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Protein

MORC family CW-type zinc finger protein 3

Gene

MORC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nuclear factor which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism (PubMed:20501696). Sumoylated MORC3-NBs can also associate with PML-NBs (PubMed:20501696). Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro (PubMed:11927593). May be required for influenza A transcription during viral infection (PubMed:26202233).4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri404 – 454CW-typePROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

GO - Biological processi

  • cell aging Source: MGI
  • maintenance of protein location in nucleus Source: MGI
  • negative regulation of fibroblast proliferation Source: MGI
  • peptidyl-serine phosphorylation Source: MGI
  • post-embryonic development Source: Ensembl
  • protein phosphorylation Source: MGI
  • protein stabilization Source: MGI
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000159256-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
MORC family CW-type zinc finger protein 3
Alternative name(s):
Nuclear matrix protein 21 Publication
Zinc finger CW-type coiled-coil domain protein 3
Gene namesi
Name:MORC3Imported
Synonyms:KIAA0136Imported, NXP2Imported, ZCWCC3Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:23572. MORC3.

Subcellular locationi

GO - Cellular componenti

  • nuclear matrix Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • PML body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi35E → A: Fails to localize to PML nuclear bodies and activate TP53. 1 Publication1
Mutagenesisi67D → N: Forms nuclear bodies, but rapidly diffuses throughout the nucleus under conditions of ATP depletion. 1 Publication1
Mutagenesisi101G → A: Diffuse nuclear localization. Fails to form nuclear bodies in the presence of ATP. 1 Publication1
Mutagenesisi419W → A: Diffuse nuclear localization, possibly due to loss of DNA or nucleosome binding. 1 Publication1
Mutagenesisi597K → R: Loss of sumoylation; when associated with R-650; R-651; R-740 and R-794. 1 Publication1
Mutagenesisi650K → R: Loss of sumoylation; when associated with R-597; R-651; R-740 and R-794. 1 Publication1
Mutagenesisi651K → R: Loss of sumoylation; when associated with R-597; R-650; R-740 and R-794. 1 Publication1
Mutagenesisi740K → R: Loss of sumoylation; when associated with R-597; R-650; R-651 and R-794. 1 Publication1
Mutagenesisi794K → R: Loss of sumoylation; when associated with R-597; R-650; R-651 and R-740. 1 Publication1

Organism-specific databases

DisGeNETi23515.
OpenTargetsiENSG00000159256.
PharmGKBiPA128394632.

Polymorphism and mutation databases

BioMutaiMORC3.
DMDMi108935853.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000965381 – 939MORC family CW-type zinc finger protein 3Add BLAST939

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei503PhosphoserineCombined sources1
Modified residuei514PhosphoserineCombined sources1
Modified residuei540PhosphoserineCombined sources1
Modified residuei560PhosphoserineCombined sources1
Cross-linki597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki650Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)4 Publications
Cross-linki650Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki651Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)2 Publications
Cross-linki651Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki740Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)2 Publications
Cross-linki740Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei765PhosphoserineCombined sources1
Cross-linki794Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication

Post-translational modificationi

Sumoylation is involved in interaction with PML and localization to PML nuclear bodies.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14149.
MaxQBiQ14149.
PaxDbiQ14149.
PeptideAtlasiQ14149.
PRIDEiQ14149.

PTM databases

iPTMnetiQ14149.
PhosphoSitePlusiQ14149.

Expressioni

Tissue specificityi

Expressed in heart, placenta, skeletal muscle, brain, pancreas, lung, liver, but not kidney.1 Publication

Gene expression databases

BgeeiENSG00000159256.
CleanExiHS_MORC3.
ExpressionAtlasiQ14149. baseline and differential.
GenevisibleiQ14149. HS.

Organism-specific databases

HPAiHPA018406.
HPA034848.

Interactioni

Subunit structurei

Homodimer (PubMed:17332504). The sumoylated form interacts with PML (via SUMO-interacting motif) (PubMed:20501696, PubMed:17332504). Interacts with PT53 (PubMed:17332504). Interacts with influenza A virus PA and PB1 polymerase subunits during infection (PubMed:26202233).3 Publications

Protein-protein interaction databases

BioGridi117062. 17 interactors.
IntActiQ14149. 15 interactors.
STRINGi9606.ENSP00000383333.

Structurei

Secondary structure

1939
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi408 – 412Combined sources5
Turni414 – 416Combined sources3
Beta strandi419 – 422Combined sources4
Helixi435 – 437Combined sources3
Helixi441 – 443Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QQ4X-ray1.75A/B400-460[»]
5SVXX-ray1.56A407-454[»]
5SVYX-ray1.05A407-455[»]
ProteinModelPortaliQ14149.
SMRiQ14149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni326 – 353Nuclear matrix binding1 PublicationAdd BLAST28
Regioni500 – 591RNA binding1 PublicationAdd BLAST92

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili686 – 877Sequence analysisAdd BLAST192

Sequence similaritiesi

Contains 1 CW-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri404 – 454CW-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1845. Eukaryota.
ENOG411033B. LUCA.
GeneTreeiENSGT00530000062983.
HOGENOMiHOG000246950.
HOVERGENiHBG055625.
InParanoidiQ14149.
OMAiYKRQCHM.
OrthoDBiEOG091G018P.
PhylomeDBiQ14149.
TreeFamiTF329118.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
InterProiIPR003594. HATPase_C.
IPR011124. Znf_CW.
[Graphical view]
PfamiPF07496. zf-CW. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 3 hits.
PROSITEiPS51050. ZF_CW. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14149-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQPPRGIR LSALCPKFLH TNSTSHTWPF SAVAELIDNA YDPDVNAKQI
60 70 80 90 100
WIDKTVINDH ICLTFTDNGN GMTSDKLHKM LSFGFSDKVT MNGHVPVGLY
110 120 130 140 150
GNGFKSGSMR LGKDAIVFTK NGESMSVGLL SQTYLEVIKA EHVVVPIVAF
160 170 180 190 200
NKHRQMINLA ESKASLAAIL EHSLFSTEQK LLAELDAIIG KKGTRIIIWN
210 220 230 240 250
LRSYKNATEF DFEKDKYDIR IPEDLDEITG KKGYKKQERM DQIAPESDYS
260 270 280 290 300
LRAYCSILYL KPRMQIILRG QKVKTQLVSK SLAYIERDVY RPKFLSKTVR
310 320 330 340 350
ITFGFNCRNK DHYGIMMYHR NRLIKAYEKV GCQLRANNMG VGVVGIIECN
360 370 380 390 400
FLKPTHNKQD FDYTNEYRLT ITALGEKLND YWNEMKVKKN TEYPLNLPVE
410 420 430 440 450
DIQKRPDQTW VQCDACLKWR KLPDGMDQLP EKWYCSNNPD PQFRNCEVPE
460 470 480 490 500
EPEDEDLVHP TYEKTYKKTN KEKFRIRQPE MIPRINAELL FRPTALSTPS
510 520 530 540 550
FSSPKESVPR RHLSEGTNSY ATRLLNNHQV PPQSEPESNS LKRRLSTRSS
560 570 580 590 600
ILNAKNRRLS SQFENSVYKG DDDDEDVIIL EENSTPKPAV DHDIDMKSEQ
610 620 630 640 650
SHVEQGGVQV EFVGDSEPCG QTGSTSTSSS RCDQGNTAAT QTEVPSLVVK
660 670 680 690 700
KEETVEDEID VRNDAVILPS CVEAEAKIHE TQETTDKSAD DAGCQLQELR
710 720 730 740 750
NQLLLVTEEK ENYKRQCHMF TDQIKVLQQR ILEMNDKYVK KETCHQSTET
760 770 780 790 800
DAVFLLESIN GKSESPDHMV SQYQQALEEI ERLKKQCSAL QHVKAECSQC
810 820 830 840 850
SNNESKSEMD EMAVQLDDVF RQLDKCSIER DQYKSEVELL EMEKSQIRSQ
860 870 880 890 900
CEELKTEVEQ LKSTNQQTAT DVSTSSNIEE SVNHMDGESL KLRSLRVNVG
910 920 930
QLLAMIVPDL DLQQVNYDVD VVDEILGQVV EQMSEISST
Length:939
Mass (Da):107,113
Last modified:June 13, 2006 - v3
Checksum:i7DF0EC31936BF5FF
GO

Sequence cautioni

The sequence BAA09485 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA89432 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50926 mRNA. Translation: BAA09485.2. Different initiation.
AK292957 mRNA. Translation: BAF85646.1.
AP000693, AP000692 Genomic DNA. Translation: BAA89432.1. Different initiation.
CCDSiCCDS42924.1.
RefSeqiNP_056173.1. NM_015358.2.
UniGeneiHs.421150.

Genome annotation databases

EnsembliENST00000400485; ENSP00000383333; ENSG00000159256.
GeneIDi23515.
KEGGihsa:23515.
UCSCiuc002yvi.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50926 mRNA. Translation: BAA09485.2. Different initiation.
AK292957 mRNA. Translation: BAF85646.1.
AP000693, AP000692 Genomic DNA. Translation: BAA89432.1. Different initiation.
CCDSiCCDS42924.1.
RefSeqiNP_056173.1. NM_015358.2.
UniGeneiHs.421150.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QQ4X-ray1.75A/B400-460[»]
5SVXX-ray1.56A407-454[»]
5SVYX-ray1.05A407-455[»]
ProteinModelPortaliQ14149.
SMRiQ14149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117062. 17 interactors.
IntActiQ14149. 15 interactors.
STRINGi9606.ENSP00000383333.

PTM databases

iPTMnetiQ14149.
PhosphoSitePlusiQ14149.

Polymorphism and mutation databases

BioMutaiMORC3.
DMDMi108935853.

Proteomic databases

EPDiQ14149.
MaxQBiQ14149.
PaxDbiQ14149.
PeptideAtlasiQ14149.
PRIDEiQ14149.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000400485; ENSP00000383333; ENSG00000159256.
GeneIDi23515.
KEGGihsa:23515.
UCSCiuc002yvi.3. human.

Organism-specific databases

CTDi23515.
DisGeNETi23515.
GeneCardsiMORC3.
HGNCiHGNC:23572. MORC3.
HPAiHPA018406.
HPA034848.
MIMi610078. gene.
neXtProtiNX_Q14149.
OpenTargetsiENSG00000159256.
PharmGKBiPA128394632.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1845. Eukaryota.
ENOG411033B. LUCA.
GeneTreeiENSGT00530000062983.
HOGENOMiHOG000246950.
HOVERGENiHBG055625.
InParanoidiQ14149.
OMAiYKRQCHM.
OrthoDBiEOG091G018P.
PhylomeDBiQ14149.
TreeFamiTF329118.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000159256-MONOMER.

Miscellaneous databases

ChiTaRSiMORC3. human.
GeneWikiiMORC3.
GenomeRNAii23515.
PROiQ14149.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159256.
CleanExiHS_MORC3.
ExpressionAtlasiQ14149. baseline and differential.
GenevisibleiQ14149. HS.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
InterProiIPR003594. HATPase_C.
IPR011124. Znf_CW.
[Graphical view]
PfamiPF07496. zf-CW. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 3 hits.
PROSITEiPS51050. ZF_CW. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMORC3_HUMAN
AccessioniPrimary (citable) accession number: Q14149
Secondary accession number(s): A8KA92, Q9UEZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 13, 2006
Last modified: November 30, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.