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P47941

- CRKL_MOUSE

UniProt

P47941 - CRKL_MOUSE

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Protein

Crk-like protein

Gene

Crkl

Organism
Mus musculus (Mouse)
Status
Reviewed - 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: Ensembl

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_198634. Regulation of signaling by CBL.
REACT_230639. Downstream signal transduction.
REACT_262560. Frs2-mediated activation.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:104686. Crkl.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
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:February 1, 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 .
CCDSi CCDS28002.1.
PIRi S58352.
RefSeqi NP_001264160.1. NM_001277231.1.
NP_031790.2. NM_007764.5.
UniGenei Mm.21048.
Mm.451241.
Mm.486420.

3D structure databases

ProteinModelPortali P47941.
SMRi P47941. Positions 1-303.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198888. 16 interactions.
IntActi P47941. 5 interactions.
MINTi MINT-4092019.
STRINGi 10090.ENSMUSP00000006293.

PTM databases

PhosphoSitei P47941.

2D gel databases

REPRODUCTION-2DPAGE IPI00113362.

Proteomic databases

MaxQBi P47941.
PaxDbi P47941.
PRIDEi P47941.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000006293 ; ENSMUSP00000006293 ; ENSMUSG00000006134 .
GeneIDi 12929.
KEGGi mmu:12929.
UCSCi uc007ykv.1. mouse.

Organism-specific databases

CTDi 1399.
MGIi MGI:104686. Crkl.

Phylogenomic databases

eggNOGi NOG292767.
GeneTreei ENSGT00390000001475.
HOGENOMi HOG000236288.
HOVERGENi HBG105616.
InParanoidi P47941.
KOi K04438.
OMAi RTLYDFT.
OrthoDBi EOG7NW69P.
PhylomeDBi P47941.
TreeFami TF321436.

Enzyme and pathway databases

Reactomei REACT_198634. Regulation of signaling by CBL.
REACT_230639. Downstream signal transduction.
REACT_262560. Frs2-mediated activation.

Miscellaneous databases

NextBioi 282596.
PROi P47941.
SOURCEi Search...

Gene expression databases

Bgeei P47941.
ExpressionAtlasi P47941. baseline and differential.
Genevestigatori P47941.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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. 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(2008) [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: February 1, 1996
Last sequence update: February 1, 2005
Last modified: November 26, 2014
This is version 125 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