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Protein

Crk-like protein

Gene

Crkl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May mediate the transduction of intracellular signals.

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. anterior/posterior pattern specification Source: MGI
  2. blood vessel development Source: MGI
  3. heart development Source: MGI
  4. organ morphogenesis Source: MGI
  5. parathyroid gland development Source: MGI
  6. pattern specification process Source: MGI
  7. thymus development Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_278498. Downstream signal transduction.
REACT_283484. Frs2-mediated activation.
REACT_286373. Regulation of signaling by CBL.

Names & Taxonomyi

Protein namesi
Recommended name:
Crk-like protein
Gene namesi
Name:Crkl
Synonyms:Crkol
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:104686. Crkl.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Crk-like proteinPRO_0000079348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271PhosphotyrosineBy similarity
Modified residuei207 – 2071PhosphotyrosineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47941.
PaxDbiP47941.
PRIDEiP47941.

2D gel databases

REPRODUCTION-2DPAGEIPI00113362.

PTM databases

PhosphoSiteiP47941.

Expressioni

Gene expression databases

BgeeiP47941.
ExpressionAtlasiP47941. baseline and differential.
GenevestigatoriP47941.

Interactioni

Subunit structurei

Interacts with DOCK2 and EPOR. Interacts with phosphorylated CBLB and IRS4 (By similarity). Interacts with INPP5D/SHIP1.By similarity1 Publication

Protein-protein interaction databases

BioGridi198888. 16 interactions.
IntActiP47941. 5 interactions.
MINTiMINT-4092019.
STRINGi10090.ENSMUSP00000006293.

Structurei

3D structure databases

ProteinModelPortaliP47941.
SMRiP47941. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 10289SH2PROSITE-ProRule annotationAdd
BLAST
Domaini123 – 18361SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini235 – 29662SH3 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the CRK family.Curated
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG292767.
GeneTreeiENSGT00390000001475.
HOGENOMiHOG000236288.
HOVERGENiHBG105616.
InParanoidiP47941.
KOiK04438.
OMAiRTLYDFT.
OrthoDBiEOG7NW69P.
PhylomeDBiP47941.
TreeFamiTF321436.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47941-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSARFDSSD RSAWYMGPVT RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL
60 70 80 90 100
SVSENSRVSH YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE
110 120 130 140 150
PAPRYPSPPV GSVSAPNLPT AEENLEYVRT LYDFPGNDAE DLPFKKGELL
160 170 180 190 200
VIIEKPEEQW WSARNKDGRV GMIPVPYVEK LVRSSPHGKH GNRNSNSYGI
210 220 230 240 250
PEPAHAYAQP QTTTPLPTVA STPGAAINPL PSTQNGPVFA KAIQKRVPCA
260 270 280 290 300
YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD

DNE
Length:303
Mass (Da):33,830
Last modified:January 31, 2005 - v2
Checksum:iA8C801F78EF73573
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651N → T in CAA62220 (PubMed:7478571).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90648 mRNA. Translation: CAA62220.1.
AK048641 mRNA. Translation: BAC33406.1.
AK052315 mRNA. Translation: BAC34933.1.
AK163981 mRNA. Translation: BAE37567.1.
CCDSiCCDS28002.1.
PIRiS58352.
RefSeqiNP_001264160.1. NM_001277231.1.
NP_031790.2. NM_007764.5.
UniGeneiMm.21048.
Mm.451241.
Mm.486420.

Genome annotation databases

EnsembliENSMUST00000006293; ENSMUSP00000006293; ENSMUSG00000006134.
GeneIDi12929.
KEGGimmu:12929.
UCSCiuc007ykv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90648 mRNA. Translation: CAA62220.1.
AK048641 mRNA. Translation: BAC33406.1.
AK052315 mRNA. Translation: BAC34933.1.
AK163981 mRNA. Translation: BAE37567.1.
CCDSiCCDS28002.1.
PIRiS58352.
RefSeqiNP_001264160.1. NM_001277231.1.
NP_031790.2. NM_007764.5.
UniGeneiMm.21048.
Mm.451241.
Mm.486420.

3D structure databases

ProteinModelPortaliP47941.
SMRiP47941. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198888. 16 interactions.
IntActiP47941. 5 interactions.
MINTiMINT-4092019.
STRINGi10090.ENSMUSP00000006293.

PTM databases

PhosphoSiteiP47941.

2D gel databases

REPRODUCTION-2DPAGEIPI00113362.

Proteomic databases

MaxQBiP47941.
PaxDbiP47941.
PRIDEiP47941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006293; ENSMUSP00000006293; ENSMUSG00000006134.
GeneIDi12929.
KEGGimmu:12929.
UCSCiuc007ykv.1. mouse.

Organism-specific databases

CTDi1399.
MGIiMGI:104686. Crkl.

Phylogenomic databases

eggNOGiNOG292767.
GeneTreeiENSGT00390000001475.
HOGENOMiHOG000236288.
HOVERGENiHBG105616.
InParanoidiP47941.
KOiK04438.
OMAiRTLYDFT.
OrthoDBiEOG7NW69P.
PhylomeDBiP47941.
TreeFamiTF321436.

Enzyme and pathway databases

ReactomeiREACT_278498. Downstream signal transduction.
REACT_283484. Frs2-mediated activation.
REACT_286373. Regulation of signaling by CBL.

Miscellaneous databases

NextBioi282596.
PROiP47941.
SOURCEiSearch...

Gene expression databases

BgeeiP47941.
ExpressionAtlasiP47941. baseline and differential.
GenevestigatoriP47941.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tyrosine phosphorylation of murine Crkl."
    de Jong R.L., Haataja L., Voncken J.W., Heisterkamp N., Groffen J.
    Oncogene 11:1469-1474(1994) [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.
    , 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(2004) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPP5D.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiCRKL_MOUSE
AccessioniPrimary (citable) accession number: P47941
Secondary accession number(s): Q3TQ18, Q8BGC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1996
Last sequence update: January 31, 2005
Last modified: March 31, 2015
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.