Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96N67 (DOCK7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dedicator of cytokinesis protein 7
Gene names
Name:DOCK7
Synonyms:KIAA1771
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2140 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

Interacts with TSC1. Interacts with nucleotide-free RAC1 and RAC3. Ref.1 Ref.8

Subcellular location

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

Tissue specificity

Widely expressed. Ref.5

Domain

The DHR-2 domain mediates GEF activity.

Sequence similarities

Belongs to the DOCK family.

Contains 1 DHR-1 domain.

Contains 1 DHR-2 domain.

Sequence caution

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 BAB70933.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB71042.1 differs from that shown. Reason: Frameshift at position 1792.

The sequence BAC86032.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell projection
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   Molecular functionDevelopmental protein
Guanine-nucleotide releasing factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of Rac GTPase activity

Inferred from direct assay Ref.1. Source: BHF-UCL

axonogenesis

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

establishment of neuroblast polarity

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

microtubule cytoskeleton organization

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

neuron projection development

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

pigmentation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentaxon

Traceable author statement Ref.1. Source: BHF-UCL

basal part of cell

Traceable author statement Ref.1. Source: BHF-UCL

growth cone

Traceable author statement Ref.1. Source: BHF-UCL

neuron projection

Traceable author statement Ref.1. Source: BHF-UCL

   Molecular_functionRac GTPase binding

Inferred from direct assay Ref.1. Source: BHF-UCL

guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96N67-1)

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: Q96N67-2)

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.
Isoform 3 (identifier: Q96N67-3)

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.
Isoform 4 (identifier: Q96N67-4)

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.
Isoform 5 (identifier: Q96N67-5)

The sequence of this isoform differs from the canonical sequence as follows:
     923-953: Missing.
Isoform 6 (identifier: Q96N67-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21402140Dedicator of cytokinesis protein 7
PRO_0000189995

Regions

Domain561 – 727167DHR-1
Domain1678 – 2114437DHR-2
Coiled coil365 – 39531 Potential
Coiled coil2086 – 211227 Potential

Amino acid modifications

Modified residue281Phosphoserine Ref.15
Modified residue301Phosphoserine Ref.10 Ref.15
Modified residue1801Phosphoserine Ref.10 Ref.13 Ref.15
Modified residue1821Phosphoserine Ref.10 Ref.15
Modified residue8821Phosphoserine Ref.10
Modified residue8881Phosphoserine Ref.10
Modified residue8961Phosphoserine Ref.13
Modified residue9001Phosphoserine Ref.10 Ref.13
Modified residue9051Phosphoserine Ref.13
Modified residue9071Phosphothreonine Ref.10 Ref.13
Modified residue9091Phosphothreonine Ref.13
Modified residue9101Phosphoserine Ref.10 Ref.13
Modified residue13831Phosphoserine Ref.10 Ref.17
Modified residue14301Phosphoserine Ref.15
Modified residue14321Phosphoserine Ref.10
Modified residue14381Phosphoserine Ref.13
Modified residue19621N6-acetyllysine Ref.14

Natural variations

Alternative sequence923 – 95331Missing in isoform 3, isoform 4 and isoform 5.
VSP_012440
Alternative sequence1419 – 14279Missing in isoform 2, isoform 3, isoform 4 and isoform 6.
VSP_022240
Alternative sequence1832 – 18365STGWE → DGK in isoform 2 and isoform 4.
VSP_007707
Natural variant8241I → T.
Corresponds to variant rs35400360 [ dbSNP | Ensembl ].
VAR_057524

Experimental info

Sequence conflict7501H → R in BAC86032. Ref.4
Sequence conflict14401E → G in BAC86032. Ref.4
Sequence conflict15201S → N in BAB70933. Ref.4
Sequence conflict15211A → V in BAC86032. Ref.4
Sequence conflict16391P → L in BAC86032. Ref.4
Sequence conflict18591E → K in BAB70933. Ref.4
Sequence conflict19081K → T in BAB71042. Ref.4

Sequences

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

Last modified January 9, 2007. Version 4.
Checksum: A14857DCB9C3AE6E

FASTA2,140242,561
        10         20         30         40         50         60 
MAERRAFAQK ISRTVAAEVR KQISGQYSGS PQLLKNLNIV GNISHHTTVP LTEAVDPVDL 

        70         80         90        100        110        120 
EDYLITHPLA VDSGPLRDLI EFPPDDIEVV YSPRDCRTLV SAVPEESEMD PHVRDCIRSY 

       130        140        150        160        170        180 
TEDWAIVIRK YHKLGTGFNP NTLDKQKERQ KGLPKQVFES DEAPDGNSYQ DDQDDLKRRS 

       190        200        210        220        230        240 
MSIDDTPRGS WACSIFDLKN SLPDALLPNL LDRTPNEEID RQNDDQRKSN RHKELFALHP 

       250        260        270        280        290        300 
SPDEEEPIER LSVPDIPKEH FGQRLLVKCL SLKFEIEIEP IFASLALYDV KEKKKISENF 

       310        320        330        340        350        360 
YFDLNSEQMK GLLRPHVPPA AITTLARSAI FSITYPSQDV FLVIKLEKVL QQGDIGECAE 

       370        380        390        400        410        420 
PYMIFKEADA TKNKEKLEKL KSQADQFCQR LGKYRMPFAW TAIHLMNIVS SAGSLERDST 

       430        440        450        460        470        480 
EVEISTGERK GSWSERRNSS IVGRRSLERT TSGDDACNLT SFRPATLTVT NFFKQEGDRL 

       490        500        510        520        530        540 
SDEDLYKFLA DMRRPSSVLR RLRPITAQLK IDISPAPENP HYCLTPELLQ VKLYPDSRVR 

       550        560        570        580        590        600 
PTREILEFPA RDVYVPNTTY RNLLYIYPQS LNFANRQGSA RNITVKVQFM YGEDPSNAMP 

       610        620        630        640        650        660 
VIFGKSSCSE FSKEAYTAVV YHNRSPDFHE EIKVKLPATL TDHHHLLFTF YHVSCQQKQN 

       670        680        690        700        710        720 
TPLETPVGYT WIPMLQNGRL KTGQFCLPVS LEKPPQAYSV LSPEVPLPGM KWVDNHKGVF 

       730        740        750        760        770        780 
NVEVVAVSSI HTQDPYLDKF FALVNALDEH LFPVRIGDMR IMENNLENEL KSSISALNSS 

       790        800        810        820        830        840 
QLEPVVRFLH LLLDKLILLV IRPPVIAGQI VNLGQASFEA MASIINRLHK NLEGNHDQHG 

       850        860        870        880        890        900 
RNSLLASYIH YVFRLPNTYP NSSSPGPGGL GGSVHYATMA RSAVRPASLN LNRSRSLSNS 

       910        920        930        940        950        960 
NPDISGTPTS PDDEVRSIIG SKGLDRSNSW VNTGGPKAAP WGSNPSPSAE STQAMDRSCN 

       970        980        990       1000       1010       1020 
RMSSHTETSS FLQTLTGRLP TKKLFHEELA LQWVVCSGSV RESALQQAWF FFELMVKSMV 

      1030       1040       1050       1060       1070       1080 
HHLYFNDKLE APRKSRFPER FMDDIAALVS TIASDIVSRF QKDTEMVERL NTSLAFFLND 

      1090       1100       1110       1120       1130       1140 
LLSVMDRGFV FSLIKSCYKQ VSSKLYSLPN PSVLVSLRLD FLRIICSHEH YVTLNLPCSL 

      1150       1160       1170       1180       1190       1200 
LTPPASPSPS VSSATSQSSG FSTNVQDQKI ANMFELSVPF RQQHYLAGLV LTELAVILDP 

      1210       1220       1230       1240       1250       1260 
DAEGLFGLHK KVINMVHNLL SSHDSDPRYS DPQIKARVAM LYLPLIGIIM ETVPQLYDFT 

      1270       1280       1290       1300       1310       1320 
ETHNQRGRPI CIATDDYESE SGSMISQTVA MAIAGTSVPQ LTRPGSFLLT STSGRQHTTF 

      1330       1340       1350       1360       1370       1380 
SAESSRSLLI CLLWVLKNAD ETVLQKWFTD LSVLQLNRLL DLLYLCVSCF EYKGKKVFER 

      1390       1400       1410       1420       1430       1440 
MNSLTFKKSK DMRAKLEEAI LGSIGARQEM VRRSRGQLGT YTIASPPERS PSGSAFGSQE 

      1450       1460       1470       1480       1490       1500 
NLRWRKDMTH WRQNTEKLDK SRAEIEHEAL IDGNLATEAN LIILDTLEIV VQTVSVTESK 

      1510       1520       1530       1540       1550       1560 
ESILGGVLKV LLHSMACNQS AVYLQHCFAT QRALVSKFPE LLFEEETEQC ADLCLRLLRH 

      1570       1580       1590       1600       1610       1620 
CSSSIGTIRS HASASLYLLM RQNFEIGNNF ARVKMQVTMS LSSLVGTSQN FNEEFLRRSL 

      1630       1640       1650       1660       1670       1680 
KTILTYAEED LELRETTFPD QVQDLVFNLH MILSDTVKMK EHQEDPEMLI DLMYRIAKGY 

      1690       1700       1710       1720       1730       1740 
QTSPDLRLTW LQNMAGKHSE RSNHAEAAQC LVHSAALVAE YLSMLEDRKY LPVGCVTFQN 

      1750       1760       1770       1780       1790       1800 
ISSNVLEESA VSDDVVSPDE EGICSGKYFT ESGLVGLLEQ AAASFSMAGM YEAVNEVYKV 

      1810       1820       1830       1840       1850       1860 
LIPIHEANRD AKKLSTIHGK LQEAFSKIVH QSTGWERMFG TYFRVGFYGT KFGDLDEQEF 

      1870       1880       1890       1900       1910       1920 
VYKEPAITKL AEISHRLEGF YGERFGEDVV EVIKDSNPVD KCKLDPNKAY IQITYVEPYF 

      1930       1940       1950       1960       1970       1980 
DTYEMKDRIT YFDKNYNLRR FMYCTPFTLD GRAHGELHEQ FKRKTILTTS HAFPYIKTRV 

      1990       2000       2010       2020       2030       2040 
NVTHKEEIIL TPIEVAIEDM QKKTQELAFA THQDPADPKM LQMVLQGSVG TTVNQGPLEV 

      2050       2060       2070       2080       2090       2100 
AQVFLSEIPS DPKLFRHHNK LRLCFKDFTK RCEDALRKNK SLIGPDQKEY QRELERNYHR 

      2110       2120       2130       2140 
LKEALQPLIN RKIPQLYKAV LPVTCHRDSF SRMSLRKMDL 

« Hide

Isoform 2 [UniParc].

Checksum: 56C741287C8296C4
Show »

FASTA2,129241,412
Isoform 3 [UniParc].

Checksum: 4A44093C2074BD4B
Show »

FASTA2,100238,534
Isoform 4 [UniParc].

Checksum: A768EB92CB1CDB3D
Show »

FASTA2,098238,274
Isoform 5 [UniParc].

Checksum: 0171AA19EEB3B57F
Show »

FASTA2,109239,422
Isoform 6 [UniParc].

Checksum: 2C21C8938ACE0AD5
Show »

FASTA2,131241,673

References

« Hide 'large scale' references
[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]"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. expand/collapse author list , 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].
[3]"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.
[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] 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 and Thalamus.
[5]"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.
[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 1332-2140 (ISOFORM 2).
Tissue: Ovary.
[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.
[8]"Phosphorylation and binding partner analysis of the TSC1-TSC2 complex."
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M.
Biochem. Biophys. Res. Commun. 333:818-826(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TSC1, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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.
[10]"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-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.
[11]"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].
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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.
[14]"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].
[15]"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.
[16]"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].
[17]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ341187 mRNA. Translation: ABC68221.1.
AL451044 expand/collapse EMBL AC list , AC096946, AC103923, AL138847 Genomic DNA. Translation: CAI13104.1.
AL451044, AC096946 Genomic DNA. Translation: CAI13105.1.
AL138847 expand/collapse EMBL AC list , AC096946, AC103923, AL451044 Genomic DNA. Translation: CAI22995.1.
DQ309763 mRNA. Translation: ABC33725.1. Frameshift.
DQ118679 mRNA. Translation: AAZ38451.1.
DQ118680 mRNA. Translation: AAZ38452.1.
AK055493 mRNA. Translation: BAB70933.1. Different initiation.
AK055905 mRNA. Translation: BAB71042.1. Frameshift.
AK125049 mRNA. Translation: BAC86032.1. Different initiation.
AB051558 mRNA. Translation: BAB21862.1.
BC016392 mRNA. Translation: AAH16392.2. Frameshift.
RefSeqNP_001258928.1. NM_001271999.1.
NP_001258929.1. NM_001272000.1.
NP_001258930.1. NM_001272001.1.
NP_212132.2. NM_033407.3.
XP_005271349.1. XM_005271292.1.
UniGeneHs.744927.

3D structure databases

ProteinModelPortalQ96N67.
SMRQ96N67. Positions 561-729, 1682-2113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124527. 33 interactions.
IntActQ96N67. 30 interactions.

PTM databases

PhosphoSiteQ96N67.

Polymorphism databases

DMDM122065170.

Proteomic databases

PaxDbQ96N67.
PRIDEQ96N67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251157; ENSP00000251157; ENSG00000116641. [Q96N67-2]
ENST00000340370; ENSP00000340742; ENSG00000116641. [Q96N67-5]
GeneID85440.
KEGGhsa:85440.
UCSCuc001dam.3. human. [Q96N67-6]
uc001dan.4. human. [Q96N67-3]
uc001dao.4. human. [Q96N67-4]
uc001dap.4. human. [Q96N67-5]
uc001daq.4. human. [Q96N67-2]

Organism-specific databases

CTD85440.
GeneCardsGC01M062920.
HGNCHGNC:19190. DOCK7.
HPAHPA008607.
neXtProtNX_Q96N67.
PharmGKBPA134872825.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242127.
HOVERGENHBG051390.
OMAYIHYVFR.
PhylomeDBQ96N67.
TreeFamTF313629.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ96N67.
BgeeQ96N67.
CleanExHS_DOCK7.
GenevestigatorQ96N67.

Family and domain databases

InterProIPR027007. DHR-1_domain.
IPR027357. DHR-2.
IPR026791. DOCK.
IPR010703. DOCK_C.
IPR021816. DOCK_C/D_N.
[Graphical view]
PANTHERPTHR23317. PTHR23317. 1 hit.
PfamPF06920. Ded_cyto. 1 hit.
PF14429. DOCK-C2. 1 hit.
PF11878. DUF3398. 1 hit.
[Graphical view]
PROSITEPS51650. DHR_1. 1 hit.
PS51651. DHR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDOCK7. human.
GeneWikiDock7.
GenomeRNAi85440.
NextBio76016.
PROQ96N67.

Entry information

Entry nameDOCK7_HUMAN
AccessionPrimary (citable) accession number: Q96N67
Secondary accession number(s): Q00M63 expand/collapse secondary AC list , Q2PPY7, Q45RE8, Q45RE9, Q5T1B9, Q5T1C0, Q6ZV32, Q8TB82, Q96NG6, Q9C092
Entry history
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 107 of the entry and version 4 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM