiHOG000006631.
HOVERGENiHBG051389.
InParanoidiQ9H7D0.
KOiK17707.
OMAiHRSSQET.
OrthoDBiEOG7QNVK8.
PhylomeDBiQ9H7D0.
TreeFamiTF300423.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR032376. DOCK_N.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23317. PTHR23317. 2 hits.
PfamiPF06920. DHR-2. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF16172. DOCK_N. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H7D0-1) [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
MARWIPTKRQ KYGVAIYNYN ASQDVELSLQ IGDTVHILEM YEGWYRGYTL
60 70 80 90 100
QNKSKKGIFP ETYIHLKEAT VEDLGQHETV IPGELPLVQE LTSTLREWAV
110 120 130 140 150
IWRKLYVNNK LTLFRQLQQM TYSLIEWRSQ ILSGTLPKDE LAELKKKVTA
160 170 180 190 200
KIDHGNRMLG LDLVVRDDNG NILDPDETST IALFKAHEVA SKRIEEKIQE
210 220 230 240 250
EKSILQNLDL RGQSIFSTIH TYGLYVNFKN FVCNIGEDAE LFMALYDPDQ
260 270 280 290 300
STFISENYLI RWGSNGMPKE IEKLNNLQAV FTDLSSMDLI RPRVSLVCQI
310 320 330 340 350
VRVGHMELKE GKKHTCGLRR PFGVAVMDIT DIIHGKVDDE EKQHFIPFQQ
360 370 380 390 400
IAMETYIRQR QLIMSPLITS HVIGENEPLT SVLNKVIAAK EVNHKGQGLW
410 420 430 440 450
VSLKLLPGDL TQVQKNFSHL VDRSTAIARK MGFPEIILPG DVRNDIYVTL
460 470 480 490 500
IHGEFDKGKK KTPKNVEVTM SVHDEEGKLL EKAIHPGAGY EGISEYKSVV
510 520 530 540 550
YYQVKQPCWY ETVKVSIAIE EVTRCHIRFT FRHRSSQETR DKSERAFGVA
560 570 580 590 600
FVKLMNPDGT TLQDGRHDLV VYKGDNKKME DAKFYLTLPG TKMEMEEKEL
610 620 630 640 650
QASKNLVTFT PSKDSTKDSF QIATLICSTK LTQNVDLLGL LNWRSNSQNI
660 670 680 690 700
KHNLKKLMEV DGGEIVKFLQ DTLDALFNIM MEMSDSETYD FLVFDALVFI
710 720 730 740 750
ISLIGDIKFQ HFNPVLETYI YKHFSATLAY VKLSKVLNFY VANADDSSKT
760 770 780 790 800
ELLFAALKAL KYLFRFIIQS RVLYLRFYGQ SKDGDEFNNS IRQLFLAFNM
810 820 830 840 850
LMDRPLEEAV KIKGAALKYL PSIINDVKLV FDPVELSVLF CKFIQSIPDN
860 870 880 890 900
QLVRQKLNCM TKIVESTLFR QSECREVLLP LLTDQLSGQL DDNSNKPDHE
910 920 930 940 950
ASSQLLSNIL EVLDRKDVGA TAVHIQLIME RLLRRINRTV IGMNRQSPHI
960 970 980 990 1000
GSFVACMIAL LQQMDDSHYS HYISTFKTRQ DIIDFLMETF IMFKDLIGKN
1010 1020 1030 1040 1050
VYAKDWMVMN MTQNRVFLRA INQFAEVLTR FFMDQASFEL QLWNNYFHLA
1060 1070 1080 1090 1100
VAFLTHESLQ LETFSQAKRN KIVKKYGDMR KEIGFRIRDM WYNLGPHKIK
1110 1120 1130 1140 1150
FIPSMVGPIL EVTLTPEVEL RKATIPIFFD MMQCEFNFSG NGNFHMFENE
1160 1170 1180 1190 1200
LITKLDQEVE GGRGDEQYKV LLEKLLLEHC RKHKYLSSSG EVFALLVSSL
1210 1220 1230 1240 1250
LENLLDYRTI IMQDESKENR MSCTVNVLNF YKEKKREDIY IRYLYKLRDL
1260 1270 1280 1290 1300
HRDCENYTEA AYTLLLHAEL LQWSDKPCVP HLLQKDSYYV YTQQELKEKL
1310 1320 1330 1340 1350
YQEIISYFDK GKMWEKAIKL SKELAETYES KVFDYEGLGN LLKKRASFYE
1360 1370 1380 1390 1400
NIIKAMRPQP EYFAVGYYGQ GFPSFLRNKI FIYRGKEYER REDFSLRLLT
1410 1420 1430 1440 1450
QFPNAEKMTS TTPPGEDIKS SPKQYMQCFT VKPVMSLPPS YKDKPVPEQI
1460 1470 1480 1490 1500
LNYYRANEVQ QFRYSRPFRK GEKDPDNEFA TMWIERTTYT TAYTFPGILK
1510 1520 1530 1540 1550
WFEVKQISTE EISPLENAIE TMELTNERIS NCVQQHAWDR SLSVHPLSML
1560 1570 1580 1590 1600
LSGIVDPAVM GGFSNYEKAF FTEKYLQEHP EDQEKVELLK RLIALQMPLL
1610 1620 1630 1640 1650
TEGIRIHGEK LTEQLKPLHE RLSSCFRELK EKVEKHYGVI TLPPNLTERK
1660 1670 1680 1690 1700
QSRTGSIVLP YIMSSTLRRL SITSVTSSVV STSSNSSDNA PSRPGSDGSI
1710 1720 1730 1740 1750
LEPLLERRAS SGARVEDLSL REENSENRIS KFKRKDWSLS KSQVIAEKAP
1760 1770 1780 1790 1800
EPDLMSPTRK AQRPKSLQLM DNRLSPFHGS SPPQSTPLSP PPLTPKATRT
1810 1820 1830 1840 1850
LSSPSLQTDG IAATPVPPPP PPKSKPYEGS QRNSTELAPP LPVRREAKAP
1860 1870
PPPPPKARKS GIPTSEPGSQ
Length:1,870
Mass (Da):215,309
Last modified:December 12, 2006 - v3
Checksum:i947A3DC1190EF7A9
GO
Isoform 2 (identifier: Q9H7D0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     351-1870: Missing.

Show »
Length:350
Mass (Da):40,421
Checksum:iCFC696403289D76F
GO

Sequence cautioni

The sequence BAB14962.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC86503.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti987 – 9871M → L in BAC86503 (PubMed:14702039).Curated
Sequence conflicti1161 – 11611G → E in BAC86503 (PubMed:14702039).Curated
Sequence conflicti1548 – 15481S → Y in CAH10503 (PubMed:17974005).Curated
Sequence conflicti1833 – 18331N → S in BAC86503 (PubMed:14702039).Curated
Sequence conflicti1842 – 18421P → S in CAH10503 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti250 – 2501Q → R.
Corresponds to variant rs17053341 [ dbSNP | Ensembl ].
VAR_033886
Natural varianti1023 – 10231Q → R.
Corresponds to variant rs2271111 [ dbSNP | Ensembl ].
VAR_053065
Natural varianti1285 – 12851K → R.2 Publications
Corresponds to variant rs2659585 [ dbSNP | Ensembl ].
VAR_053066
Natural varianti1836 – 18361E → K.
Corresponds to variant rs35688737 [ dbSNP | Ensembl ].
VAR_033887

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei351 – 18701520Missing in isoform 2. 1 PublicationVSP_021868Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC041005 Genomic DNA. No translation available.
AC091185 Genomic DNA. No translation available.
BC011877 mRNA. Translation: AAH11877.1.
BC041761 mRNA. Translation: AAH41761.2.
BC137175 mRNA. Translation: AAI37176.1.
BC137176 mRNA. Translation: AAI37177.1.
AK024687 mRNA. Translation: BAB14962.1. Different initiation.
AK126249 mRNA. Translation: BAC86503.1. Different initiation.
CR627414 mRNA. Translation: CAH10503.1.
CCDSiCCDS6047.1. [Q9H7D0-1]
RefSeqiNP_079216.4. NM_024940.6. [Q9H7D0-1]
UniGeneiHs.195403.

Genome annotation databases

EnsembliENST00000276440; ENSP00000276440; ENSG00000147459. [Q9H7D0-1]
ENST00000481100; ENSP00000429737; ENSG00000147459. [Q9H7D0-2]
GeneIDi80005.
KEGGihsa:80005.
UCSCiuc003xef.4. human. [Q9H7D0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC041005 Genomic DNA. No translation available.
AC091185 Genomic DNA. No translation available.
BC011877 mRNA. Translation: AAH11877.1.
BC041761 mRNA. Translation: AAH41761.2.
BC137175 mRNA. Translation: AAI37176.1.
BC137176 mRNA. Translation: AAI37177.1.
AK024687 mRNA. Translation: BAB14962.1. Different initiation.
AK126249 mRNA. Translation: BAC86503.1. Different initiation.
CR627414 mRNA. Translation: CAH10503.1.
CCDSiCCDS6047.1. [Q9H7D0-1]
RefSeqiNP_079216.4. NM_024940.6. [Q9H7D0-1]
UniGeneiHs.195403.

3D structure databases

ProteinModelPortaliQ9H7D0.
SMRiQ9H7D0. Positions 1-72, 443-629, 1216-1639.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123062. 55 interactions.
IntActiQ9H7D0. 23 interactions.
MINTiMINT-7944979.
STRINGi9606.ENSP00000276440.

PTM databases

iPTMnetiQ9H7D0.
PhosphoSiteiQ9H7D0.

Polymorphism and mutation databases

BioMutaiDOCK5.
DMDMi119370380.

Proteomic databases

EPDiQ9H7D0.
MaxQBiQ9H7D0.
PaxDbiQ9H7D0.
PRIDEiQ9H7D0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276440; ENSP00000276440; ENSG00000147459. [Q9H7D0-1]
ENST00000481100; ENSP00000429737; ENSG00000147459. [Q9H7D0-2]
GeneIDi80005.
KEGGihsa:80005.
UCSCiuc003xef.4. human. [Q9H7D0-1]

Organism-specific databases

CTDi80005.
GeneCardsiDOCK5.
H-InvDBHIX0007394.
HGNCiHGNC:23476. DOCK5.
HPAiHPA017719.
HPA056837.
neXtProtiNX_Q9H7D0.
PharmGKBiPA134932307.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1998. Eukaryota.
ENOG410XQH7. LUCA.
GeneTreeiENSGT00610000085806.
HOGENOMiHOG000006631.
HOVERGENiHBG051389.
InParanoidiQ9H7D0.
KOiK17707.
OMAiHRSSQET.
OrthoDBiEOG7QNVK8.
PhylomeDBiQ9H7D0.
TreeFamiTF300423.

Enzyme and pathway databases

ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiDOCK5. human.
GeneWikiiDock5.
GenomeRNAii80005.
NextBioi70083.
PROiQ9H7D0.

Gene expression databases

BgeeiQ9H7D0.
CleanExiHS_DOCK5.
ExpressionAtlasiQ9H7D0. baseline and differential.
GenevisibleiQ9H7D0. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR032376. DOCK_N.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23317. PTHR23317. 2 hits.
PfamiPF06920. DHR-2. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF16172. DOCK_N. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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 2), VARIANT ARG-1285.
    Tissue: Brain, Skin and Uterus.
  3. "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 900-1870 (ISOFORM 1), VARIANT ARG-1285.
    Tissue: Endothelial cell and Liver.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1528-1870 (ISOFORM 1).
    Tissue: Skeletal muscle.
  5. "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.
  6. "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-1814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1789; THR-1794; SER-1834 AND SER-1869, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-1834, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-818, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-1766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDOCK5_HUMAN
AccessioniPrimary (citable) accession number: Q9H7D0
Secondary accession number(s): B2RNY0
, Q5XKD5, Q6AI11, Q6PJS6, Q6ZTS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: December 12, 2006
Last modified: May 11, 2016
This is version 122 of the entry and version 3 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 8
    Human chromosome 8: 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. 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.