SENP6

Sentrin-specifična proteaza 6 jest enzim koji je kod ljudi kodiran genom SENP6.

SENP6
Identifikatori
Aliasi	SENP6
Vanjski ID-jevi	OMIM: 605003 MGI: 1922075 HomoloGene: 9196 GeneCards: SENP6
Lokacija gena (čovjek) Hrom. Hromosom 6 (čovjek) Bend 6q14.1 Početak 75,601,509 bp Kraj 75,718,281 bp
Lokacija gena (miš) Hrom. Hromosom 9 (miš) Bend 9|9 E1 Početak 80,066,903 bp Kraj 80,144,953 bp
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • GO:0070122 peptidase activity • cysteine-type peptidase activity • GO:0001948, GO:0016582 vezivanje za proteine • hydrolase activity • SUMO-specific endopeptidase activity Ćelijska komponenta • jedro • nukleoplazma • citosol • citoplazma Biološki proces • protein desumoylation • protein modification by small protein removal • regulation of spindle assembly • protein sumoylation • Proteoliza • regulation of kinetochore assembly Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	26054	215351
Ensembl	ENSG00000112701	ENSMUSG00000034252
UniProt	Q9GZR1	Q6P7W0
RefSeq (mRNK)	NM_001100409 NM_001304792 NM_015571	NM_146003 NM_001311110
RefSeq (bjelančevina)	NP_001093879 NP_001291721 NP_056386	NP_001298039 NP_666115
Lokacija (UCSC)	Chr 6: 75.6 – 75.72 Mb	Chr 9: 80.07 – 80.14 Mb
PubMed pretraga
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 1.112 aminokiselina, а molekulska težina 126.146 Da.

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MAAGKSGGSA		GEITFLEALA		RSESKRDGGF		KNNWSFDHEE		ESEGDTDKDG
TNLLSVDEDE		DSETSKGKKL		NRRSEIVANS		SGEFILKTYV		RRNKSESFKT
LKGNPIGLNM		LSNNKKLSEN		TQNTSLCSGT		VVHGRRFHHA		HAQIPVVKTA
AQSSLDRKER		KEYPPHVQKV		EINPVRLSRL		QGVERIMKKT		EESESQVEPE
IKRKVQQKRH		CSTYQPTPPL		SPASKKCLTH		LEDLQRNCRQ		AITLNESTGP
LLRTSIHQNS		GGQKSQNTGL		TTKKFYGNNV		EKVPIDIIVN		CDDSKHTYLQ
TNGKVILPGA		KIPKITNLKE		RKTSLSDLND		PIILSSDDDD		DNDRTNRRES
ISPQPADSAC		SSPAPSTGKV		EAALNENTCR		AERELRSIPE		DSELNTVTLP
RKARMKDQFG		NSIINTPLKR		RKVFSQEPPD		ALALSCQSSF		DSVILNCRSI
RVGTLFRLLI		EPVIFCLDFI		KIQLDEPDHD		PVEIILNTSD		LTKCEWCNVR
KLPVVFLQAI		PAVYQKLSIQ		LQMNKEDKVW		NDCKGVNKLT		NLEEQYIILI
FQNGLDPPAN		MVFESIINEI		GIKNNISNFF		AKIPFEEANG		RLVACTRTYE
ESIKGSCGQK		ENKIKTVSFE		SKIQLRSKQE		FQFFDEEEET		GENHTIFIGP
VEKLIVYPPP		PAKGGISVTN		EDLHCLNEGE		FLNDVIIDFY		LKYLVLEKLK
KEDADRIHIF		SSFFYKRLNQ		RERRNHETTN		LSIQQKRHGR		VKTWTRHVDI
FEKDFIFVPL		NEAAHWFLAV		VCFPGLEKPK		YEPNPHYHEN		AVIQKCSTVE
DSCISSSASE		MESCSQNSSA		KPVIKKMLNK		KHCIAVIDSN		PGQEESDPRY
KRNICSVKYS		VKKINHTASE		NEEFNKGEST		SQKVADRTKS		ENGLQNESLS
STHHTDGLSK		IRLNYSDESP		EAGKMLEDEL		VDFSEDQDNQ		DDSSDDGFLA
DDNCSSEIGQ		WHLKPTICKQ		PCILLMDSLR		GPSRSNVVKI		LREYLEVEWE
VKKGSKRSFS		KDVMKGSNPK		VPQQNNFSDC		GVYVLQYVES		FFENPILSFE
LPMNLANWFP		PPRMRTKREE		IRNIILKLQE		DQSKEKRKHK		DTYSTEAPLG
EGTEQYVNSI		SD

Funkcija

Molekule slični ubikvitinu (UBL), kao što je mali modifikator povezan s ubikvitinom 1 (SUMO1), strukturno su povezani s ubikvitinom i mogu se vezati za ciljanje proteina na sličan način kao i ubikvitin. Međutim, kovalentno vezivanje UBL-a ne dovodi do razgradnje modificiranih proteina. Modifikacija SUMO1 je uključena u ciljanje RANGAP1 na kompleks iedarnih pora, kao i u stabilizaciju I-kapa-B-alfa (NFKBIA; MIM 164008) od proteasomske razgradnje 26S. Poput ubikvitina, UBL se sintetiziraju kao proteini prekursori, s jedan ili više aminokiselina nakon C-terminalnog glicin-glicinskih ostataka zrelog UBL proteina. Stoga, prije njihove konjugacije na ciljane proteine, repne sekvence UBL prekursora treba ukloniti UBL-specifičnim proteazama, kao što je SENP6.

Dopunska literatura

• Mikolajczyk J, Drag M, Békés M, Cao JT, Ronai Z, Salvesen GS (septembar 2007). "Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs". The Journal of Biological Chemistry. 282 (36): 26217–24. doi:10.1074/jbc.M702444200. PMID 17591783.
• Drag M, Mikolajczyk J, Krishnakumar IM, Huang Z, Salvesen GS (januar 2008). "Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family". The Biochemical Journal. 409 (2): 461–9. doi:10.1042/BJ20070940. PMID 17916063. S2CID 12234952.
• Yeh ET, Gong L, Kamitani T (maj 2000). "Ubiquitin-like proteins: new wines in new bottles". Gene. 248 (1–2): 1–14. doi:10.1016/S0378-1119(00)00139-6. PMID 10806345.
• Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (oktobar 1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.
• Kim KI, Baek SH, Jeon YJ, Nishimori S, Suzuki T, Uchida S, Shimbara N, Saitoh H, Tanaka K, Chung CH (maj 2000). "A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs". The Journal of Biological Chemistry. 275 (19): 14102–6. doi:10.1074/jbc.275.19.14102. PMID 10799485.
• Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, Sarge KD (maj 2001). "Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor". The Journal of Biological Chemistry. 276 (21): 18513–8. doi:10.1074/jbc.M008066200. PMID 11278381.
• Tojo M, Matsuzaki K, Minami T, Honda Y, Yasuda H, Chiba T, Saya H, Fujii-Kuriyama Y, Nakao M (novembar 2002). "The aryl hydrocarbon receptor nuclear transporter is modulated by the SUMO-1 conjugation system". The Journal of Biological Chemistry. 277 (48): 46576–85. doi:10.1074/jbc.M205987200. PMID 12354770.
• Bailey D, O'Hare P (januar 2004). "Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1". The Journal of Biological Chemistry. 279 (1): 692–703. doi:10.1074/jbc.M306195200. PMID 14563852.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (august 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Choi SJ, Chung SS, Rho EJ, Lee HW, Lee MH, Choi HS, Seol JH, Baek SH, Bang OS, Chung CH (oktobar 2006). "Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1". The Journal of Biological Chemistry. 281 (41): 30669–77. doi:10.1074/jbc.M604033200. PMID 16912044.
• Mukhopadhyay D, Ayaydin F, Kolli N, Tan SH, Anan T, Kametaka A, Azuma Y, Wilkinson KD, Dasso M (septembar 2006). "SUSP1 antagonizes formation of highly SUMO2/3-conjugated species" (PDF). The Journal of Cell Biology. 174 (7): 939–49. doi:10.1083/jcb.200510103. PMC 2064386. PMID 17000875.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (novembar 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.