Serine/threonine-protein kinase PAK 5 (EC 2.7.11.1) (p21-activated kinase 5) (PAK-5) (p21-activated kinase 7) (PAK-7)
1_MFGKK 6_ KKKIE 11_ ISGPS 16_ NFEHR 21_ VHTGF 26_ DPQEQ 31_ KFTGL 36_ PQQWH 41_ SLLAD 46_ TANRP 51_ KPMVD 56_ PSCIT 61_ PIQLA 66_ PMKTI 71_ VRGNK 76_ PCKET 81_ SINGL 86_ LEDFD 91_ NISVT 96_ RSNSL 101_ RKESP 106_ PTPDQ 111_ GASSH 116_ GPGHA 121_ EENGF 126_ ITFSQ 131_ YSSES 136_ DTTAD 141_ YTTEK 146_ YREKS 151_ LYGDD 156_ LDPYY 161_ RGSHA 166_ AKQNG 171_ HVMKM 176_ KHGEA 181_ YYSEV 186_ KPLKS 191_ DFARF 196_ SADYH 201_ SHLDS 206_ LSKPS 211_ EYSDL 216_ KWEYQ 221_ RASSS 226_ SPLDY 231_ SFQFT 236_ PSRTA 241_ GTSGC 246_ SKESL 251_ AYSES 256_ EWGPS 261_ LDDYD 266_ RRPKS 271_ SYLNQ 276_ TSPQP 281_ TMRQR 286_ SRSGS 291_ GLQEP 296_ MMPFG 301_ ASAFK 306_ THPQG 311_ HSYNS 316_ YTYPR 321_ LSEPT 326_ MCIPK 331_ VDYDR 336_ AQMVL 341_ SPPLS 346_ GSDTY 351_ PRGPA 356_ KLPQS 361_ QSKSG 366_ YSSSS 371_ HQYPS 376_ GYHKA 381_ TLYHH 386_ PSLQS 391_ SSQYI 396_ STASY 401_ LSSLS 406_ LSSST 411_ YPPPS 416_ WGSSS 421_ DQQPS 426_ RVSHE 431_ QFRAA 436_ LQLVV 441_ SPGDP 446_ REYLA 451_ NFIKI 456_ GEGST 461_ GIVCI 466_ ATEKH 471_ TGKQV 476_ AVKKM 481_ DLRKQ 486_ QRREL 491_ LFNEV 496_ VIMRD 501_ YHHDN 506_ VVDMY 511_ SSYLV 516_ GDELW 521_ VVMEF 526_ LEGGA 531_ LTDIV 536_ THTRM 541_ NEEQI 546_ ATVCL 551_ SVLRA 556_ LSYLH 561_ NQGVI 566_ HRDIK 571_ SDSIL 576_ LTSDG 581_ RIKLS 586_ DFGFC 591_ AQVSK 596_ EVPKR 601_ KSLVG 606_ TPYWM 611_ APEVI 616_ SRLPY 621_ GTEVD 626_ IWSLG 631_ IMVIE 636_ MIDGE 641_ PPYFN 646_ EPPLQ 651_ AMRRI 656_ RDSLP 661_ PRVKD 666_ LHKVS 671_ SVLRG 676_ FLDLM 681_ LVREP 686_ SQRAT 691_ AQELL 696_ GHPFL 701_ KLAGP 706_ PSCIV 711_PLMRQ
1: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions