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Protein

Nuclear egress protein 1

Gene

NEC1

Organism
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.UniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri106 – 211CCCH-typeUniRule annotationAdd BLAST106

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear egress protein 1UniRule annotation
Gene namesi
Name:NEC1UniRule annotation
Ordered Locus Names:UL53
OrganismiHuman cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Taxonomic identifieri10360 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinaeCytomegalovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008992 Componenti: Genome
  • UP000008991 Componenti: Genome

Subcellular locationi

  • Host nucleus inner membrane UniRule annotation1 Publication

  • Note: Remains attached to the nucleus inner membrane through interaction with NEC2.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Host nucleus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001160131 – 376Nuclear egress protein 1Add BLAST376

Post-translational modificationi

Phosphorylated at serine residues in the N-terminus. This phosphorylation regulates the localization within the inner nuclear membrane.UniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP16794.

Interactioni

Subunit structurei

Forms a heterohexameric complex with NEC2. Interacts with capsid vertex specific component 2/CVC2; this interaction directs the capsid to the host inner nuclear membrane to initiate budding.UniRule annotation

Structurei

Secondary structure

1376
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi61 – 63Combined sources3
Helixi65 – 70Combined sources6
Helixi73 – 81Combined sources9
Beta strandi89 – 91Combined sources3
Beta strandi94 – 97Combined sources4
Helixi98 – 100Combined sources3
Beta strandi105 – 110Combined sources6
Beta strandi113 – 118Combined sources6
Turni119 – 121Combined sources3
Helixi134 – 142Combined sources9
Helixi144 – 146Combined sources3
Turni148 – 151Combined sources4
Helixi152 – 156Combined sources5
Turni157 – 160Combined sources4
Helixi162 – 168Combined sources7
Helixi172 – 184Combined sources13
Beta strandi186 – 195Combined sources10
Beta strandi198 – 208Combined sources11
Beta strandi210 – 212Combined sources3
Helixi214 – 224Combined sources11
Turni225 – 227Combined sources3
Beta strandi228 – 235Combined sources8
Beta strandi238 – 246Combined sources9
Helixi257 – 266Combined sources10
Helixi271 – 279Combined sources9
Helixi281 – 288Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DOBX-ray2.47A61-289[»]
5DOCX-ray1.94A/B88-290[»]
5DOEX-ray3.00B72-290[»]
ProteinModelPortaliP16794.
SMRiP16794.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the herpesviridae NEC1 protein family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri106 – 211CCCH-typeUniRule annotationAdd BLAST106

Keywords - Domaini

Zinc-finger

Family and domain databases

HAMAPiMF_04023. HSV_NEC1. 1 hit.
InterProiIPR021152. Herpes_UL31.
[Graphical view]
PfamiPF02718. Herpes_UL31. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16794-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVSGVRTP RERRSALRSL LRKRRQRELA SKVASTVNGA TSANNHGEPP
60 70 80 90 100
SPADARPRLT LHDLHDIFRE HPELELKYLN MMKMAITGKE SICLPFNFHS
110 120 130 140 150
HRQHTCLDIS PYGNEQVSRI ACTSCEDNRI LPTASDAMVA FINQTSNIMK
160 170 180 190 200
NRNFYYGFCK SSELLKLSTN QPPIFQIYYL LHAANHDIVP FMHAEDGRLH
210 220 230 240 250
MHVIFENPDV HIPCDCITQM LTAAREDYSV TLNIVRDHVV ISVLCHAVSA
260 270 280 290 300
SSVKIDVTIL QRKIDEMDIP NDVSESFERY KELIQELCQS SGNNLYEEAT
310 320 330 340 350
SSYAIRSPLT ASPLHVVSTN GCGPSSSSQS TPPHLHPPSQ ATQPHHYSHH
360 370
QSQSQQHHHR PQSPPPPLFL NSIRAP
Length:376
Mass (Da):42,313
Last modified:August 1, 1990 - v1
Checksum:iBF44D5F8DE2B88B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17209 Genomic DNA. Translation: AAA46007.1.
X17403 Genomic DNA. Translation: CAA35412.1.
BK000394 Genomic DNA. Translation: DAA00158.1.
PIRiS09816. QQBEW2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17209 Genomic DNA. Translation: AAA46007.1.
X17403 Genomic DNA. Translation: CAA35412.1.
BK000394 Genomic DNA. Translation: DAA00158.1.
PIRiS09816. QQBEW2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DOBX-ray2.47A61-289[»]
5DOCX-ray1.94A/B88-290[»]
5DOEX-ray3.00B72-290[»]
ProteinModelPortaliP16794.
SMRiP16794.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP16794.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

HAMAPiMF_04023. HSV_NEC1. 1 hit.
InterProiIPR021152. Herpes_UL31.
[Graphical view]
PfamiPF02718. Herpes_UL31. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNEC1_HCMVA
AccessioniPrimary (citable) accession number: P16794
Secondary accession number(s): Q7M6N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 52 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

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.