Search by BoMiProt ID - Bomi3631


Primary Information

BoMiProt ID Bomi3631
Protein Name Activated CDC42 kinase 1/ACK-1/Activated CDC42 kinase 2/Tyrosine kinase non-receptor protein 2
Organism Bos taurus
Uniprot IdQ17R13
Milk Fractionwhey
Ref Sequence Id NP_776310.2
Aminoacid Length 1039
Molecular Weight 114868
Fasta Sequence https://www.uniprot.org/uniprot/Q17R13.fasta
Gene Name TNK2/ACK1/ACK2
Gene Id 280710
Protein Existence Status Reviewed

Secondary Information

Protein Function Involved in ell spreading and migration, cell survival, cell growth and proliferation.It binds Cdc42Hs in its GTP-bound form and inhibits both the intrinsic and GTPase-activating protein (GAP)-stimulated GTPase activity of Cdc42Hs.
Biochemical Properties contains (from N to C terminus) the kinase catalytic domain, SH3 domain, and Cdc42-binding Cdc42/Rac interactive binding (CRIB) domain followed by a proline rich domain.binding is mediated by a unique sequence of 47 amino acids C-terminal to an SH3 domain.Catalyses the following reaction- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
PTMs Phosphorylation,Ubl conjugation
Significance of PTMs autophosphorylation on Tyr284 enhances kinase activity.ACK1 interacts most strongly with the SH3 domains of Src family kinases (Src or Hck) via its C-terminal proline-rich domain.
Linking IDs Bomi3631
Bibliography Yokoyama N, Miller WT. Biochemical properties of the Cdc42-associated tyrosine kinase ACK1. Substrate specificity, authphosphorylation, and interaction with Hck. J Biol Chem. 2003 Nov 28;278(48):47713-23. doi: 10.1074/jbc.M306716200. Epub 2003 Sep 22. PMID: 14506255.
Protein Function Involved in ell spreading and migration, cell survival, cell growth and proliferation.It binds Cdc42Hs in its GTP-bound form and inhibits both the intrinsic and GTPase-activating protein (GAP)-stimulated GTPase activity of Cdc42Hs.
Biochemical Properties contains (from N to C terminus) the kinase catalytic domain, SH3 domain, and Cdc42-binding Cdc42/Rac interactive binding (CRIB) domain followed by a proline rich domain.binding is mediated by a unique sequence of 47 amino acids C-terminal to an SH3 domain.Catalyses the following reaction- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
PTMs Phosphorylation,Ubl conjugation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q17R13|ACK1_BOVIN Activated CDC42 kinase 1 OS=Bos taurus OX=9913 GN=TNK2 PE=1 SV=1 MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLW EAVKRRKAMCKRKSWMSKVFSGKRLEAEFPPHHSQSTFRKTSPTPGGSAGEGSLQSLTCL IGEKDLHLFEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIREVNA MHSLDHRNLIRLYGVVLTPPMKTVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGM GYLEAKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHY*284VMQEHRKVPFAWCAPE SLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDI YNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRA ENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPD KIDELYLGNPMDPPDLLSVELSTSRPTQHLGRVKKPTY*518DPVSEDQDPLSSDFKRLGLRKP GLPRGLWLAKPSARVPGTKAGRGGGEVTLIDFGEEPVVPAPRPCAPSLAQLAMDACSLLD KTPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEVCSINSTLVGAGVSA EPSQGETNYAFVPEPARLLPPLEDNLFLPPQSGGKPPNSAQTAEIFQALQQECMRQLQVP PGS*723LVPSPSPGGDDKPQVPPRVPIPPRPTRSRGELSPVPPGEEEMGRWPGPASPPRVPPR EPLSPQGSRTPSPLVPPGSSPLPPRLSSSPGKTMPTTQSFASDPKY*826ATPQVIQAPGPRAG PCILPIVRDGKKVSSTHY*858YLLPERPPYLERY*871QRFLHEAQS*880PRGPDPTPIPLLLPPPSTPA PAAPTATVRPMPQAAPDPKANFSSNNSNPGARPSSLRATARLPQRGYPGDGPEAGRPADK IQMLQAMVHGVTTEECQAALQSHSWSVQRAAQYLKVEQLFGLGLRPRGECHNVLEMFDWN LEQAGCHLLGSCGPAHHKR
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs autophosphorylation on Tyr284 enhances kinase activity.ACK1 interacts most strongly with the SH3 domains of Src family kinases (Src or Hck) via its C-terminal proline-rich domain.
Linking IDs
Bibliography Yokoyama N, Miller WT. Biochemical properties of the Cdc42-associated tyrosine kinase ACK1. Substrate specificity, authphosphorylation, and interaction with Hck. J Biol Chem. 2003 Nov 28;278(48):47713-23. doi: 10.1074/jbc.M306716200. Epub 2003 Sep 22. PMID: 14506255.