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Protein

Dedicator of cytokinesis protein 2

Gene

Dock2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2.1 Publication

GO - Molecular functioni

  • GTPase activator activity Source: MGI
  • Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
  • T cell receptor binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • alpha-beta T cell activation Source: MGI
  • alpha-beta T cell proliferation Source: MGI
  • chemotaxis Source: MGI
  • cytoskeleton organization Source: MGI
  • establishment of T cell polarity Source: MGI
  • immunological synapse formation Source: MGI
  • macropinocytosis Source: UniProtKB
  • membrane raft polarization Source: MGI
  • myeloid dendritic cell activation involved in immune response Source: UniProtKB
  • negative thymic T cell selection Source: MGI
  • positive regulation of GTPase activity Source: MGI
  • positive regulation of phagocytosis Source: UniProtKB
  • positive regulation of Rac protein signal transduction Source: MGI
  • positive thymic T cell selection Source: MGI
  • small GTPase mediated signal transduction Source: InterPro
  • T cell activation Source: MGI
  • T cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Names & Taxonomyi

Protein namesi
Recommended name:
Dedicator of cytokinesis protein 2
Alternative name(s):
Protein Hch
Gene namesi
Name:Dock2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2149010. Dock2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18281828Dedicator of cytokinesis protein 2PRO_0000189987Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041N6-acetyllysineBy similarity
Modified residuei588 – 5881PhosphoserineCombined sources
Modified residuei593 – 5931PhosphoserineBy similarity
Modified residuei738 – 7381N6-acetyllysineBy similarity
Modified residuei797 – 7971N6-acetyllysineBy similarity
Modified residuei1683 – 16831PhosphoserineBy similarity
Modified residuei1704 – 17041PhosphoserineCombined sources
Modified residuei1729 – 17291PhosphoserineCombined sources
Modified residuei1744 – 17441PhosphoserineBy similarity
Modified residuei1747 – 17471PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8C3J5.
MaxQBiQ8C3J5.
PaxDbiQ8C3J5.
PRIDEiQ8C3J5.

PTM databases

iPTMnetiQ8C3J5.
PhosphoSiteiQ8C3J5.

Expressioni

Tissue specificityi

Specifically expressed in hematopoietic cells.1 Publication

Gene expression databases

BgeeiQ8C3J5.
CleanExiMM_DOCK2.
ExpressionAtlasiQ8C3J5. baseline and differential.
GenevisibleiQ8C3J5. MM.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with RAC1 and RAC2. Interacts with CRKL and VAV. Interacts with CD3Z (By similarity).By similarityCurated

GO - Molecular functioni

Protein-protein interaction databases

BioGridi220457. 1 interaction.
IntActiQ8C3J5. 2 interactions.
MINTiMINT-1594776.
STRINGi10090.ENSMUSP00000090884.

Structurei

3D structure databases

ProteinModelPortaliQ8C3J5.
SMRiQ8C3J5. Positions 1-167, 423-609, 1195-1621.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 6962SH3PROSITE-ProRule annotationAdd
BLAST
Domaini423 – 607185DHR-1PROSITE-ProRule annotationAdd
BLAST
Domaini1210 – 1621412DHR-2PROSITE-ProRule annotationAdd
BLAST

Domaini

The DHR-2 domain probably mediates the GEF activity.By similarity

Sequence similaritiesi

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

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG1998. Eukaryota.
ENOG410XQH7. LUCA.
GeneTreeiENSGT00610000085806.
HOGENOMiHOG000006631.
HOVERGENiHBG051389.
InParanoidiQ8C3J5.
KOiK12367.
OMAiMEHSQSD.
OrthoDBiEOG7QNVK8.
TreeFamiTF300423.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR026799. DOCK_2.
IPR010703. DOCK_C.
IPR032376. DOCK_N.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23317. PTHR23317. 1 hit.
PTHR23317:SF73. PTHR23317:SF73. 1 hit.
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. 2 hits.
SSF50044. SSF50044. 1 hit.
PROSITEiPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C3J5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPWRKTDKE RHGVAIYNFQ GSEAQHLTLQ IGDVVRIQET CGDWYRGYLI
60 70 80 90 100
KHKLSQGIFP TSFIHLKEVT VEKRRNIENI IPAEIPLAQE VTTTLWEWGS
110 120 130 140 150
IWKQLYVASK KERFLQVQSM MYDLMEWRSQ LLSGTLPKDE LKELKQKVTS
160 170 180 190 200
KIDYGNKILE LDLIVRDEDG NILDPDKTSV ISLFHAHEEA TYKITERIKE
210 220 230 240 250
EMSKDQPDYG VYSRISSSPT HSLYVFVRNF VCRIGEDAEL FMSLYDPHKQ
260 270 280 290 300
TVISENYLVR WGSKGFPKEI EMLNNLKVVF TDLGNKDLNR DKIFLICQIV
310 320 330 340 350
RIGKMDLKDI NAKKCTQGLR RPFGVAVMDI TDIIKGKAES DEEKQHFIPF
360 370 380 390 400
HPVSAENDFL HSLLGKVIAS KGDSGGQGLW VTMKMLVGDI IQIRKDYPHL
410 420 430 440 450
VDRTTVVARK LGFPEIIMPG DVRNDIYITL LQGDFDKYTK TTQRNVEVIM
460 470 480 490 500
CVCTEDGKVL PNAICVGAGD KAMNEYHSVV YYQVKQPRWM ETVKVAVPIE
510 520 530 540 550
DMQRIHLRFM FRHRSSLESK DKGEKNFAMS YVKLMKEDGT TLHDGYHELV
560 570 580 590 600
VLKGDSKKME DASAYLTLPS YRHPVENKGA TLSRSSSSVG GLSVSSRDVF
610 620 630 640 650
SISTLVCSTK LTQNVGLLGL LKWRMKPQLL QENLEKLKIV DGEEVVKFLQ
660 670 680 690 700
DTLDALFNIM MEHSQSNEYD ILVFDALIYI IGLIADRKFQ HFNTVLEAYI
710 720 730 740 750
QQHFSATLAY KKLMTVLKTY LDTSSRGEQC EPILRTLKAL EYVFKFIVRS
760 770 780 790 800
RTLFSQLYEG KEQMEFEESM RRLFESINNL MKSQYKTTIL LQVAALKYIP
810 820 830 840 850
SVLHDVETVF DAKLLSQLLY EFYTCIPPVK LQKQKVQSMN EIVQSNLFKK
860 870 880 890 900
QECRDILLPV ITKELKELLE QRDDGQHQAE KKHCVELLNS ILEVLSCQDA
910 920 930 940 950
AFTYDHIQEI MVQLLRTVNR TVITMGRDHA LISHFVACMT AILDQMGDQH
960 970 980 990 1000
YSFYIETFQT SSDLVDFLME TFIMFKDLIG KNVYPGDWMA MSMVQNRVFL
1010 1020 1030 1040 1050
RAINKFAETM NQKFLEHTSF EFQLWNNYFH LAVAFITQDS LQLEQFTHAK
1060 1070 1080 1090 1100
YNKILNKYGD MRRLIGFSIR DMWYKLGQNK ICFIPGMVGP ILEMTLIPEA
1110 1120 1130 1140 1150
ELRKATIPIF FDMMLCEYQR TGAFKKFENE IILKLDHEVE GGRGDEQYMQ
1160 1170 1180 1190 1200
LLESILMECT AEHPTIAKSV ENFVSLVKGL LEKLLDYRGV MTDESKDNRM
1210 1220 1230 1240 1250
SCTVNLLNFY KDNNREEMYI RYLYKLRDLH LDCENYTEAA YTLLLHTWLL
1260 1270 1280 1290 1300
KWSDEQCASQ VMQTGQQHPQ THRQLKETLY ETIIGYFDKG KMWEEAISLC
1310 1320 1330 1340 1350
KELAEQYEME IFDYELLSQN LTQQAKFYEN IMKILRTKPD YFAVGYYGQG
1360 1370 1380 1390 1400
FPSFLRNKVF IYRGKEYERR EDFQMQLLSQ FPNAEKMNTT SAPGDDVRNA
1410 1420 1430 1440 1450
PGQYIQCFTV QPVLDEHPRF KNKPVPDQII NFYKSNYVQK FHYSRPVRRG
1460 1470 1480 1490 1500
KVDPENEFAS MWIERTSFLT AYKLPGILRW FEVVHMSQTT ISPLENAIET
1510 1520 1530 1540 1550
MSTVNEKILM MINQYQSDES LPINPLSMLL NGIVDPAVMG GFAKYEKAFF
1560 1570 1580 1590 1600
TEEYSREHPE DQDKLSHLKD LIAWQIPFLG AGIKIHEKRV SDNLRPFHDR
1610 1620 1630 1640 1650
MEECFKNLKM KVEKEYGVRE MPDFEDRRVG RPRSMLRSYR QMSVISLASM
1660 1670 1680 1690 1700
HSDCSTPSKV PAESFDLESA PPKTPKVEEE PISPGSTLPE VKLRRSKKRT
1710 1720 1730 1740 1750
KRSSVVFADE KAATESDLKR LSRKQEFMSD TNLSEHAAIP ARVSILSQMS
1760 1770 1780 1790 1800
FASQSMPTIP ALTLSVAGVP GLDEANTSPR LSQTFFQVSD GDKKTLKKKK
1810 1820
VNQFFKTMLA SKSSEESKQI PDFLSTNM
Length:1,828
Mass (Da):211,704
Last modified:July 27, 2011 - v3
Checksum:i7EB3200A7CD04AA7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti936 – 9361V → E in AAK13045 (PubMed:11518968).Curated
Sequence conflicti1722 – 17221S → F in BAC39514 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027438 mRNA. Translation: AAK13045.1.
AK085708 mRNA. Translation: BAC39514.2.
AL671971
, AL669849, CR392356, CR762384 Genomic DNA. Translation: CAI25210.2.
AL669849
, AL671971, CR392356, CR762384 Genomic DNA. Translation: CAI25278.2.
CR392356
, AL669849, AL671971, CR762384 Genomic DNA. Translation: CAI51908.1.
CR762384
, AL669849, AL671971, CR392356 Genomic DNA. Translation: CAI52041.1.
RefSeqiNP_203538.2. NM_033374.3.
UniGeneiMm.380679.

Genome annotation databases

EnsembliENSMUST00000093193; ENSMUSP00000090884; ENSMUSG00000020143.
GeneIDi94176.
KEGGimmu:94176.
UCSCiuc029rle.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027438 mRNA. Translation: AAK13045.1.
AK085708 mRNA. Translation: BAC39514.2.
AL671971
, AL669849, CR392356, CR762384 Genomic DNA. Translation: CAI25210.2.
AL669849
, AL671971, CR392356, CR762384 Genomic DNA. Translation: CAI25278.2.
CR392356
, AL669849, AL671971, CR762384 Genomic DNA. Translation: CAI51908.1.
CR762384
, AL669849, AL671971, CR392356 Genomic DNA. Translation: CAI52041.1.
RefSeqiNP_203538.2. NM_033374.3.
UniGeneiMm.380679.

3D structure databases

ProteinModelPortaliQ8C3J5.
SMRiQ8C3J5. Positions 1-167, 423-609, 1195-1621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220457. 1 interaction.
IntActiQ8C3J5. 2 interactions.
MINTiMINT-1594776.
STRINGi10090.ENSMUSP00000090884.

PTM databases

iPTMnetiQ8C3J5.
PhosphoSiteiQ8C3J5.

Proteomic databases

EPDiQ8C3J5.
MaxQBiQ8C3J5.
PaxDbiQ8C3J5.
PRIDEiQ8C3J5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000093193; ENSMUSP00000090884; ENSMUSG00000020143.
GeneIDi94176.
KEGGimmu:94176.
UCSCiuc029rle.2. mouse.

Organism-specific databases

CTDi1794.
MGIiMGI:2149010. Dock2.

Phylogenomic databases

eggNOGiKOG1998. Eukaryota.
ENOG410XQH7. LUCA.
GeneTreeiENSGT00610000085806.
HOGENOMiHOG000006631.
HOVERGENiHBG051389.
InParanoidiQ8C3J5.
KOiK12367.
OMAiMEHSQSD.
OrthoDBiEOG7QNVK8.
TreeFamiTF300423.

Miscellaneous databases

PROiQ8C3J5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C3J5.
CleanExiMM_DOCK2.
ExpressionAtlasiQ8C3J5. baseline and differential.
GenevisibleiQ8C3J5. MM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR026799. DOCK_2.
IPR010703. DOCK_C.
IPR032376. DOCK_N.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23317. PTHR23317. 1 hit.
PTHR23317:SF73. PTHR23317:SF73. 1 hit.
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. 2 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. "Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration."
    Fukui Y., Hashimoto O., Sanui T., Oono T., Koga H., Abe M., Inayoshi A., Noda M., Oike M., Shirai T., Sasazuki T.
    Nature 412:826-831(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Thymus.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-1828.
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-1704 AND SER-1729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Lung, Spleen and Testis.

Entry informationi

Entry nameiDOCK2_MOUSE
AccessioniPrimary (citable) accession number: Q8C3J5
Secondary accession number(s): Q5SRI4, Q99M79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.