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Protein

E3 SUMO-protein ligase K-bZIP

Gene

K8

Organism
Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in viral gene regulation and seems to be essential for KSHV reactivation. Disrupts host G1 cell cycle control thus allowing viral transcription and translation to proceed at the early stages of infection. Catalyzes its own SUMO modification as well as that of its interacting partners such as host TP53 AND RB1.3 Publications

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

G1/S host cell cycle checkpoint dysregulation by virus, Host-virus interaction, Modulation of host cell cycle by virus, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase K-bZIP (EC:6.3.2.-)
Gene namesi
Name:K8
OrganismiHuman herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Taxonomic identifieri868565 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeRhadinovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000000942 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286E3 SUMO-protein ligase K-bZIPPRO_0000423846Add
BLAST

Post-translational modificationi

Sumoylated.

Keywords - PTMi

Ubl conjugation

Interactioni

Subunit structurei

Interacts with host HDAC1 and HDAC2, these interactions suppress HDAC activities. Interacts with protein ORF57.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC2Q927697EBI-9006943,EBI-301821From a different organism.
ORF57Q2HR755EBI-9006943,EBI-6884751

Protein-protein interaction databases

BioGridi1776965. 3 interactions.
IntActiQ2HR82. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ2HR82.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

InterProiIPR010805. KSHV_K8.
[Graphical view]
PfamiPF07188. KSHV_K8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2HR82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRMKDIPTK SSPGTDNSEK DEAVIEEDLS LNGQPFFTDN TDGGENEVSW
60 70 80 90 100
TSSLLSTYVG CQPPAIPVCE TVIDLTAPSQ SGAPGDEHLP CSLNAETKFH
110 120 130 140 150
IPDPSWTLSH TPPRGPHISQ QLPTRRSKRR LHRKFEEERL CTKAKQGAGR
160 170 180 190 200
PVPASVVKVG NITPHYGEEL TRGDAVPAAP ITPPYPRVQR PAQPTHVLFS
210 220 230 240 250
PVFVSLKAEV CDQSHSPTRK QGRYGRVSSK AYTRQLQQAL EEKDAQLCFL
260 270 280
AARLEAHKEQ IIFLRDMLMR MCQQPASPTD APLPPC
Length:286
Mass (Da):31,574
Last modified:March 21, 2006 - v1
Checksum:i69FE9D78A4BB4FEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148805 Genomic DNA. Translation: ABD28901.1.
RefSeqiYP_001129403.1. NC_009333.1.

Genome annotation databases

GeneIDi4961462.
KEGGivg:4961462.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148805 Genomic DNA. Translation: ABD28901.1.
RefSeqiYP_001129403.1. NC_009333.1.

3D structure databases

ProteinModelPortaliQ2HR82.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1776965. 3 interactions.
IntActiQ2HR82. 6 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4961462.
KEGGivg:4961462.

Enzyme and pathway databases

UniPathwayiUPA00886.

Family and domain databases

InterProiIPR010805. KSHV_K8.
[Graphical view]
PfamiPF07188. KSHV_K8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a spliced gene from Kaposi's sarcoma-associated herpesvirus encoding a protein with similarities to latent membrane proteins 1 and 2A of Epstein-Barr virus."
    Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.
    J. Virol. 73:6953-6963(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview."
    Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.
    J. Gen. Virol. 87:1781-1804(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Lytic replication-associated protein (RAP) encoded by Kaposi sarcoma-associated herpesvirus causes p21CIP-1-mediated G1 cell cycle arrest through CCAAT/enhancer-binding protein-alpha."
    Wu F.Y., Tang Q.Q., Chen H., ApRhys C., Farrell C., Chen J., Fujimuro M., Lane M.D., Hayward G.S.
    Proc. Natl. Acad. Sci. U.S.A. 99:10683-10688(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL CYCLE ARREST.
  4. "Binding of Kaposi's sarcoma-associated herpesvirus K-bZIP to interferon-responsive factor 3 elements modulates antiviral gene expression."
    Lefort S., Soucy-Faulkner A., Grandvaux N., Flamand L.
    J. Virol. 81:10950-10960(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific."
    Chang P.C., Izumiya Y., Wu C.Y., Fitzgerald L.D., Campbell M., Ellison T.J., Lam K.S., Luciw P.A., Kung H.J.
    J. Biol. Chem. 285:5266-5273(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS SUMO E3 LIGASE.
  6. "Leucine zipper domain is required for Kaposi sarcoma-associated herpesvirus (KSHV) K-bZIP protein to interact with histone deacetylase and is important for KSHV replication."
    Martinez F.P., Tang Q.
    J. Biol. Chem. 287:15622-15634(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST HDAC1 AND HDAC2.
  7. "Chromatin immunoprecipitation and microarray analysis suggest functional cooperation between Kaposi's Sarcoma-associated herpesvirus ORF57 and K-bZIP."
    Hunter O.V., Sei E., Richardson R.B., Conrad N.K.
    J. Virol. 87:4005-4016(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PROTEIN ORF57.

Entry informationi

Entry nameiKBZIP_HHV8P
AccessioniPrimary (citable) accession number: Q2HR82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: March 21, 2006
Last modified: October 14, 2015
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.