NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0092-8674(85)80052-0; PubMed=2988784 [NCBI, ExPASy, EBI, Israel, Japan]
Nilsen T.W., Maroney P.A., Goodwin R.G., Rottman F.M., Crittenden L.B., Raines M.A., Kung H.-J.;
"c-erbB activation in ALV-induced erythroblastosis: novel RNA processing and promoter insertion result in expression of an amino-truncated EGF receptor.";
Cell 41:719-726(1985).

Comments

CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
MISCELLANEOUS: This protein is produced by erythroleukemia cells in chickens which have been injected with the avian leukosis virus and subsequently develop leukemia. The leukemias are induced by the insertion of retroviral promoter elements in or near the c-erbB gene, which leads to c-erbB activation.
MISCELLANEOUS: This protein is synthesized as a Gag-Env-ErbB protein.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M10066; AAA48763.1; ALT_INIT; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B00643; TVFVLV.

3D structure databases

HSSP

Q9H2C9; 1M17. [HSSP ENTRY / PDB]

SMR

P00534; 116-426.

ModBase

P00534.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004714;	Molecular function: transmembrane receptor protein tyrosine kinase activity (inferred from electronic annotation from EC).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.

Pfam

PF07714; Pkinase_Tyr; 1.
Pfam graphical view of domain structure.

PRINTS

PR00109; TYRKINASE.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00219; TyrKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P00534.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Kinase; Nucleotide-binding; Oncogene; Phosphoprotein; Transferase; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 634`	`634`	`Tyrosine-protein kinase transforming protein erbB.`	`PRO_0000160251`
`DOMAIN`	`132 399`	`268`	`Protein kinase.`
`NP_BIND`	`138 146`	`9`	`ATP (By similarity).`
`ACT_SITE`	`257 257`		`Proton acceptor (By similarity).`
`BINDING`	`165 165`		`ATP (By similarity).`

Sequence information

Length: 634 AA [This is the length of the unprocessed precursor]

Molecular weight: 70891 Da [This is the MW of the unprocessed precursor]

CRC64: E705E33A0BE01FCC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKCAHFIDGP HCVKACPAGV LGENDTLVWK YADANAVCQL CHPNCTRGCK GPGLEGCPNG 

        70         80         90        100        110        120 
SKTPSIAAGV VGGLLCLVVV GLGIGLYLRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN 

       130        140        150        160        170        180 
QAHLRILKET EFKKVKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL 

       190        200        210        220        230        240 
DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPYGCLLD YIREHKDNIG SQYLLNWCVQ 

       250        260        270        280        290        300 
IAKGMNYLEE RRLVHRDLAA RNVLVKTPQH VKITDFGLAK LLGADEKEYH AEGGKVPIKW 

       310        320        330        340        350        360 
MALESILHRI YTHQSDVWSY GVTVWELMTF GSKPYDGIPA SEISSVLEKG ERLPQPPICT 

       370        380        390        400        410        420 
IDVYMIMVKC WMIDADSRPK FRELIAEFSK MARDPPRYLV IQGDERMHLP SPTDSKFYRT 

       430        440        450        460        470        480 
LMEEEDMEDI VDADEYLVPH QGFFNSPSTS RTPLLSSLSA TSNNSATNCI DRNGQGHPVR 

       490        500        510        520        530        540 
EDSFVQRYSS DPTGNFLEES IDDGFLPAPE YVNQLMPKKP STAMVQNQIY NNISLTAISK 

       550        560        570        580        590        600 
LPMDSRYQNS HSTAVDNPEY LNTNQSPLAK TVFESSPYWI QSGNHQINLD NPDYQQDFLP 

       610        620        630 
NETKPNGLLK VPAAENPEYL RVAAPKSEYI EASA

P00534 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools