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Protein

E3 ubiquitin-protein ligase RNF216

Gene

RNF216

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

Functioni

Isoform 1 acts as an E3 ubiquitin ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Promotes degradation of TRAF3, TLR4 and TLR9. Contributes to the regulation of antiviral responses. Down-regulates activation of NF-kappa-B, IRF3 activation and IFNB production. Isoform 3 inhibits TNF and IL-1 mediated activation of NF-kappa-B. Promotes TNF and RIP mediated apoptosis.2 Publications

Pathwayi: protein ubiquitination

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri515 – 56652RING-type 1Add
BLAST
Zinc fingeri583 – 64866IBR-typeAdd
BLAST
Zinc fingeri675 – 71440RING-type 2Add
BLAST

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • negative regulation of type I interferon production Source: Reactome
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • regulation of defense response to virus by host Source: UniProtKB
  • regulation of interferon-beta production Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Host-virus interaction, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF216 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 216
Triad domain-containing protein 3
Ubiquitin-conjugating enzyme 7-interacting protein 1
Zinc finger protein inhibiting NF-kappa-B
Gene namesi
Name:RNF216
Synonyms:TRIAD3, UBCE7IP1, ZIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:21698. RNF216.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Gordon Holmes syndrome (GDHS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by cerebellar symptoms and signs of sex steroid deficiency. Clinical features include cerebellar and brain stem atrophy, cerebellar ataxia, hypothalamic LHRH deficiency, hypogonadotrophic hypogonadism, lack of secondary sexual characteristics, and infertility.
See also OMIM:212840
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti660 – 6601R → C in GDHS. 1 Publication
VAR_070048
Natural varianti694 – 6941R → C in GDHS. 1 Publication
Corresponds to variant rs387907368 [ dbSNP | Ensembl ].
VAR_070049

Keywords - Diseasei

Disease mutation, Hypogonadotropic hypogonadism

Organism-specific databases

MalaCardsiRNF216.
MIMi212840. phenotype.
Orphaneti1173. Cerebellar ataxia - hypogonadism.
PharmGKBiPA162401829.

Polymorphism and mutation databases

BioMutaiRNF216.
DMDMi57015417.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 866866E3 ubiquitin-protein ligase RNF216PRO_0000056293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki351 – 351Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei419 – 4191PhosphoserineCombined sources
Cross-linki448 – 448Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki658 – 658Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Auto-ubiquitinated.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NWF9.
MaxQBiQ9NWF9.
PeptideAtlasiQ9NWF9.
PRIDEiQ9NWF9.

PTM databases

iPTMnetiQ9NWF9.
PhosphoSiteiQ9NWF9.

Expressioni

Tissue specificityi

Ubiquitous, with the highest levels of expression in testis and peripheral blood leukocytes.

Gene expression databases

BgeeiQ9NWF9.
CleanExiHS_RNF216.
ExpressionAtlasiQ9NWF9. baseline and differential.
GenevisibleiQ9NWF9. HS.

Organism-specific databases

HPAiHPA018955.
HPA021123.

Interactioni

Subunit structurei

Interacts with UBE2L3 and to some extent with UBE2L6. Interacts with TRAF3, TLR3, TLR4, TLR5 and TLR9. Isoform 3/ZIN binds RIPK1 and HIV VIF.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
vifP125044EBI-723337,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi119981. 21 interactions.
IntActiQ9NWF9. 4 interactions.
MINTiMINT-1194402.

Structurei

3D structure databases

ProteinModelPortaliQ9NWF9.
SMRiQ9NWF9. Positions 515-708.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili475 – 49117Sequence analysisAdd
BLAST
Coiled coili737 – 76327Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi769 – 86294Pro-richAdd
BLAST

Domaini

The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.By similarity

Sequence similaritiesi

Contains 1 IBR-type zinc finger.Curated
Contains 2 RING-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri515 – 56652RING-type 1Add
BLAST
Zinc fingeri583 – 64866IBR-typeAdd
BLAST
Zinc fingeri675 – 71440RING-type 2Add
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00510000048032.
HOGENOMiHOG000154166.
HOVERGENiHBG102854.
InParanoidiQ9NWF9.
KOiK11976.
OMAiPAPQQHD.
OrthoDBiEOG7B8S3G.
PhylomeDBiQ9NWF9.
TreeFamiTF330852.

Family and domain databases

InterProiIPR002867. IBR_dom.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NWF9-2) [UniParc]FASTAAdd to basket

Also known as: TRIAD3A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEEGNNNEEV IHLNNFHCHR GQEWINLRDG PITISDSSDE ERIPMLVTPA
60 70 80 90 100
PQQHEEEDLD DDVILTEDDS EDDYGEFLDL GPPGISEFTK PSGQTEREPK
110 120 130 140 150
PGPSHNQAAN DIVNPRSEQK VIILEEGSLL YTESDPLETQ NQSSEDSETE
160 170 180 190 200
LLSNLGESAA LADDQAIEED CWLDHPYFQS LNQQPREITN QVVPQERQPE
210 220 230 240 250
AELGRLLFQH EFPGPAFPRP EPQQGGISGP SSPQPAHPLG EFEDQQLASD
260 270 280 290 300
DEEPGPAFPM QESQEPNLEN IWGQEAAEVD QELVELLVKE TEARFPDVAN
310 320 330 340 350
GFIEEIIHFK NYYDLNVLCN FLLENPDYPK REDRIIINPS SSLLASQDET
360 370 380 390 400
KLPKIDFFDY SKLTPLDQRC FIQAADLLMA DFKVLSSQDI KWALHELKGH
410 420 430 440 450
YAITRKALSD AIKKWQELSP ETSGKRKKRK QMNQYSYIDF KFEQGDIKIE
460 470 480 490 500
KRMFFLENKR RHCRSYDRRA LLPAVQQEQE FYEQKIKEMA EHEDFLLALQ
510 520 530 540 550
MNEEQYQKDG QLIECRCCYG EFPFEELTQC ADAHLFCKEC LIRYAQEAVF
560 570 580 590 600
GSGKLELSCM EGSCTCSFPT SELEKVLPQT ILYKYYERKA EEEVAAAYAD
610 620 630 640 650
ELVRCPSCSF PALLDSDVKR FSCPNPHCRK ETCRKCQGLW KEHNGLTCEE
660 670 680 690 700
LAEKDDIKYR TSIEEKMTAA RIRKCHKCGT GLIKSEGCNR MSCRCGAQMC
710 720 730 740 750
YLCRVSINGY DHFCQHPRSP GAPCQECSRC SLWTDPTEDD EKLIEEIQKE
760 770 780 790 800
AEEEQKRKNG ENTFKRIGPP LEKPVEKVQR VEALPRPVPQ NLPQPQMPPY
810 820 830 840 850
AFAHPPFPLP PVRPVFNNFP LNMGPIPAPY VPPLPNVRVN YDFGPIHMPL
860
EHNLPMHFGP QPRHRF
Length:866
Mass (Da):99,406
Last modified:January 4, 2005 - v3
Checksum:i6A46B66A6569DE74
GO
Isoform 2 (identifier: Q9NWF9-1) [UniParc]FASTAAdd to basket

Also known as: TRIAD3B

The sequence of this isoform differs from the canonical sequence as follows:
     67-67: E → ETNKPQRSRPNLIKPAAQWQDLKRLGEERPKKSRAAFESDKSSYFSVCNNPLFDSGAQ

Show »
Length:923
Mass (Da):105,882
Checksum:iFFAA15927AE14608
GO
Isoform 3 (identifier: Q9NWF9-3) [UniParc]FASTAAdd to basket

Also known as: ZIN, TRIAD3

The sequence of this isoform differs from the canonical sequence as follows:
     1-378: Missing.

Note: 4 different alternatively spliced mRNAs code for this protein isoform.
Show »
Length:488
Mass (Da):56,697
Checksum:i6EB1D218DE2E4E6A
GO

Sequence cautioni

The sequence BAA91422.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti408 – 4081L → F in AAL38043 (PubMed:11854271).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti660 – 6601R → C in GDHS. 1 Publication
VAR_070048
Natural varianti694 – 6941R → C in GDHS. 1 Publication
Corresponds to variant rs387907368 [ dbSNP | Ensembl ].
VAR_070049

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 378378Missing in isoform 3. 2 PublicationsVSP_012443Add
BLAST
Alternative sequencei67 – 671E → ETNKPQRSRPNLIKPAAQWQ DLKRLGEERPKKSRAAFESD KSSYFSVCNNPLFDSGAQ in isoform 2. 1 PublicationVSP_012444

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY062174 mRNA. Translation: AAL38043.1.
AF513717 mRNA. Translation: AAP47174.1.
AF513718 mRNA. Translation: AAP47175.1.
AY177396 mRNA. Translation: AAO60361.1.
AY177397 mRNA. Translation: AAO60362.1.
AY177398 mRNA. Translation: AAO60363.1.
BX537406 mRNA. Translation: CAD97648.1.
AC008167 Genomic DNA. Translation: AAS07532.1.
BC000787 mRNA. Translation: AAH00787.2.
BC063825 mRNA. Translation: AAH63825.1.
AK000916 mRNA. Translation: BAA91422.1. Different initiation.
AF228527 mRNA. Translation: AAF36723.1.
CCDSiCCDS34594.1. [Q9NWF9-1]
CCDS34595.1. [Q9NWF9-2]
RefSeqiNP_996994.1. NM_207111.3. [Q9NWF9-1]
NP_996999.1. NM_207116.2. [Q9NWF9-2]
XP_005249842.1. XM_005249785.2. [Q9NWF9-1]
XP_006715811.1. XM_006715748.1. [Q9NWF9-3]
XP_011513736.1. XM_011515434.1. [Q9NWF9-1]
XP_011513738.1. XM_011515436.1. [Q9NWF9-3]
UniGeneiHs.487458.
Hs.733601.

Genome annotation databases

EnsembliENST00000389902; ENSP00000374552; ENSG00000011275. [Q9NWF9-1]
ENST00000425013; ENSP00000404602; ENSG00000011275. [Q9NWF9-2]
GeneIDi54476.
KEGGihsa:54476.
UCSCiuc003sox.3. human. [Q9NWF9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY062174 mRNA. Translation: AAL38043.1.
AF513717 mRNA. Translation: AAP47174.1.
AF513718 mRNA. Translation: AAP47175.1.
AY177396 mRNA. Translation: AAO60361.1.
AY177397 mRNA. Translation: AAO60362.1.
AY177398 mRNA. Translation: AAO60363.1.
BX537406 mRNA. Translation: CAD97648.1.
AC008167 Genomic DNA. Translation: AAS07532.1.
BC000787 mRNA. Translation: AAH00787.2.
BC063825 mRNA. Translation: AAH63825.1.
AK000916 mRNA. Translation: BAA91422.1. Different initiation.
AF228527 mRNA. Translation: AAF36723.1.
CCDSiCCDS34594.1. [Q9NWF9-1]
CCDS34595.1. [Q9NWF9-2]
RefSeqiNP_996994.1. NM_207111.3. [Q9NWF9-1]
NP_996999.1. NM_207116.2. [Q9NWF9-2]
XP_005249842.1. XM_005249785.2. [Q9NWF9-1]
XP_006715811.1. XM_006715748.1. [Q9NWF9-3]
XP_011513736.1. XM_011515434.1. [Q9NWF9-1]
XP_011513738.1. XM_011515436.1. [Q9NWF9-3]
UniGeneiHs.487458.
Hs.733601.

3D structure databases

ProteinModelPortaliQ9NWF9.
SMRiQ9NWF9. Positions 515-708.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119981. 21 interactions.
IntActiQ9NWF9. 4 interactions.
MINTiMINT-1194402.

PTM databases

iPTMnetiQ9NWF9.
PhosphoSiteiQ9NWF9.

Polymorphism and mutation databases

BioMutaiRNF216.
DMDMi57015417.

Proteomic databases

EPDiQ9NWF9.
MaxQBiQ9NWF9.
PeptideAtlasiQ9NWF9.
PRIDEiQ9NWF9.

Protocols and materials databases

DNASUi54476.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389902; ENSP00000374552; ENSG00000011275. [Q9NWF9-1]
ENST00000425013; ENSP00000404602; ENSG00000011275. [Q9NWF9-2]
GeneIDi54476.
KEGGihsa:54476.
UCSCiuc003sox.3. human. [Q9NWF9-2]

Organism-specific databases

CTDi54476.
GeneCardsiRNF216.
HGNCiHGNC:21698. RNF216.
HPAiHPA018955.
HPA021123.
MalaCardsiRNF216.
MIMi212840. phenotype.
609948. gene.
neXtProtiNX_Q9NWF9.
Orphaneti1173. Cerebellar ataxia - hypogonadism.
PharmGKBiPA162401829.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00510000048032.
HOGENOMiHOG000154166.
HOVERGENiHBG102854.
InParanoidiQ9NWF9.
KOiK11976.
OMAiPAPQQHD.
OrthoDBiEOG7B8S3G.
PhylomeDBiQ9NWF9.
TreeFamiTF330852.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSiRNF216. human.
GeneWikiiRNF216.
GenomeRNAii54476.
PROiQ9NWF9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NWF9.
CleanExiHS_RNF216.
ExpressionAtlasiQ9NWF9. baseline and differential.
GenevisibleiQ9NWF9. HS.

Family and domain databases

InterProiIPR002867. IBR_dom.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation."
    Chen D., Li X., Zhai Z., Shu H.-B.
    J. Biol. Chem. 277:15985-15991(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH RIPK1.
  2. "Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors."
    Chuang T.-H., Ulevitch R.J.
    Nat. Immunol. 5:495-502(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, INTERACTION WITH TLR3; TLR4; TLR5 AND TLR9.
    Tissue: Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Endometrium.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney and Uterus.
  6. "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] OF 450-866 (ISOFORMS 1/2/3).
    Tissue: Embryo.
  7. "Identification of a novel TRIAD protein, TRIAD3."
    van der Reijden B.A., Jansen J.H.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 509-866 (ISOFORMS 1/2/3).
  8. "Ring finger protein ZIN interacts with human immunodeficiency virus type 1 Vif."
    Feng F., Davis A., Lake J.A., Carr J., Xia W., Burrell C., Li P.
    J. Virol. 78:10574-10581(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV VIF PROTEIN (ISOFORM 3).
  9. "The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS signaling pathway by targeting TRAF3 for degradation."
    Nakhaei P., Mesplede T., Solis M., Sun Q., Zhao T., Yang L., Chuang T.H., Ware C.F., Lin R., Hiscott J.
    PLoS Pathog. 5:E1000650-E1000650(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRAF3.
  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-419, 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-448 AND LYS-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-351 AND LYS-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: VARIANTS GDHS CYS-660 AND CYS-694.

Entry informationi

Entry nameiRN216_HUMAN
AccessioniPrimary (citable) accession number: Q9NWF9
Secondary accession number(s): Q6Y691
, Q75ML7, Q7Z2H7, Q7Z7C1, Q8NHW7, Q9NYT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 4, 2005
Last modified: July 6, 2016
This is version 149 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.