RING finger protein 145 (EC 2.3.2.27)
1_MAAKE 6_ KLEAV 11_ LNVAL 16_ RVPSI 21_ MLLDV 26_ LYRWD 31_ VSSFF 36_ QQIQR 41_ SSLSN 46_ NPLFQ 51_ YKYLA 56_ LNMHY 61_ VGYIL 66_ SVVLL 71_ TLPRQ 76_ HLVQL 81_ YLYFL 86_ TALLL 91_ YAGHQ 96_ ISRDY 101_ VRSEL 106_ EFAYE 111_ GPMYL 116_ EPLSM 121_ NRFTT 126_ ALIGQ 131_ LVVCT 136_ LCSCV 141_ MKTKQ 146_ IWLFS 151_ AHMLP 156_ LLARL 161_ CLVPL 166_ ETIVI 171_ INKFA 176_ MIFTG 181_ LEVLY 186_ FLGSN 191_ LLVPY 196_ NLAKS 201_ AYREL 206_ VQVVE 211_ VYGLL 216_ ALGMS 221_ LWNQL 226_ VVPVL 231_ FMVFW 236_ LVLFA 241_ LQIYS 246_ YFSTR 251_ DQPAS 256_ RERLL 261_ FLFLT 266_ SIAEC 271_ CSTPY 276_ SLLGL 281_ VFTVS 286_ FVALG 291_ VLTLC 296_ KFYLQ 301_ GYRAF 306_ MNDPA 311_ MNRGM 316_ TEGVT 321_ LLILA 326_ VQTGL 331_ IELQV 336_ VHRAF 341_ LLSII 346_ LFIVV 351_ ASILQ 356_ SMLEI 361_ ADPIV 366_ LALGA 371_ SRDKS 376_ LWKHF 381_ RAVSL 386_ CLFLL 391_ VFPAY 396_ MAYMI 401_ CQFFH 406_ MDFWL 411_ LIIIS 416_ SSILT 421_ SLQVL 426_ GTLFI 431_ YVLFM 436_ VEEFR 441_ KEPVE 446_ NMDDV 451_ IYYVN 456_ GTYRL 461_ LEFLV 466_ ALCVV 471_ AYGVS 476_ ETIFG 481_ EWTVM 486_ GSMII 491_ FIHSY 496_ YNVWL 501_ RAQLG 506_ WKSFL 511_ LRRDA 516_ VNKIK 521_ SLPIA 526_ TKEQL 531_ EKHND 536_ ICAIC 541_ YQDMK 546_ SAVIT 551_ PCSHF 556_ FHAGC 561_ LKKWL 566_ YVQET 571_ CPLCH 576_ CHLKN 581_ SSQLP 586_ GLGTE 591_ PVLQP 596_ HAGAE 601_ QNVMF 606_ QEGTE 611_ PPGQE 616_ HTPGT 621_ RIQEG 626_ SRDNN 631_ EYIAR 636_ RPDNQ 641_ EGAFD 646_ PKEYP 651_ HSAKD 656_EAHPV
1: E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. In response to bacterial infection, negatively regulates the phagocyte oxidative burst by controlling the turnover of the NADPH oxidase complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-linked polyubiquitination and degradation of CYBB NADPH oxidase catalytic subunits, both essential for the generation of antimicrobial reactive oxygen species. Involved in the maintenance of cholesterol homeostasis. In response to high sterol concentrations ubiquitinates HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets it for degradation. The interaction with INSIG1 is required for this function. In addition, triggers ubiquitination of SCAP, likely inhibiting its transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2, ultimately down-regulating cholesterol biosynthesis