Difference between revisions of "Ubiquitin-like modifier-activating enzyme 1"

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{{#invoke:InfoboxforTarget|run|Uba1, Ube1|[https://www.uniprot.org/uniprot/Q09472 Q09472]|Rattus norvegicus|Cys179, Cys234|[http://pfam.xfam.org/family/PF00899 ThiF family],<br/>[http://pfam.xfam.org/family/PF16190 Ubiquitin-activating enzyme E1 FCCH domain],<br/>Ubiquitin-activating E1 family|[[:Category:Ubiquitin-like modifier-activating enzyme 1|Ligand list]]|Ubiquitinase/Deubiquitinase,<br/>Post-translational Modification}}
  
 
==Summary==
 
==Summary==

Revision as of 02:27, 8 August 2019

Basic Information
Short Name Uba1, Ube1
UNP ID Q09472
Organism Rattus norvegicus
Cys Site Cys179, Cys234
Family/Domain ThiF family,
Ubiquitin-activating enzyme E1 FCCH domain,
Ubiquitin-activating E1 family
Known Ligand Ligand list
Function Type Ubiquitinase/Deubiquitinase,
Post-translational Modification

Summary

Protein Function

UBA1 participates in ubiquitination and the NEDD8 pathway for protein folding and degradation, among many other biological processes.
This protein encoded by this gene catalyzes the first step in ubiquitin conjugation, or ubiquitination, to mark cellular proteins for degradation. Specifically, UBA1 catalyzes the ATP-dependent adenylation of ubiquitin, thereby forming a thioester bond between the two. It also continues to participate in subsequent steps of ubiquination as a Ub carrier. (From Wikipedia)
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.

Cys Function & Property

Cys179 is close to the cofactor Acetyl-CoA binding site in space.

  • Hydrophobic property:
539-hydro.png
  • SASA：
Cys179: Unknown
Cys234: Unknown

Protein Sequence

MSSSPLSKKR RVSGPDPKPG SNCSSAQSVL SEVSSVPTNG MAKNGSEADI
DESLYSRQLY VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT
LHDQGTTQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVTAYTGP
LVEDFLSGFQ VVVLTNSPLE EQLRVGEFCH SRGIKLVVAD TRGLFGQLFC
DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFETGDFVSF
SEVQGMVQLN GCQPIEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
ISFKSLPASL AEPDFVMTDF AKYSRPAQLH IGFQALHQFC AQHNRPPRPR
NEEDATELVT LAQAVNARSP PAVQQDNVDE DLIRKLAYVA AGDLAPINAF
IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEALT EDKCLPRQNR
YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEV
VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PYIQVTSHQN
RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD
EFEGLFKQPA ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP
QTWGDCVTWA CHHWHTQYCN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH
PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG SQDRAAVASL LQSVQVPEFT
PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP GFKMYPIDFE
KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA
VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ
EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF
FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV
PYVRYTIR

Structural Information

  • Known structures with covalent ligands:
Unknown
  • Protein structure:
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Related Pathway

Experimental Evidence

LC/MS/MS, Tryptic Digest, Elastase Digest, Subtilysin Digest

Reference

  1. Viquez O M, Caito S W, McDonald W H, et al. Electrophilic adduction of ubiquitin activating enzyme E1 by N, N-diethyldithiocarbamate inhibits ubiquitin activation and is accompanied by striatal injury in the rat[J]. Chemical research in toxicology, 2012, 25(11): 2310-2321. 22874009
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