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Q18PE1 (DOK7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein Dok-7
Alternative name(s):
Downstream of tyrosine kinase 7
Gene names
Name:DOK7
Synonyms:C4orf25
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable muscle-intrinsic activator of MUSK that plays an essential role in neuromuscular synaptogenesis. Acts in aneural activation of MUSK and subsequent acetylcholine receptor (AchR) clustering in myotubes. Induces autophosphorylation of MUSK. Ref.5

Subunit structure

Homodimer By similarity. Forms a heterotetramer composed of 2 DOK7 and 2 MUSK molecules which facilitates MUSK trans-autophosphorylation on tyrosine residue and activation By similarity. Interacts (via IRS-type PTB domain) with MUSK (via cytoplasmic part); requires MUSK phosphorylation. Ref.5

Subcellular location

Cell membrane; Peripheral membrane protein By similarity. Cell junctionsynapse By similarity. Note: Accumulates at neuromuscular junctions By similarity.

Tissue specificity

Preferentially expressed in skeletal muscle and heart. Present in thigh muscle, diaphragm and heart but not in the liver or spleen (at protein level). Ref.1

Domain

The PH domain mediated binding to phospholipids with phosphoinositol headgroups. Affinity is highest for phosphatidyl 3,4,5-trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate By similarity.

Involvement in disease

Myasthenia, limb-girdle, familial (LGM) [MIM:254300]: A congenital myasthenic syndrome characterized by a typical 'limb girdle' pattern of muscle weakness with small, simplified neuromuscular junctions but normal acetylcholine receptor and acetylcholinesterase function.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Sequence similarities

Contains 1 IRS-type PTB domain.

Contains 1 PH domain.

Sequence caution

The sequence BAC11367.1 differs from that shown. Reason: Contains a poly-A tail in the 5'region.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q18PE1-1)

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: Q18PE1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.
     139-178: VLARDIPPAV...FEGGTRCGYW → MMSSSWPGTS...ADSSLKAGPG
Note: No experimental confirmation available.
Isoform 4 (identifier: Q18PE1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     175-255: CGYWAGVFFL...SLLSHAGRPG → GWRLLPVLGR...TCGQAGQWRG
     256-504: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q18PE1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     500-504: VNPPP → GAAASAPGPA...ELEQRKAAPQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504Protein Dok-7
PRO_0000250371

Regions

Domain4 – 109106PH
Domain105 – 210106IRS-type PTB
Compositional bias262 – 35998Ser-rich

Natural variations

Alternative sequence1 – 138138Missing in isoform 2.
VSP_020633
Alternative sequence139 – 17840VLARD…RCGYW → MMSSSWPGTSPRLSRGSGSC LTSGATGPCQADSSLKAGPG in isoform 2.
VSP_020634
Alternative sequence175 – 25581CGYWA…AGRPG → GWRLLPVLGRGGADQLPVRL HRPRHLPHQGPLWAAAGSTR PKSPGTLDCGGACGPGSPGN PTAGEAAEPPLTCGQAGQWR G in isoform 4.
VSP_047252
Alternative sequence256 – 504249Missing in isoform 4.
VSP_047253
Alternative sequence500 – 5045VNPPP → GAAASAPGPATAHSGSPGPV AVDSPGPERPRGESPTYVNI PVSPSSRKQLHYMGLELQEA SEGVRGAGASLYAQIDIMAT ETAHRVGVRHARAREEQLSE LEQRKAAPQ in isoform 3.
VSP_020635
Natural variant31E → K in LGM; results in a significant reduction of AChR clusters. Ref.9
VAR_068750
Natural variant311P → T in LGM; results in a significant reduction of AChR clusters. Ref.9
VAR_068751
Natural variant331A → V in LGM; results in reduced stimulation of MUSK autophosphorylation. Ref.5 Ref.7
VAR_068752
Natural variant451S → L Does not affect AChR clusters number or complexity. Ref.8 Ref.9
Corresponds to variant rs62272670 [ dbSNP | Ensembl ].
VAR_068753
Natural variant771T → M in LGM; results in a decrease of branched, c-shaped and perforated AChR clusters. Ref.9
VAR_068754
Natural variant991A → V. Ref.9
Corresponds to variant rs138010842 [ dbSNP | Ensembl ].
VAR_068755
Natural variant1091G → C in LGM; results in a significant reduction of AChR clusters. Ref.9
VAR_068756
Natural variant1161V → M in LGM. Ref.8
VAR_068757
Natural variant1321H → Q in LGM. Ref.7
VAR_068758
Natural variant1391V → L in LGM; results in a significant reduction of AChR clusters. Ref.9
VAR_068759
Natural variant1461P → L in LGM. Ref.8
VAR_068760
Natural variant1571L → R in LGM. Ref.8
VAR_068761
Natural variant1581R → Q in LGM; reduced stimulation of MUSK autophosphorylation when associated with A-174; results in a significant reduction of AChR clusters. Ref.5 Ref.9
Corresponds to variant rs6811423 [ dbSNP | Ensembl ].
VAR_031246
Natural variant1611G → R in LGM; results in a significant reduction of AChR clusters. Ref.9
VAR_068762
Natural variant1661G → R in LGM; results in a significant reduction of AChR clusters. Ref.9
VAR_068763
Natural variant1711G → D in LGM; results in a significant reduction of AChR clusters. Ref.9
VAR_068764
Natural variant1711G → R in LGM. Ref.8
VAR_068765
Natural variant1721G → R in LGM. Ref.8
VAR_068766
Natural variant1801G → A in LGM; results in a significant reduction of AChR clusters. Ref.6 Ref.9
VAR_027544
Natural variant1801G → V in LGM. Ref.8
VAR_068767
Natural variant1971D → N. Ref.9
Corresponds to variant rs16844422 [ dbSNP | Ensembl ].
VAR_027545
Natural variant2611R → H. Ref.9
Corresponds to variant rs16844460 [ dbSNP | Ensembl ].
VAR_027546
Natural variant2721H → Q. Ref.9
Corresponds to variant rs115614731 [ dbSNP | Ensembl ].
VAR_068768
Natural variant2961Q → R. Ref.4 Ref.9
Corresponds to variant rs6811423 [ dbSNP | Ensembl ].
VAR_027547
Natural variant3231R → C. Ref.9
Corresponds to variant rs150728781 [ dbSNP | Ensembl ].
VAR_068769
Natural variant3791G → R.
Corresponds to variant rs6831659 [ dbSNP | Ensembl ].
VAR_050508
Natural variant3821E → K. Ref.9
VAR_068770
Natural variant4021R → Q. Ref.9
VAR_068771
Natural variant4151P → S. Ref.9
Corresponds to variant rs16844464 [ dbSNP | Ensembl ].
VAR_027548
Natural variant4271G → D.
Corresponds to variant rs2020433 [ dbSNP | Ensembl ].
VAR_027549
Natural variant4401A → T. Ref.9
VAR_068772
Natural variant4511R → W. Ref.9
Corresponds to variant rs16844470 [ dbSNP | Ensembl ].
VAR_027550
Natural variant4611G → D. Ref.2 Ref.4 Ref.9
Corresponds to variant rs9684786 [ dbSNP | Ensembl ].
VAR_027551
Natural variant4691P → H in LGM. Ref.7
Corresponds to variant rs147185207 [ dbSNP | Ensembl ].
VAR_068773
Natural variant5031P → T. Ref.9
Corresponds to variant rs184556570 [ dbSNP | Ensembl ].
VAR_068774

Experimental info

Mutagenesis301S → W: Reduced stimulation of MUSK autophosphorylation. Ref.5
Mutagenesis321V → A: Reduced stimulation of MUSK autophosphorylation. Ref.5
Mutagenesis1741R → A: Reduced stimulation of MUSK autophosphorylation; when associated with Q-158. Ref.5

Sequences

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

Last modified July 25, 2006. Version 1.
Checksum: 54750E0B0BC33317

FASTA50453,097
        10         20         30         40         50         60 
MTEAALVEGQ VKLRDGKKWK SRWLVLRKPS PVADCLLMLV YKDKSERIKG LRERSSLTLE 

        70         80         90        100        110        120 
DICGLEPGLP YEGLVHTLAI VCLSQAIMLG FDSHEAMCAW DARIRYALGE VHRFHVTVAP 

       130        140        150        160        170        180 
GTKLESGPAT LHLCNDVLVL ARDIPPAVTG QWKLSDLRRY GAVPSGFIFE GGTRCGYWAG 

       190        200        210        220        230        240 
VFFLSSAEGE QISFLFDCIV RGISPTKGPF GLRPVLPDPS PPGPSTVEER VAQEALETLQ 

       250        260        270        280        290        300 
LEKRLSLLSH AGRPGSGGDD RSLSSSSSEA SHLDVSASSR LTAWPEQSSS SASTSQEGPR 

       310        320        330        340        350        360 
PAAAQAAGEA MVGASRPPPK PLRPRQLQEV GRQSSSDSGI ATGSHSSYSS SLSSYAGSSL 

       370        380        390        400        410        420 
DVWRATDELG SLLSLPAAGA PEPSLCTCLP GTVEYQVPTS LRAHYDTPRS LCLAPRDHSP 

       430        440        450        460        470        480 
PSQGSPGNSA ARDSGGQTSA GCPSGWLGTR RRGLVMEAPQ GSEATLPGPA PGEPWEAGGP 

       490        500 
HAGPPPAFFS ACPVCGGLKV NPPP 

« Hide

Isoform 2 [UniParc].

Checksum: 8CFC71602C970AC3
Show »

FASTA36637,161
Isoform 4 [UniParc].

Checksum: 098963FABA4A7185
Show »

FASTA25527,514
Isoform 3 [UniParc].

Checksum: 384FFACAA0AD8359
Show »

FASTA60863,938

References

« Hide 'large scale' references
[1]"The muscle protein Dok-7 is essential for neuromuscular synaptogenesis."
Okada K., Inoue A., Okada M., Murata Y., Kakuta S., Jigami T., Kubo S., Shiraishi H., Eguchi K., Motomura M., Akiyama T., Iwakura Y., Higuchi O., Yamanashi Y.
Science 312:1802-1805(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"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 2), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ASP-461.
Tissue: Brain and Ovary.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1), VARIANTS ARG-296 AND ASP-461.
Tissue: Blood and Mammary gland.
[5]"The cytoplasmic adaptor protein Dok7 activates the receptor tyrosine kinase MuSK via dimerization."
Bergamin E., Hallock P.T., Burden S.J., Hubbard S.R.
Mol. Cell 39:100-109(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUSK, FUNCTION, CHARACTERIZATION OF VARIANTS LGM VAL-33 AND GLN-158, MUTAGENESIS OF SER-30; VAL-32 AND ARG-174.
[6]"Dok-7 mutations underlie a neuromuscular junction synaptopathy."
Beeson D., Higuchi O., Palace J., Cossins J., Spearman H., Maxwell S., Newsom-Davis J., Burke G., Fawcett P., Motomura M., Muller J.S., Lochmuller H., Slater C., Vincent A., Yamanashi Y.
Science 313:1975-1978(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGM ALA-180.
[7]"Phenotypical spectrum of DOK7 mutations in congenital myasthenic syndromes."
Muller J.S., Herczegfalvi A., Vilchez J.J., Colomer J., Bachinski L.L., Mihaylova V., Santos M., Schara U., Deschauer M., Shevell M., Poulin C., Dias A., Soudo A., Hietala M., Aarimaa T., Krahe R., Karcagi V., Huebner A. expand/collapse author list , Beeson D., Abicht A., Lochmuller H.
Brain 130:1497-1506(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGM VAL-33; GLN-132 AND HIS-469.
[8]"Phenotype genotype analysis in 15 patients presenting a congenital myasthenic syndrome due to mutations in DOK7."
Ben Ammar A., Petit F., Alexandri N., Gaudon K., Bauche S., Rouche A., Gras D., Fournier E., Koenig J., Stojkovic T., Lacour A., Petiot P., Zagnoli F., Viollet L., Pellegrini N., Orlikowski D., Lazaro L., Ferrer X. expand/collapse author list , Stoltenburg G., Paturneau-Jouas M., Hentati F., Fardeau M., Sternberg D., Hantai D., Richard P., Eymard B.
J. Neurol. 257:754-766(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGM MET-116; LEU-146; ARG-157; ARG-171; ARG-172 AND VAL-180, VARIANT LEU-45.
[9]"The spectrum of mutations that underlie the neuromuscular junction synaptopathy in DOK7 congenital myasthenic syndrome."
Cossins J., Liu W.W., Belaya K., Maxwell S., Oldridge M., Lester T., Robb S., Beeson D.
Hum. Mol. Genet. 21:3765-3775(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGM LYS-3; THR-31; MET-77; CYS-109; LEU-139; GLN-158; ARG-161; ARG-166; ASP-171 AND ALA-180, VARIANTS LEU-45; VAL-99; ASN-197; HIS-261; GLN-272; ARG-296; CYS-323; LYS-382; GLN-402; SER-415; THR-440; TRP-451; ASP-461 AND THR-503, CHARACTERIZATION OF VARIANTS LGM LYS-3; THR-31; MET-77; CYS-109; LEU-139; GLN-158; ARG-161; ARG-166; ASP-171 AND ALA-180, CHARACTERIZATION OF VARIANT LEU-45.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB220918 mRNA. Translation: BAE96739.1.
AK075037 mRNA. Translation: BAC11367.1. Sequence problems.
AK091037 mRNA. Translation: BAC03572.1.
AL590235 Genomic DNA. No translation available.
BC043568 mRNA. Translation: AAH43568.1.
BC062369 mRNA. Translation: AAH62369.1.
BC131544 mRNA. Translation: AAI31545.1.
BC141852 mRNA. Translation: AAI41853.1.
CCDSCCDS3370.2. [Q18PE1-1]
CCDS54717.1. [Q18PE1-4]
RefSeqNP_001158145.1. NM_001164673.1. [Q18PE1-4]
NP_001243825.1. NM_001256896.1.
NP_775931.3. NM_173660.4. [Q18PE1-1]
UniGeneHs.122110.
Hs.701584.

3D structure databases

ProteinModelPortalQ18PE1.
SMRQ18PE1. Positions 3-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130124. 1 interaction.
IntActQ18PE1. 1 interaction.
STRING9606.ENSP00000344432.

PTM databases

PhosphoSiteQ18PE1.

Polymorphism databases

DMDM115311705.

Proteomic databases

PaxDbQ18PE1.
PRIDEQ18PE1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340083; ENSP00000344432; ENSG00000175920. [Q18PE1-1]
ENST00000389653; ENSP00000374304; ENSG00000175920. [Q18PE1-3]
ENST00000507039; ENSP00000423614; ENSG00000175920. [Q18PE1-4]
GeneID285489.
KEGGhsa:285489.
UCSCuc003ghd.3. human. [Q18PE1-1]
uc003ghf.4. human. [Q18PE1-2]

Organism-specific databases

CTD285489.
GeneCardsGC04P003465.
GeneReviewsDOK7.
HGNCHGNC:26594. DOK7.
HPAHPA059449.
MIM254300. phenotype.
610285. gene.
neXtProtNX_Q18PE1.
Orphanet994. Fetal akinesia deformation sequence.
98913. Postsynaptic congenital myasthenic syndromes.
PharmGKBPA162384035.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69734.
HOGENOMHOG000230953.
HOVERGENHBG080009.
OMASLDICHG.
OrthoDBEOG75B84J.
PhylomeDBQ18PE1.
TreeFamTF332288.

Enzyme and pathway databases

SignaLinkQ18PE1.

Gene expression databases

ArrayExpressQ18PE1.
BgeeQ18PE1.
CleanExHS_DOK7.
GenevestigatorQ18PE1.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF02174. IRS. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS51064. IRS_PTB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi285489.
NextBio95544.
PROQ18PE1.
SOURCESearch...

Entry information

Entry nameDOK7_HUMAN
AccessionPrimary (citable) accession number: Q18PE1
Secondary accession number(s): A2A499 expand/collapse secondary AC list , A2RRD4, E9PB56, Q6P6A6, Q86XG5, Q8N2J3, Q8NBC1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: July 25, 2006
Last modified: July 9, 2014
This is version 78 of the entry and version 1 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 4

Human chromosome 4: entries, gene names and cross-references to MIM