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 Id | Q17R13 |
Milk Fraction | whey |
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. |