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P13115 (SRC1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Src-1

EC=2.7.10.2
Alternative name(s):
p60-Src-1
Gene names
Name:src-a
Synonyms:src1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cell membrane By similarity.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 532531Tyrosine-protein kinase Src-1
PRO_0000088145

Regions

Domain80 – 14162SH3
Domain147 – 24498SH2
Domain266 – 519254Protein kinase
Nucleotide binding272 – 2809ATP By similarity

Sites

Active site3851Proton acceptor By similarity
Binding site2941ATP By similarity

Amino acid modifications

Modified residue4151Phosphotyrosine; by autocatalysis By similarity
Lipidation21N-myristoyl glycine By similarity

Sequences

Sequence LengthMass (Da)Tools
P13115 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 83977919D1612D41

FASTA53259,895
        10         20         30         40         50         60 
MGATKSKPRE GGPRSRSLDI VEGSHQPFTS LSASQTPNKS LDSHRPPAQP FGGNCDLTPF 

        70         80         90        100        110        120 
GGINFSDTIT SPQRTGPLAG GVTTFVALYD YESRTETDLS FKKGERLQIV NNTEGDWWLA 

       130        140        150        160        170        180 
RSLSSGQTGY IPSNYVAPSD SIQAEEWYLG KITRREAERL LLSLENPRGT FLVRESETTK 

       190        200        210        220        230        240 
GAYCLSVSDY DANRGLNVKH YKIRKLDSGG FYITSRTQFI SLQQLVAYYS KHADGLCHRL 

       250        260        270        280        290        300 
TTVCPTAKPQ TQGLSRDAWE IPRDSLRLEL KLGQGCFGEV WMGTWNGTTR VAIKTLKPGT 

       310        320        330        340        350        360 
MSPEAFLQEA QVMKKLRHEK LVQLYAVVSE EPIYIVTEYI SKGSLLDFLK GEMGRYLRLP 

       370        380        390        400        410        420 
QLVDMAAQIA SGMAYVERMN YVHRDLRAAN ILVGENLVCK VADFGLARLI EDNEYTARQG 

       430        440        450        460        470        480 
AKFPIKWTAP EAALYGRFTI KSDVWSFGIL LTELTTKGRV PYPGMVNREV LDQVERGYRM 

       490        500        510        520        530 
PCPPDCPESL HDLMFQCWRK DPEERPTFEY LQAFLEDYFT ATEPQYQPGD NL 

« Hide

References

[1]"The two Xenopus laevis SRC genes are co-expressed and each produces functional pp60src."
Steele R.E., Unger T.F., Mardis M.J., Fero J.B.
J. Biol. Chem. 264:10649-10653(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Steele R.E.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 220; 242 AND 340.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24704 mRNA. Translation: AAA49962.2.
UniGeneXl.10268.

3D structure databases

ProteinModelPortalP13115.
SMRP13115. Positions 82-532.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP13115.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-6252879. src.

Phylogenomic databases

HOVERGENHBG008761.

Enzyme and pathway databases

BRENDA2.7.10.2. 6726.

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.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
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...

Entry information

Entry nameSRC1_XENLA
AccessionPrimary (citable) accession number: P13115
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 111 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families