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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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri404 – 45451CW-typePROSITE-ProRule annotationAdd
BLAST

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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351E → A: Fails to localize to PML nuclear bodies and activate TP53. 1 Publication
Mutagenesisi67 – 671D → N: Forms nuclear bodies, but rapidly diffuses throughout the nucleus under conditions of ATP depletion. 1 Publication
Mutagenesisi101 – 1011G → A: Diffuse nuclear localization. Fails to form nuclear bodies in the presence of ATP. 1 Publication
Mutagenesisi419 – 4191W → A: Diffuse nuclear localization, possibly due to loss of DNA or nucleosome binding. 1 Publication
Mutagenesisi597 – 5971K → R: Loss of sumoylation; when associated with R-650; R-651; R-740 and R-794. 1 Publication
Mutagenesisi650 – 6501K → R: Loss of sumoylation; when associated with R-597; R-651; R-740 and R-794. 1 Publication
Mutagenesisi651 – 6511K → R: Loss of sumoylation; when associated with R-597; R-650; R-740 and R-794. 1 Publication
Mutagenesisi740 – 7401K → R: Loss of sumoylation; when associated with R-597; R-650; R-651 and R-794. 1 Publication
Mutagenesisi794 – 7941K → R: Loss of sumoylation; when associated with R-597; R-650; R-651 and R-740. 1 Publication

Organism-specific databases

PharmGKBiPA128394632.

Polymorphism and mutation databases

BioMutaiMORC3.
DMDMi108935853.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 939939MORC family CW-type zinc finger protein 3PRO_0000096538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei503 – 5031PhosphoserineCombined sources
Modified residuei514 – 5141PhosphoserineCombined sources
Modified residuei540 – 5401PhosphoserineCombined sources
Modified residuei560 – 5601PhosphoserineCombined sources
Cross-linki597 – 597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki650 – 650Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki650 – 650Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki651 – 651Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki651 – 651Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki740 – 740Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki740 – 740Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei765 – 7651PhosphoserineCombined sources
Cross-linki794 – 794Glycyl 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.
PhosphoSiteiQ14149.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ14149.
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 interactions.
IntActiQ14149. 13 interactions.
STRINGi9606.ENSP00000383333.

Structurei

Secondary structure

1
939
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi408 – 4125Combined sources
Turni414 – 4163Combined sources
Beta strandi419 – 4224Combined sources
Helixi435 – 4373Combined sources
Helixi441 – 4433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QQ4X-ray1.75A/B400-460[»]
ProteinModelPortaliQ14149.
SMRiQ14149. Positions 406-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni326 – 35328Nuclear matrix binding1 PublicationAdd
BLAST
Regioni500 – 59192RNA binding1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili686 – 877192Sequence analysisAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri404 – 45451CW-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1845. Eukaryota.
ENOG411033B. LUCA.
GeneTreeiENSGT00530000062983.
HOGENOMiHOG000246950.
HOVERGENiHBG055625.
InParanoidiQ14149.
OMAiYKRQCHM.
OrthoDBiEOG7X3QQB.
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 BAA09485.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA89432.1 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
EntryMethodResolution (Å)ChainPositionsPDBsum
4QQ4X-ray1.75A/B400-460[»]
ProteinModelPortaliQ14149.
SMRiQ14149. Positions 406-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117062. 17 interactions.
IntActiQ14149. 13 interactions.
STRINGi9606.ENSP00000383333.

PTM databases

iPTMnetiQ14149.
PhosphoSiteiQ14149.

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

Phylogenomic databases

eggNOGiKOG1845. Eukaryota.
ENOG411033B. LUCA.
GeneTreeiENSGT00530000062983.
HOGENOMiHOG000246950.
HOVERGENiHBG055625.
InParanoidiQ14149.
OMAiYKRQCHM.
OrthoDBiEOG7X3QQB.
PhylomeDBiQ14149.
TreeFamiTF329118.

Miscellaneous databases

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

Gene expression databases

BgeeiQ14149.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Trachea.
  3. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The newly identified human nuclear protein NXP-2 possesses three distinct domains, the nuclear matrix-binding, RNA-binding, and coiled-coil domains."
    Kimura Y., Sakai F., Nakano O., Kisaki O., Sugimoto H., Sawamura T., Sadano H., Osumi T.
    J. Biol. Chem. 277:20611-20617(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Placenta.
  5. Cited for: FUNCTION, INTERACTION WITH TP53 AND PML, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-35.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Two-step colocalization of MORC3 with PML nuclear bodies."
    Mimura Y., Takahashi K., Kawata K., Akazawa T., Inoue N.
    J. Cell Sci. 123:2014-2024(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUMOYLATION AT LYS-597; LYS-650; LYS-651; LYS-740 AND LYS-794, SUBUNIT, INTERACTION WITH PML, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-67; GLY-101; TRP-419; LYS-597; LYS-650; LYS-651; LYS-740 AND LYS-794.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514; SER-540; SER-560 AND SER-765, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  11. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-740, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The Cellular Factor NXP2/MORC3 Is a Positive Regulator of Influenza Virus Multiplication."
    Ver L.S., Marcos-Villar L., Landeras-Bueno S., Nieto A., Ortin J.
    J. Virol. 89:10023-10030(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH INFLUENZA A VIRUS PA AND PB1 POLYMERASE SUBUNITS.
  15. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-650 AND LYS-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Liu Y., Tempel W., Dong A., Bountra C., Arrowsmith C.H., Edwards A.M., Min J.
    Submitted (JUN-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 400-460.

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: July 6, 2016
This is version 120 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.