Reviewed, UniProtKB/Swiss-Prot P46109 (CRKL_HUMAN)

Names and origin

Protein names

Recommended name:
    Crk-like protein

Gene names

Name:

CRKL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May mediate the transduction of intracellular signals.
Subunit structure	Interacts with INPP5D/SHIP1. Interacts with DOCK2 and EPOR. Interacts with phosphorylated CBLB and IRS4.
Sequence similarities	Contains 1 SH2 domain. Contains 2 SH3 domains.

Ontologies

Keywords
Domain	Repeat SH2 domain SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	JNK cascade Traceable author statement. Source: ProtInc Ras protein signal transduction Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular function	SH3/SH2 adaptor activity Traceable author statement. Source: ProtInc protein tyrosine kinase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Arms	Q9EQG6	1	EBI-910,EBI-976654	From a different organism.
MAP4K1	Q92918	3	EBI-910,EBI-881
MAP4K5	Q9Y4K4	1	EBI-910,EBI-1279

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 303

303

Crk-like protein

PRO_0000079347

Regions

Domain

14 – 102

89

SH2

Domain

123 – 183

61

SH3 1

Domain

235 – 296

62

SH3 2

Amino acid modifications

Modified residue

107

1

Phosphoserine By similarity

Modified residue

132

1

Phosphotyrosine By similarity

Modified residue

207

1

Phosphotyrosine

Modified residue

251

1

Phosphotyrosine

Secondary structure

1

.

.

.

.

.

.

.

.

.

303

Helix Strand Turn

Details...

Beta strand

240 – 242

3

Beta strand

271 – 276

6

Beta strand

285 – 287

3

Helix

288 – 290

3

Beta strand

291 – 293

3

Sequences

	Sequence		Length	Mass (Da)
	P46109-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 294CF1EE2CD44B81	FASTA	303	33,777
	10 20 30 40 50 60 MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL SVSENSRVSH 70 80 90 100 110 120 YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPM GSVSAPNLPT 130 140 150 160 170 180 AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK 190 200 210 220 230 240 LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA 250 260 270 280 290 300 KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD ENE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8361759] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Spleen.
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[4]	"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: 9614078] [Abstract] Cited for: INTERACTION WITH IRS4.
[5]	"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: 10022120] [Abstract] Cited for: INTERACTION WITH CBLB.
[6]	"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: 12393632] [Abstract] Cited for: INTERACTION WITH DOCK2.
[7]	"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: 11443118] [Abstract] Cited for: INTERACTION WITH EPOR.
[8]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207 AND TYR-251, MASS SPECTROMETRY.
[9]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X59656 mRNA. Translation: CAA42199.1.
CR456423 mRNA. Translation: CAG30309.1.
BC043500 mRNA. Translation: AAH43500.1.

PIR

S41754.

RefSeq

NP_005198.1.

UniGene

Hs.592205

3D structure databases

PDBMSD

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	220-303	[»]
2EO3	NMR	-	A	1-104	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:29165N.

IntAct

P46109.

PTM databases

PhosphoSite

P46109.

2-D gel databases

OGP

P46109.

Proteomic databases

PeptideAtlas

P46109.

Genome annotation databases

Ensembl

ENSG00000099942. Homo sapiens. [Contig view]

GeneID

1399.

KEGG

hsa:1399.

Organism-specific databases

H-InvDB

HIX0016264.

HGNC

HGNC:2363. CRKL.

HPA

HPA001100.

MIM

602007. gene.

PharmGKB

PA26881.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P46109.

HOVERGEN

P46109.

Gene expression databases

ArrayExpress

P46109.

CleanEx

HS_CRKL.

GermOnline

ENSG00000099942. Homo sapiens.

Family and domain databases

InterPro

IPR000980. SH2.
IPR001452. SH3.
IPR011511. SH3_2.
[Graphical view]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

Pfam

PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.

ProDom

PD000093. SH2. 1 hit.
PD000066. SH3. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]

PROSITE

PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P46109.

NextBio

5727.

SOURCE

Search...

Entry information

Entry name

CRKL_HUMAN

Accession

Primary (citable) accession number: P46109

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 4, 2008
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)