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Q9H3Y6 (SRMS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Srms

EC=2.7.10.2
Gene names
Name:SRMS
Synonyms:C20orf148
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor tyrosine-protein kinase which phosphorylates DOK1 on tyrosine residues. May be involved in proliferation or differentiation of keratinocytes in the skin. Ref.2

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Interacts (via the SH2 and SH3 domains) with DOK1. Ref.2

Subcellular location

Cytoplasm. Note: Localizes to punctate cytoplasmic structures. Ref.2

Tissue specificity

Highly expressed in most breast cancers (at protein level).

Domain

The N-terminal region regulates its kinase activity (Ref.2).

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-tyrosine autophosphorylation

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DOK1Q997047EBI-8541270,EBI-1384360

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Tyrosine-protein kinase Srms
PRO_0000088160

Regions

Domain51 – 11262SH3
Domain120 – 21293SH2
Domain230 – 488259Protein kinase
Nucleotide binding236 – 2449ATP By similarity
Region1 – 5151N-terminal

Sites

Active site3501Proton acceptor By similarity
Binding site2581ATP

Amino acid modifications

Modified residue3801Phosphotyrosine; by autocatalysis Ref.2

Natural variations

Natural variant731R → C. Ref.3
Corresponds to variant rs56053583 [ dbSNP | Ensembl ].
VAR_041831
Natural variant751G → R. Ref.3
Corresponds to variant rs55863722 [ dbSNP | Ensembl ].
VAR_041832
Natural variant881I → V. Ref.3
Corresponds to variant rs35558836 [ dbSNP | Ensembl ].
VAR_041833
Natural variant2181P → L.
Corresponds to variant rs378483 [ dbSNP | Ensembl ].
VAR_051700
Natural variant2551V → M.
Corresponds to variant rs34969822 [ dbSNP | Ensembl ].
VAR_051701
Natural variant3011V → L. Ref.3
Corresponds to variant rs310657 [ dbSNP | Ensembl ].
VAR_041834
Natural variant3251P → L.
Corresponds to variant rs8122355 [ dbSNP | Ensembl ].
VAR_051702
Natural variant3771D → E. Ref.3
Corresponds to variant rs55838540 [ dbSNP | Ensembl ].
VAR_041835
Natural variant3971A → V. Ref.3
Corresponds to variant rs6011889 [ dbSNP | Ensembl ].
VAR_041836
Natural variant4521P → L. Ref.3
Corresponds to variant rs8120713 [ dbSNP | Ensembl ].
VAR_041837
Natural variant4531A → T. Ref.3
Corresponds to variant rs310655 [ dbSNP | Ensembl ].
VAR_041838
Natural variant4571V → L. Ref.3
Corresponds to variant rs310654 [ dbSNP | Ensembl ].
VAR_041839
Natural variant4651S → T. Ref.3
Corresponds to variant rs33933649 [ dbSNP | Ensembl ].
VAR_041840

Experimental info

Mutagenesis2231W → A: Loss of kinase activity. Ref.2
Mutagenesis2581K → M: Loss of kinase activity. Exhibits a diffused cytoplasmic localization. Ref.2
Mutagenesis3801Y → F: Significant reduction in phosphorylation. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9H3Y6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 83193AD26C5F6F68

FASTA48854,507
        10         20         30         40         50         60 
MEPFLRRRLA FLSFFWDKIW PAGGEPDHGT PGSLDPNTDP VPTLPAEPCS PFPQLFLALY 

        70         80         90        100        110        120 
DFTARCGGEL SVRRGDRLCA LEEGGGYIFA RRLSGQPSAG LVPITHVAKA SPETLSDQPW 

       130        140        150        160        170        180 
YFSGVSRTQA QQLLLSPPNE PGAFLIRPSE SSLGGYSLSV RAQAKVCHYR VSMAADGSLY 

       190        200        210        220        230        240 
LQKGRLFPGL EELLTYYKAN WKLIQNPLLQ PCMPQKAPRQ DVWERPHSEF ALGRKLGEGY 

       250        260        270        280        290        300 
FGEVWEGLWL GSLPVAIKVI KSANMKLTDL AKEIQTLKGL RHERLIRLHA VCSGGEPVYI 

       310        320        330        340        350        360 
VTELMRKGNL QAFLGTPEGR ALRLPPLLGF ACQVAEGMSY LEEQRVVHRD LAARNVLVDD 

       370        380        390        400        410        420 
GLACKVADFG LARLLKDDIY SPSSSSKIPV KWTAPEAANY RVFSQKSDVW SFGVLLHEVF 

       430        440        450        460        470        480 
TYGQCPYEGM TNHETLQQIM RGYRLPRPAA CPAEVYVLML ECWRSSPEER PSFATLREKL 


HAIHRCHP 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The unique N-terminal region of SRMS regulates enzymatic activity and phosphorylation of its novel substrate Dok1."
Goel R.K., Miah S., Black K., Kalra N., Dai C., Lukong K.E.
FEBS J. 280:4539-4559(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DOK1, N-TERMINAL REGION, AUTOPHOSPHORYLATION AT TYR-380, MUTAGENESIS OF TRP-223; LYS-258 AND TYR-380.
[3]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-73; ARG-75; VAL-88; LEU-301; GLU-377; VAL-397; LEU-452; THR-453; LEU-457 AND THR-465.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL121829 Genomic DNA. Translation: CAC15526.1.
RefSeqNP_543013.1. NM_080823.3.

3D structure databases

ProteinModelPortalQ9H3Y6.
SMRQ9H3Y6. Positions 56-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112603. 2 interactions.
IntActQ9H3Y6. 1 interaction.
STRING9606.ENSP00000217188.

Chemistry

BindingDBQ9H3Y6.
ChEMBLCHEMBL5703.
GuidetoPHARMACOLOGY2207.

PTM databases

PhosphoSiteQ9H3Y6.

Polymorphism databases

DMDM27805732.

Proteomic databases

PaxDbQ9H3Y6.
PRIDEQ9H3Y6.

Protocols and materials databases

DNASU6725.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217188; ENSP00000217188; ENSG00000125508.
GeneID6725.
KEGGhsa:6725.
UCSCuc002yfi.1. human.

Organism-specific databases

CTD6725.
GeneCardsGC20M062172.
HGNCHGNC:11298. SRMS.
HPACAB044668.
CAB044669.
neXtProtNX_Q9H3Y6.
PharmGKBPA36122.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidQ9H3Y6.
KOK08895.
OMALYEVFTY.
OrthoDBEOG7KM5SC.
PhylomeDBQ9H3Y6.
TreeFamTF351634.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ9H3Y6.

Gene expression databases

BgeeQ9H3Y6.
CleanExHS_SRMS.
GenevestigatorQ9H3Y6.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi6725.
NextBio26232.
PROQ9H3Y6.

Entry information

Entry nameSRMS_HUMAN
AccessionPrimary (citable) accession number: Q9H3Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 113 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

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 20

Human chromosome 20: entries, gene names and cross-references to MIM