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P47941 (CRKL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Crk-like protein
Gene names
Name:Crkl
Synonyms:Crkol
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May mediate the transduction of intracellular signals.

Subunit structure

Interacts with DOCK2 and EPOR. Interacts with phosphorylated CBLB and IRS4 By similarity. Interacts with INPP5D/SHIP1. Ref.3

Post-translational modification

Phosphorylated on tyrosine. Phosphorylation is prominent during early development, but decreases at later embryonic stages and in newborn mice.

Sequence similarities

Belongs to the CRK family.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Crk-like protein
PRO_0000079348

Regions

Domain14 – 10289SH2
Domain123 – 18361SH3 1
Domain235 – 29662SH3 2

Amino acid modifications

Modified residue1071Phosphoserine Ref.4
Modified residue1271Phosphotyrosine By similarity
Modified residue1321Phosphotyrosine Ref.6
Modified residue2071Phosphotyrosine Ref.6
Modified residue2511Phosphotyrosine Ref.5

Experimental info

Sequence conflict1651N → T in CAA62220. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47941 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: A8C801F78EF73573

FASTA30333,830
        10         20         30         40         50         60 
MSSARFDSSD RSAWYMGPVT RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL SVSENSRVSH 

        70         80         90        100        110        120 
YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPV GSVSAPNLPT 

       130        140        150        160        170        180 
AEENLEYVRT LYDFPGNDAE DLPFKKGELL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK 

       190        200        210        220        230        240 
LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPTVA STPGAAINPL PSTQNGPVFA 

       250        260        270        280        290        300 
KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD 


DNE

« Hide

References

« Hide 'large scale' references
[1]"Tyrosine phosphorylation of murine Crkl."
de Jong R.L., Haataja L., Voncken J.W., Heisterkamp N., Groffen J.
Oncogene 11:1469-1474(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL X CBA.
Tissue: Placenta.
[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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Embryonic head and Embryonic heart.
[3]"SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates migration through two critical tyrosine residues and forms a novel signaling complex with DOK1 and CRKL."
Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R., Griffin J.D.
J. Biol. Chem. 276:2451-2458(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INPP5D.
[4]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, MASS SPECTROMETRY.
Tissue: Embryonic brain.
[5]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-251, MASS SPECTROMETRY.
[6]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132 AND TYR-207, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X90648 mRNA. Translation: CAA62220.1.
AK048641 mRNA. Translation: BAC33406.1.
AK052315 mRNA. Translation: BAC34933.1.
AK163981 mRNA. Translation: BAE37567.1.
IPIIPI00113362.
PIRS58352.
RefSeqNP_031790.2. NM_007764.4.
UniGeneMm.21048.
Mm.451241.
Mm.486420.

3D structure databases

ProteinModelPortalP47941.
SMRP47941. Positions 1-303.
ModBaseSearch...

Protein-protein interaction databases

IntActP47941. 3 interactions.
STRING10090.ENSMUSP00000006293.

PTM databases

PhosphoSiteP47941.

2D gel databases

REPRODUCTION-2DPAGEIPI00113362.

Proteomic databases

PaxDbP47941.
PRIDEP47941.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006293; ENSMUSP00000006293; ENSMUSG00000006134.
GeneID12929.
KEGGmmu:12929.

Organism-specific databases

CTD1399.
MGIMGI:104686. Crkl.

Phylogenomic databases

eggNOGNOG292767.
GeneTreeENSGT00390000001475.
HOGENOMHOG000236288.
HOVERGENHBG105616.
InParanoidP47941.
KOK04438.
OMASRNSNSY.
OrthoDBEOG4NS3C3.

Gene expression databases

ArrayExpressP47941.
BgeeP47941.
GenevestigatorP47941.
GermOnlineENSMUSG00000006134. Mus musculus.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMSSF50044. SH3. 2 hits.
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282596.
SOURCESearch...

Entry information

Entry nameCRKL_MOUSE
AccessionPrimary (citable) accession number: P47941
Secondary accession number(s): Q3TQ18, Q8BGC5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 2005
Last modified: April 3, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents