[1]	NUCLEOTIDE SEQUENCE [MRNA]. Schmidt U., Haubenwallner S., Beug H., Nimpf J.; "Btk expressed in primary chicken erythroblasts."; Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Plays a crucial role in B-cell ontogeny (By similarity).
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
ENZYME REGULATION: Activated by phosphorylation (By similarity).
SUBUNIT: Binds GTF2I through the PH domain. Interacts with SH3BP5 via the SH3 domain (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; Peripheral membrane protein (By similarity).
PTM: Autophosphorylated on Tyr-220 and Tyr-549. The tyrosine phosphorylation of Tyr-220 may create a docking site for a SH2 containing protein (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.
SIMILARITY: Contains 1 Btk-type zinc finger.
SIMILARITY: Contains 1 PH domain.
SIMILARITY: Contains 1 protein kinase domain.
SIMILARITY: Contains 1 SH2 domain.
SIMILARITY: Contains 1 SH3 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

AF535118; AAN04043.2; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Gga.1305

3D structure databases

SMR

Q8JH64; 2-169, 395-652.

ModBase

Q8JH64.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004715;	Molecular function: non-membrane spanning protein tyrosine kinase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001562; BTK.
IPR001849; PH.
IPR011993; PH_type.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
IPR001452; SH3.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 1.
G3DSA:3.30.505.10; SH2; 1.

Pfam

PF00779; BTK; 1.
PF00169; PH; 1.
PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00402; TECBTKDOMAIN.
PR00109; TYRKINASE.

ProDom

PD000001; Prot_kinase; 2.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00107; BTK; 1.
SM00233; PH; 1.
SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.

PROSITE

PS50003; PH_DOMAIN; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PS51113; ZF_BTK; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8JH64.

Genome annotation databases

Ensembl

ENSGALG00000004958; Gallus gallus. [Contig view]

Phylogenomic databases

HOVERGEN

Q8JH64; -.

Other

UniRef

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

Keywords

ATP-binding; Cytoplasm; Kinase; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 657`	`657`	`Tyrosine-protein kinase BTK.`	`PRO_0000088067`
`DOMAIN`	`3 132`	`130`	`PH.`
`DOMAIN`	`214 270`	`57`	`SH3.`
`DOMAIN`	`276 366`	`91`	`SH2.`
`DOMAIN`	`400 653`	`254`	`Protein kinase.`
`ZN_FING`	`134 170`	`37`	`Btk-type.`
`NP_BIND`	`406 414`	`9`	`ATP (By similarity).`
`ACT_SITE`	`519 519`		`Proton acceptor (By similarity).`
`METAL`	`142 142`		`Zinc (By similarity).`
`METAL`	`153 153`		`Zinc (By similarity).`
`METAL`	`154 154`		`Zinc (By similarity).`
`METAL`	`164 164`		`Zinc (By similarity).`
`BINDING`	`428 428`		`ATP (By similarity).`
`MOD_RES`	`220 220`		`Phosphotyrosine; by autocatalysis (By similarity).`
`MOD_RES`	`549 549`		`Phosphotyrosine; by autocatalysis (By similarity).`

Sequence information

Length: 657 AA [This is the length of the unprocessed precursor]

Molecular weight: 75879 Da [This is the MW of the unprocessed precursor]

CRC64: FE5217E8E6195F6A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASIILESIF LKRSQQKKKT SPLNFKKRLF LLTESKLSYY EYDFERGRRG SKKGSVDIEK 

        70         80         90        100        110        120 
ITCVETVVPE NNPPPERQVP KKGEDYNMEQ ISIIERFPYP FQVVYDEGPL YVFSPTEELR 

       130        140        150        160        170        180 
KRWIHQLKSV IRYNSDLVQK YHPCFWIDGQ YLCCSQTAKN AMGCKILESR NGSLKAGRSH 

       190        200        210        220        230        240 
RKTKKPLPPT PEEDTMVMKP LPPEPAPSAA GEMKKVVALY NYVPMNVQDL QLQKGEDYLI 

       250        260        270        280        290        300 
LEESHLPWWK ARDKNGREGY IPSNYVTATS NSLEIYEWYS KNITRSQAEQ LLKQEGKEGG 

       310        320        330        340        350        360 
FIVRDSTSKT GKYTVSVYAK SAVDPQGMIR HYVVCCTPQN QYYLAEKHLF NTIPELITYH 

       370        380        390        400        410        420 
QHNSAGLISR LKYPVSRHQK SAPSTAGLGY GSWEIDPKDL TFLKELGTGQ FGVVKYGKWR 

       430        440        450        460        470        480 
GQYNVAIKMI REGSMSEDEF IDEAKVMMNL SHEKLVQLYG VCTKQRPIFI ITEYMANGCL 

       490        500        510        520        530        540 
LNFLRETQRR FQPAELLEMC KDVCEAMEYL ESKQFLHRDL AARNCLVNDQ GIVKVSDFGL 

       550        560        570        580        590        600 
SRYVLDDEYT SSMGSKFPVR WSPPEVLLYS KFSSKSDVWS FGVLMWEVYS LGKMPYERFN 

       610        620        630        640        650 
NSETTEHVIQ GLRLYRPQQA SERVYAIMYS CWHEKAEERP TFSALLGSIV DITDEEP

Q8JH64 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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