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P46109

- CRKL_HUMAN

UniProt

P46109 - CRKL_HUMAN

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Protein

Crk-like protein

Gene
CRKL
Organism
Homo sapiens (Human)
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: UniProtKB
  2. protein binding Source: IntAct
  3. SH3/SH2 adaptor activity Source: ProtInc
  4. signal transducer activity Source: ProtInc

GO - Biological processi

  1. activation of MAPKK activity Source: Reactome
  2. anterior/posterior pattern specification Source: Ensembl
  3. blood vessel development Source: Ensembl
  4. heart development Source: Ensembl
  5. intracellular signal transduction Source: ProtInc
  6. JNK cascade Source: ProtInc
  7. neurotrophin TRK receptor signaling pathway Source: Reactome
  8. organ morphogenesis Source: Ensembl
  9. parathyroid gland development Source: Ensembl
  10. positive regulation of signal transduction Source: GOC
  11. Ras protein signal transduction Source: ProtInc
  12. thymus development Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12076. Frs2-mediated activation.
REACT_17025. Downstream signal transduction.
REACT_23787. Regulation of signaling by CBL.
SignaLinkiP46109.

Names & Taxonomyi

Protein namesi
Recommended name:
Crk-like protein
Gene namesi
Name:CRKL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:2363. CRKL.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endosome Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

Orphaneti261330. Distal 22q11.2 microdeletion syndrome.
PharmGKBiPA26881.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Crk-like proteinPRO_0000079347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271Phosphotyrosine1 Publication
Modified residuei207 – 2071Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46109.
PaxDbiP46109.
PeptideAtlasiP46109.
PRIDEiP46109.

2D gel databases

OGPiP46109.

PTM databases

PhosphoSiteiP46109.

Expressioni

Gene expression databases

BgeeiP46109.
CleanExiHS_CRKL.
GenevestigatoriP46109.

Organism-specific databases

HPAiHPA001100.

Interactioni

Subunit structurei

Interacts with INPP5D/SHIP1. Interacts with DOCK2 and EPOR. Interacts with phosphorylated CBLB and IRS4.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-910,EBI-375543
CBLP226812EBI-910,EBI-518228
DCBLD2Q96PD23EBI-910,EBI-8536103
EGFRP005332EBI-910,EBI-297353
ERBB2P046262EBI-910,EBI-641062
ERBB3P218603EBI-910,EBI-720706
FLT1P179489EBI-910,EBI-1026718
GAB1Q134803EBI-910,EBI-517684
Kcnma1Q084605EBI-910,EBI-1633915From a different organism.
Kidins220Q9EQG62EBI-910,EBI-976654From a different organism.
MAP4K1Q929185EBI-910,EBI-881
PIK3R1P279862EBI-910,EBI-79464
PTK2Q053972EBI-910,EBI-702142
RAPGEF1Q139052EBI-910,EBI-976876
SOS1Q078892EBI-910,EBI-297487

Protein-protein interaction databases

BioGridi107789. 66 interactions.
DIPiDIP-29165N.
IntActiP46109. 55 interactions.
MINTiMINT-137265.
STRINGi9606.ENSP00000346300.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144
Beta strandi15 – 184
Helixi21 – 288
Beta strandi29 – 313
Beta strandi36 – 405
Beta strandi42 – 465
Beta strandi48 – 547
Beta strandi57 – 6610
Turni67 – 693
Beta strandi70 – 734
Beta strandi78 – 803
Helixi81 – 888
Beta strandi93 – 964
Beta strandi105 – 1073
Beta strandi119 – 13214
Beta strandi138 – 1414
Beta strandi146 – 1549
Beta strandi157 – 1648
Beta strandi170 – 1745
Helixi175 – 1773
Beta strandi178 – 1825
Helixi190 – 1923
Helixi203 – 2053
Beta strandi238 – 2425
Beta strandi248 – 2514
Beta strandi253 – 2553
Beta strandi263 – 2697
Beta strandi271 – 2799
Beta strandi282 – 2876
Helixi288 – 2903
Beta strandi291 – 2933
Beta strandi296 – 2994

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BZXX-ray2.80A237-303[»]
2BZYX-ray2.50A/B237-303[»]
2DBKNMR-A229-303[»]
2EO3NMR-A1-104[»]
2LQNNMR-A1-303[»]
2LQWNMR-A1-303[»]
ProteinModelPortaliP46109.
SMRiP46109. Positions 1-303.

Miscellaneous databases

EvolutionaryTraceiP46109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 10289SH2Add
BLAST
Domaini123 – 18361SH3 1Add
BLAST
Domaini235 – 29662SH3 2Add
BLAST

Sequence similaritiesi

Belongs to the CRK family.
Contains 1 SH2 domain.
Contains 2 SH3 domains.

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG292767.
HOGENOMiHOG000236288.
HOVERGENiHBG105616.
InParanoidiP46109.
KOiK04438.
OMAiRTLYDFT.
OrthoDBiEOG7NW69P.
PhylomeDBiP46109.
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.

P46109-1 [UniParc]FASTAAdd to Basket

« Hide

MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL    50
SVSENSRVSH YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE 100
PAPRYPSPPM GSVSAPNLPT AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL 150
VIIEKPEEQW WSARNKDGRV GMIPVPYVEK LVRSSPHGKH GNRNSNSYGI 200
PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA KAIQKRVPCA 250
YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD 300
ENE 303
Length:303
Mass (Da):33,777
Last modified:November 1, 1995 - v1
Checksum:i294CF1EE2CD44B81
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59656 mRNA. Translation: CAA42199.1.
CR456423 mRNA. Translation: CAG30309.1.
AK292909 mRNA. Translation: BAF85598.1.
CH471176 Genomic DNA. Translation: EAX02932.1.
CH471176 Genomic DNA. Translation: EAX02933.1.
CH471176 Genomic DNA. Translation: EAX02934.1.
BC043500 mRNA. Translation: AAH43500.1.
CCDSiCCDS13785.1.
PIRiS41754.
RefSeqiNP_005198.1. NM_005207.3.
UniGeneiHs.5613.

Genome annotation databases

EnsembliENST00000354336; ENSP00000346300; ENSG00000099942.
ENST00000411769; ENSP00000396646; ENSG00000099942.
GeneIDi1399.
KEGGihsa:1399.
UCSCiuc002ztf.2. human.

Polymorphism databases

DMDMi1169094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59656 mRNA. Translation: CAA42199.1 .
CR456423 mRNA. Translation: CAG30309.1 .
AK292909 mRNA. Translation: BAF85598.1 .
CH471176 Genomic DNA. Translation: EAX02932.1 .
CH471176 Genomic DNA. Translation: EAX02933.1 .
CH471176 Genomic DNA. Translation: EAX02934.1 .
BC043500 mRNA. Translation: AAH43500.1 .
CCDSi CCDS13785.1.
PIRi S41754.
RefSeqi NP_005198.1. NM_005207.3.
UniGenei Hs.5613.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BZX X-ray 2.80 A 237-303 [» ]
2BZY X-ray 2.50 A/B 237-303 [» ]
2DBK NMR - A 229-303 [» ]
2EO3 NMR - A 1-104 [» ]
2LQN NMR - A 1-303 [» ]
2LQW NMR - A 1-303 [» ]
ProteinModelPortali P46109.
SMRi P46109. Positions 1-303.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107789. 66 interactions.
DIPi DIP-29165N.
IntActi P46109. 55 interactions.
MINTi MINT-137265.
STRINGi 9606.ENSP00000346300.

PTM databases

PhosphoSitei P46109.

Polymorphism databases

DMDMi 1169094.

2D gel databases

OGPi P46109.

Proteomic databases

MaxQBi P46109.
PaxDbi P46109.
PeptideAtlasi P46109.
PRIDEi P46109.

Protocols and materials databases

DNASUi 1399.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354336 ; ENSP00000346300 ; ENSG00000099942 .
ENST00000411769 ; ENSP00000396646 ; ENSG00000099942 .
GeneIDi 1399.
KEGGi hsa:1399.
UCSCi uc002ztf.2. human.

Organism-specific databases

CTDi 1399.
GeneCardsi GC22P021272.
HGNCi HGNC:2363. CRKL.
HPAi HPA001100.
MIMi 602007. gene.
neXtProti NX_P46109.
Orphaneti 261330. Distal 22q11.2 microdeletion syndrome.
PharmGKBi PA26881.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292767.
HOGENOMi HOG000236288.
HOVERGENi HBG105616.
InParanoidi P46109.
KOi K04438.
OMAi RTLYDFT.
OrthoDBi EOG7NW69P.
PhylomeDBi P46109.
TreeFami TF321436.

Enzyme and pathway databases

Reactomei REACT_12076. Frs2-mediated activation.
REACT_17025. Downstream signal transduction.
REACT_23787. Regulation of signaling by CBL.
SignaLinki P46109.

Miscellaneous databases

ChiTaRSi CRKL. human.
EvolutionaryTracei P46109.
GeneWikii CRKL.
GenomeRNAii 1399.
NextBioi 5727.
PROi P46109.
SOURCEi Search...

Gene expression databases

Bgeei P46109.
CleanExi HS_CRKL.
Genevestigatori P46109.

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. "Isolation and chromosomal localization of CRKL, a human crk-like gene."
    ten Hoeve J., Morris C., Heisterkamp N., Groffen J.
    Oncogene 8:2469-2474(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Trachea.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  6. "Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction."
    Koval A.P., Karas M., Zick Y., LeRoith D.
    J. Biol. Chem. 273:14780-14787(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRS4.
  7. "Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation."
    Elly C., Witte S., Zhang Z., Rosnet O., Lipkowitz S., Altman A., Liu Y.-C.
    Oncogene 18:1147-1156(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBLB.
  8. "DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines."
    Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K., Tanaka S.
    Blood 100:3968-3974(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOCK2.
  9. "CrkL is recruited through its SH2 domain to the erythropoietin receptor and plays a role in Lyn-mediated receptor signaling."
    Arai A., Kanda E., Nosaka Y., Miyasaka N., Miura O.
    J. Biol. Chem. 276:33282-33290(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPOR.
  10. "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-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structures of the SH3 domain of human CRK-like protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (DEC-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 220-303.

Entry informationi

Entry nameiCRKL_HUMAN
AccessioniPrimary (citable) accession number: P46109
Secondary accession number(s): A8KA44, D3DX35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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