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Q9R002

- IFI2_MOUSE

UniProt

Q9R002 - IFI2_MOUSE

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Protein

Interferon-activable protein 202

Gene

Ifi202

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Inhibits the transcriptional activity of several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Has anti-apoptotic effects due to inhibition of the transcriptional activity of p53. Binds dsDNA in the cytosol. Is involved in innate immune response and has anti-inflammatory activity. Inhibits caspase activation in response to cytosolic DNA and inhibits the activation of the AIM2 inflammasome, probably by sequestering cytoplasmic DNA and preventing its being bound by AIM2.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei84 – 841Mediates interaction with 53BP1
Sitei283 – 2831Mediates interaction with 53BP1

GO - Molecular functioni

  1. double-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. inflammatory response Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB-KW
  3. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  4. negative regulation of innate immune response Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon-activable protein 202
Short name:
Ifi-202
Alternative name(s):
Interferon-inducible protein p202
Lupus susceptibility protein p202
Gene namesi
Name:Ifi202
Synonyms:Ifi202a, Ifi202b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1347080. Ifi202a.
MGI:1347083. Ifi202b.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Accumulates first in the cytoplasm, and is translocated to the nucleus after a delay, where it is primarily chromatin-associated.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481K → A: Strongly reduces affinity for DNA; when associated with A-53 and W-54. 1 Publication
Mutagenesisi53 – 531K → A: Strongly reduces affinity for DNA; when associated with A-48 and W-54. 1 Publication
Mutagenesisi54 – 541G → W: Strongly reduces affinity for DNA; when associated with A-48 and A-53. 1 Publication
Mutagenesisi76 – 761K → A: Strongly reduces affinity for DNA; when associated with A-79 and A-236. 1 Publication
Mutagenesisi79 – 791K → A: Strongly reduces affinity for DNA; when associated with A-76 and A-236. 1 Publication
Mutagenesisi84 – 841H → F: Loss of interaction with 53BP1; when associated with F-283. 1 Publication
Mutagenesisi166 – 1661S → A: Strongly reduces affinity for DNA; when associated with. 1 Publication
Mutagenesisi182 – 1854NDKS → ADAA: Strongly reduces affinity for DNA. 1 Publication
Mutagenesisi187 – 1871T → A: Strongly reduces affinity for DNA; when associated with A-189 and A-198. 1 Publication
Mutagenesisi189 – 1891K → A: Strongly reduces affinity for DNA; when associated with A-187 and A-198. 1 Publication
Mutagenesisi198 – 1981K → A: Strongly reduces affinity for DNA; when associated with A-187 and A-189. 1 Publication
Mutagenesisi222 – 2243HLR → ALA: Strongly reduces affinity for DNA. 1 Publication
Mutagenesisi226 – 2261G → W: Strongly reduces affinity for DNA; when associated with A-166; A-227 and A-229. 1 Publication
Mutagenesisi227 – 2271N → A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-229. 1 Publication
Mutagenesisi229 – 2291K → A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-227. 1 Publication
Mutagenesisi236 – 2361N → A: Strongly reduces affinity for DNA; when associated with A-76 and A-79. 1 Publication
Mutagenesisi283 – 2831H → F: Loss of interaction with 53BP1; when associated with F-84. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Interferon-activable protein 202PRO_0000153719Add
BLAST

Post-translational modificationi

Phosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9R002.
PRIDEiQ9R002.

PTM databases

PhosphoSiteiQ9R002.

Expressioni

Inductioni

By beta interferon. By IL6 in splenocytes (at protein level).1 Publication

Gene expression databases

BgeeiQ9R002.
CleanExiMM_IFI202B.
GenevestigatoriQ9R002.

Interactioni

Subunit structurei

Binds to several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Also binds p53, the hypophosphorylated, growth-inhibitory form of the retinoblastoma protein and the p53-binding protein 1 (53BP1).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RB1P064005EBI-3043899,EBI-491274From a different organism.
Rb1P134057EBI-3043899,EBI-971782

Protein-protein interaction databases

BioGridi204945. 1 interaction.
IntActiQ9R002. 4 interactions.
MINTiMINT-4098521.

Structurei

Secondary structure

1
445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni47 – 504Combined sources
Beta strandi56 – 583Combined sources
Beta strandi62 – 698Combined sources
Beta strandi73 – 753Combined sources
Turni76 – 794Combined sources
Beta strandi80 – 889Combined sources
Beta strandi93 – 986Combined sources
Helixi101 – 1066Combined sources
Beta strandi112 – 12110Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi132 – 1354Combined sources
Helixi138 – 1403Combined sources
Helixi146 – 1538Combined sources
Helixi158 – 1614Combined sources
Beta strandi169 – 18113Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi196 – 2016Combined sources
Turni211 – 2133Combined sources
Beta strandi216 – 2249Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi239 – 2424Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi260 – 2678Combined sources
Beta strandi271 – 2744Combined sources
Turni275 – 2784Combined sources
Beta strandi279 – 2879Combined sources
Beta strandi289 – 2979Combined sources
Helixi300 – 3067Combined sources
Beta strandi311 – 3144Combined sources
Beta strandi316 – 3205Combined sources
Beta strandi323 – 3264Combined sources
Helixi329 – 3313Combined sources
Beta strandi332 – 3343Combined sources
Helixi356 – 3616Combined sources
Beta strandi368 – 37912Combined sources
Beta strandi381 – 3899Combined sources
Beta strandi395 – 3995Combined sources
Helixi401 – 4055Combined sources
Beta strandi413 – 42210Combined sources
Beta strandi429 – 44113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JBJX-ray2.69A/B46-242[»]
4JBKX-ray2.96A/B/C/D46-242[»]
4L5QX-ray2.23A46-243[»]
4L5RX-ray1.87C46-243[»]
4L5SX-ray2.94A/B46-243[»]
4L5TX-ray3.40A/B/C/D244-445[»]
4LNQX-ray2.00A/B53-245[»]
ProteinModelPortaliQ9R002.
SMRiQ9R002. Positions 46-242, 244-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 243198HIN-200 1PROSITE-ProRule annotationAdd
BLAST
Domaini244 – 441198HIN-200 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The HIN-20 domains mediate dsDNA binding via electrostatic interactions.1 Publication

Sequence similaritiesi

Belongs to the HIN-200 family.Curated
Contains 2 HIN-200 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG81691.
GeneTreeiENSGT00390000013296.
InParanoidiQ9R002.
KOiK12971.
OrthoDBiEOG7ZD1V8.
TreeFamiTF337385.

Family and domain databases

Gene3Di2.40.50.140. 4 hits.
InterProiIPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF02760. HIN. 2 hits.
[Graphical view]
PROSITEiPS50834. HIN_200. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R002-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNRNLRSST NSEFSEGQHQ TPSSDSSGHG EDQPQASPGP NKKSHTPKKN
60 70 80 90 100
ISKGAVLHEK PMTVMVLTAT EPFNYKEGKE NMFHATVATE SQYYRVKVFN
110 120 130 140 150
MDLKEKFTEN KFITISKYFN SSGILEINET ATVSEAAPNQ IIEVPKNIIR
160 170 180 190 200
SAKETLKISK IKELDSGTLI YGVFAVEKKK VNDKSITFKI KDNEDNIKVV
210 220 230 240 250
WDKKQHNINY EKGDKLQLFS FHLRKGNGKP ILHSGNHSFI KGEKLLKESF
260 270 280 290 300
EGDGYHKGPK QVVALKATKL FTYDSIKSKK MFHATVATDT EFFRVMVFEE
310 320 330 340 350
NLEKKFIPGN TIALSDYFGM YGSLAIHEYS SVSEVKSQNK EDSSSSDERL
360 370 380 390 400
IEHLKICDLH LQTKERLVDG EFKVYRKSTG NNCICYGIWD DTGAMKVVVS
410 420 430 440
GQLTSVNCEI GNTIRLVCFE LTSNADEWFL RSTRYSYMEV IMPEK
Length:445
Mass (Da):50,466
Last modified:July 27, 2011 - v3
Checksum:i5EA0E93E143C58EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 153EFS → DLA in AAF04260. (PubMed:10493828)Curated
Sequence conflicti13 – 153EFS → DLA in AAH55888. (PubMed:15489334)Curated
Sequence conflicti79 – 791K → N in ABB00055. 1 PublicationCurated
Sequence conflicti92 – 921Q → K in AAF04260. (PubMed:10493828)Curated
Sequence conflicti92 – 921Q → K in AAH18233. (PubMed:15489334)Curated
Sequence conflicti109 – 1091E → G in ABB00055. 1 PublicationCurated
Sequence conflicti111 – 1111K → Q in AAH18233. (PubMed:15489334)Curated
Sequence conflicti127 – 1271I → F in ABB00055. 1 PublicationCurated
Sequence conflicti141 – 1422II → MF in AAA39312. (PubMed:2477366)Curated
Sequence conflicti141 – 1422II → MF in AAF04260. (PubMed:10493828)Curated
Sequence conflicti141 – 1422II → MF in ABB00055. 1 PublicationCurated
Sequence conflicti141 – 1422II → MF in AAH18233. (PubMed:15489334)Curated
Sequence conflicti141 – 1422II → MF in AAH55888. (PubMed:15489334)Curated
Sequence conflicti187 – 1871T → I in ABB00055. 1 PublicationCurated
Sequence conflicti190 – 1901I → V in ABB00055. 1 PublicationCurated
Sequence conflicti204 – 2041K → E in AAA39312. (PubMed:2477366)Curated
Sequence conflicti204 – 2041K → E in AAF04260. (PubMed:10493828)Curated
Sequence conflicti204 – 2041K → E in ABB00055. 1 PublicationCurated
Sequence conflicti204 – 2041K → E in AAH18233. (PubMed:15489334)Curated
Sequence conflicti204 – 2041K → E in AAH55888. (PubMed:15489334)Curated
Sequence conflicti240 – 2401I → V in AAF04260. (PubMed:10493828)Curated
Sequence conflicti350 – 3501L → P in AAA39312. (PubMed:2477366)Curated
Sequence conflicti350 – 3501L → P in AAF04260. (PubMed:10493828)Curated
Sequence conflicti350 – 3501L → P in ABB00055. 1 PublicationCurated
Sequence conflicti350 – 3501L → P in AAH18233. (PubMed:15489334)Curated
Sequence conflicti350 – 3501L → P in AAH55888. (PubMed:15489334)Curated
Sequence conflicti364 – 3641K → E in AAA39312. (PubMed:2477366)Curated
Sequence conflicti364 – 3641K → E in AAF04260. (PubMed:10493828)Curated
Sequence conflicti364 – 3641K → E in ABB00055. 1 PublicationCurated
Sequence conflicti364 – 3641K → E in AAH18233. (PubMed:15489334)Curated
Sequence conflicti364 – 3641K → E in AAH55888. (PubMed:15489334)Curated
Sequence conflicti368 – 3681V → F in AAA39312. (PubMed:2477366)Curated
Sequence conflicti379 – 3791T → S in AAA39312. (PubMed:2477366)Curated
Sequence conflicti379 – 3791T → S in AAF04260. (PubMed:10493828)Curated
Sequence conflicti379 – 3791T → S in ABB00055. 1 PublicationCurated
Sequence conflicti379 – 3791T → S in AAH18233. (PubMed:15489334)Curated
Sequence conflicti379 – 3791T → S in AAH55888. (PubMed:15489334)Curated
Sequence conflicti432 – 4321S → A in AAA39312. (PubMed:2477366)Curated
Sequence conflicti432 – 4321S → A in AAF04260. (PubMed:10493828)Curated
Sequence conflicti432 – 4321S → A in ABB00055. 1 PublicationCurated
Sequence conflicti432 – 4321S → A in AAH18233. (PubMed:15489334)Curated
Sequence conflicti432 – 4321S → A in AAH55888. (PubMed:15489334)Curated

Polymorphismi

NZB mice express 10 to 100 fold more Ifi202 in spleen than B6 or NZW mice. This could account for the high susceptibility of NZB mice to systemic lupus.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31418 mRNA. Translation: AAA39312.1.
AF140672 mRNA. Translation: AAF04260.1.
DQ222946 mRNA. Translation: ABB00055.1.
AC170584 Genomic DNA. No translation available.
BC018233 mRNA. Translation: AAH18233.1.
BC055888 mRNA. Translation: AAH55888.1.
CCDSiCCDS35794.1.
PIRiA34457.
RefSeqiNP_032353.2. NM_008327.2.
NP_036070.2. NM_011940.2.
XP_001473923.2. XM_001473873.3.
XP_006536966.1. XM_006536903.1.
UniGeneiMm.218770.

Genome annotation databases

EnsembliENSMUST00000000266; ENSMUSP00000000266; ENSMUSG00000026535.
GeneIDi100044068.
26388.
KEGGimmu:100044068.
mmu:26388.
UCSCiuc007dsk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31418 mRNA. Translation: AAA39312.1 .
AF140672 mRNA. Translation: AAF04260.1 .
DQ222946 mRNA. Translation: ABB00055.1 .
AC170584 Genomic DNA. No translation available.
BC018233 mRNA. Translation: AAH18233.1 .
BC055888 mRNA. Translation: AAH55888.1 .
CCDSi CCDS35794.1.
PIRi A34457.
RefSeqi NP_032353.2. NM_008327.2.
NP_036070.2. NM_011940.2.
XP_001473923.2. XM_001473873.3.
XP_006536966.1. XM_006536903.1.
UniGenei Mm.218770.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4JBJ X-ray 2.69 A/B 46-242 [» ]
4JBK X-ray 2.96 A/B/C/D 46-242 [» ]
4L5Q X-ray 2.23 A 46-243 [» ]
4L5R X-ray 1.87 C 46-243 [» ]
4L5S X-ray 2.94 A/B 46-243 [» ]
4L5T X-ray 3.40 A/B/C/D 244-445 [» ]
4LNQ X-ray 2.00 A/B 53-245 [» ]
ProteinModelPortali Q9R002.
SMRi Q9R002. Positions 46-242, 244-442.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204945. 1 interaction.
IntActi Q9R002. 4 interactions.
MINTi MINT-4098521.

PTM databases

PhosphoSitei Q9R002.

Proteomic databases

PaxDbi Q9R002.
PRIDEi Q9R002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000266 ; ENSMUSP00000000266 ; ENSMUSG00000026535 .
GeneIDi 100044068.
26388.
KEGGi mmu:100044068.
mmu:26388.
UCSCi uc007dsk.2. mouse.

Organism-specific databases

CTDi 26388.
MGIi MGI:1347080. Ifi202a.
MGI:1347083. Ifi202b.

Phylogenomic databases

eggNOGi NOG81691.
GeneTreei ENSGT00390000013296.
InParanoidi Q9R002.
KOi K12971.
OrthoDBi EOG7ZD1V8.
TreeFami TF337385.

Miscellaneous databases

ChiTaRSi Ifi202b. mouse.
NextBioi 304323.
PROi Q9R002.
SOURCEi Search...

Gene expression databases

Bgeei Q9R002.
CleanExi MM_IFI202B.
Genevestigatori Q9R002.

Family and domain databases

Gene3Di 2.40.50.140. 4 hits.
InterProi IPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view ]
Pfami PF02760. HIN. 2 hits.
[Graphical view ]
PROSITEi PS50834. HIN_200. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Interferons as gene activators. Indications for repeated gene duplication during the evolution of a cluster of interferon-activatable genes on murine chromosome 1."
    Choubey D., Snoddy J., Chaturvedi V., Toniato E., Opdenakker G., Thakur A., Samanta H., Engel D.A., Lengyel P.
    J. Biol. Chem. 264:17182-17189(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: AKR.
  2. "Characteristics of three homologous 202 genes (Ifi202a, ifi202b, and ifi202c) from the murine interferon-activatable gene 200 cluster."
    Wang H., Chatterjee G., Meyer J.J., Liu C.J., Manjunath N.A., Bray-Ward P., Lengyel P.
    Genomics 60:281-294(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Sv.
  3. "Coding cDNA sequence for p202 in New Zealand Black mice."
    Chen J., Choubey D.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NZB.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor.
  6. "p202, an interferon-inducible modulator of transcription, inhibits transcriptional activation by the p53 tumor suppressor protein, and a segment from the p53-binding protein 1 that binds to p202 overcomes this inhibition."
    Datta B., Li B., Choubey D., Nallur G., Lengyel P.
    J. Biol. Chem. 271:27544-27555(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-84 AND HIS-283.
  7. "Evidence for an interferon-inducible gene, Ifi202, in the susceptibility to systemic lupus."
    Rozzo S.J., Allard J.D., Choubey D., Vyse T.J., Izui S., Peltz G., Kotzin B.L.
    Immunity 15:435-443(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM.
  8. "Interleukin-6 induces expression of Ifi202, an interferon-inducible candidate gene for lupus susceptibility."
    Pramanik R., Jorgensen T.N., Xin H., Kotzin B.L., Choubey D.
    J. Biol. Chem. 279:16121-16127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY IL6.
  9. "Increased expression of Ifi202, an IFN-activatable gene, in B6.Nba2 lupus susceptible mice inhibits p53-mediated apoptosis."
    Xin H., D'Souza S., Jorgensen T.N., Vaughan A.T., Lengyel P., Kotzin B.L., Choubey D.
    J. Immunol. 176:5863-5870(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53.
  10. "HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA."
    Roberts T.L., Idris A., Dunn J.A., Kelly G.M., Burnton C.M., Hodgson S., Hardy L.L., Garceau V., Sweet M.J., Ross I.L., Hume D.A., Stacey K.J.
    Science 323:1057-1060(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Structural basis for termination of AIM2-mediated signaling by p202."
    Ru H., Ni X., Zhao L., Crowley C., Ding W., Hung L.W., Shaw N., Cheng G., Liu Z.J.
    Cell Res. 23:855-858(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 46-242 IN COMPLEX WITH DNA, FUNCTION, DOMAIN, MUTAGENESIS OF LYS-48; LYS-53; GLY-54; LYS-76; LYS-79; SER-166; 182-ASN--SER-185; THR-187; LYS-189; LYS-198; 222-HIS--ARG-224; GLY-226; ASN-227; LYS-229 AND ASN-236, DNA BINDING.

Entry informationi

Entry nameiIFI2_MOUSE
AccessioniPrimary (citable) accession number: Q9R002
Secondary accession number(s): E9QLD9
, P15091, Q38JF1, Q7TMN6, Q8VEL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3