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Q3TBT3 (STING_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stimulator of interferon genes protein

Short name=mSTING
Alternative name(s):
Endoplasmic reticulum interferon stimulator
Short name=ERIS
Mediator of IRF3 activation
Short name=MMITA
Transmembrane protein 173
Gene names
Name:Tmem173
Synonyms:Eris Mita, Mpys, Sting
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by recognizing and binding cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced in response to DNA virus in the cytosol: upon binding of c-di-GMP or cGAMP, autoinhibition is alleviated and TMEM173/STING is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subunit structure

Homodimer; 'Lys-63'-linked ubiquitination at Lys-150 is required for homodimerization. Interacts with TBK1; when homodimer, leading to subsequent production of IFN-beta By similarity. Interacts with DDX58/RIG-I, MAVS and SSR2. Interacts with RNF5. Associates with the MHC-II complex. Interacts with IFIT1 and IFIT2 By similarity. Ref.2 Ref.11

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein. Cytoplasmperinuclear region. Cytoplasm By similarity. Note: In response to double-stranded DNA stimulation, relocalizes to perinuclear region, where the kinase TBK1 is recruited. Ref.2 Ref.7

Tissue specificity

Present in spleen and thymus tissue. Also present in dendritic cells (at protein level). Ref.2

Developmental stage

Expressed throughout the B-cell lineage prior to the plasma cell stage but occurs at highest levels in mature B-cells. Highly expressed in cells representing mature stages of B-cells but weakly expressed in pre-B cells, immature B-cells, and memory B-cell stages. Not detected in plasma cells. Ref.2

Domain

The c-di-GMP-binding domain (CBD) forms a homodimer via hydrophobic interactions and binds both the cyclic diguanylate monophosphate (c-di-GMP) and the cyclic GMP-AMP (cGAMP) messengers. In absence of c-di-GMP or cGAMP, the protein is autoinhibited by an intramolecular interaction between the CBD and the C-terminal tail (CTT). Binding of c-di-GMP or cGAMP to the CBD releases the autoinhibition by displacing the CTT, leading to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon. The N-terminal part of the CBD region was initially though to contain a fifth transmembrane region (TM5) but is part of the folded, soluble CBD By similarity.

Post-translational modification

Phosphorylated on Ser-357 by TBK1, leading to activation and production of IFN-beta By similarity. Phosphorylated on tyrosine residues upon MHC-II aggregation. Ref.2

Ubiquitinated. 'Lys-63'-linked ubiquitination mediated by TRIM56 at Lys-150 promotes homodimerization and recruitment of the antiviral kinase TBK1 and subsequent production of IFN-beta. 'Lys-48'-linked polyubiquitination at Lys-150 occurring after viral infection is mediated by RNF5 and leads to proteasomal degradation By similarity.

Disruption phenotype

Defects in innate immunity. Death within 7 days of herpes simplex virus 1 (HSV-1) infection. In addition, mice show a remarkable reduction in cytotoxic T-cell responses after plasmid DNA vaccination. Cells fail to induce type I interferon production in response to dsDNA and infection with herpes simplex virus 1 (HSV-1) and L.monocytogenes that deliver DNA to the host cytosol. Ref.7

Miscellaneous

Was named MPYS because the protein sequence begins by Met-Pro-Tyr-Ser residues (Ref.2).

Sequence similarities

Belongs to the TMEM173 family.

Sequence caution

The sequence AAH27757.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC37010.1 differs from that shown. Reason: Erroneous termination at position 203. Translated as Leu.

The sequence BAE42563.1 differs from that shown. Reason: Frameshift at position 377.

Ontologies

Keywords
   Biological processApoptosis
Immunity
Innate immunity
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandNucleotide-binding
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of innate immune response

Inferred from mutant phenotype PubMed 21947006Ref.10. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to exogenous dsRNA

Inferred from electronic annotation. Source: Ensembl

cellular response to interferon-beta

Inferred from mutant phenotype PubMed 21892174. Source: MGI

defense response to virus

Inferred from mutant phenotype Ref.7. Source: UniProtKB

innate immune response

Inferred from mutant phenotype Ref.8Ref.7. Source: UniProtKB

interferon-beta production

Inferred from mutant phenotype Ref.8Ref.7. Source: UniProtKB

positive regulation of defense response to virus by host

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein import into nucleus, translocation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription factor import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21892174. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 19926846. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 19926846PubMed 21892174. Source: MGI

endoplasmic reticulum membrane

Inferred from direct assay Ref.7. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 22745163. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclic-GMP-AMP binding

Inferred from direct assay Ref.10. Source: UniProtKB

cyclic-di-GMP binding

Inferred from direct assay PubMed 21947006. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21892174PubMed 22000020PubMed 23142775. Source: IntAct

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 21074459. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3TBT3-1)

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.
Isoform 2 (identifier: Q3TBT3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MIVESFGASGNPVGPCHFWSLYGVLLGVHWSVLHLGTFRGIRSAGLWLLM
Note: No experimental confirmation available.
Isoform 3 (identifier: Q3TBT3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     76-116: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Stimulator of interferon genes protein
PRO_0000271117

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4121Helical; Name=1; Potential
Topological domain42 – 465Extracellular Potential
Transmembrane47 – 6721Helical; Name=2; Potential
Topological domain68 – 8619Cytoplasmic Potential
Transmembrane87 – 10620Helical; Name=3; Potential
Topological domain107 – 1148Extracellular Potential
Transmembrane115 – 13521Helical; Name=4; Potential
Topological domain136 – 378243Cytoplasmic Potential
Region152 – 339188c-di-GMP-binding domain (CBD)
Region161 – 1666c-di-GMP binding
Region237 – 2404c-di-GMP binding
Region339 – 37840C-terminal tail (CTT) By similarity

Sites

Binding site2621c-di-GMP

Amino acid modifications

Modified residue3571Phosphoserine; by TBK1 By similarity
Cross-link150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence11M → MIVESFGASGNPVGPCHFWS LYGVLLGVHWSVLHLGTFRG IRSAGLWLLM in isoform 2.
VSP_022284
Alternative sequence76 – 11641Missing in isoform 3.
VSP_022285

Experimental info

Mutagenesis1611S → A: Decrease in cGAMP-binding. Ref.10
Mutagenesis2391Y → S: Strong decrease in cGAMP-binding. Ref.10
Mutagenesis2411N → A: Strong decrease in cGAMP-binding. Ref.10
Sequence conflict111P → Q in BAE27042. Ref.3
Sequence conflict391P → S in BAB27972. Ref.3
Sequence conflict981M → V in BAE42563. Ref.3
Sequence conflict1111T → N in BAC37010. Ref.3
Sequence conflict2101N → D in BAE34068. Ref.3
Sequence conflict2101N → D in BAE42310. Ref.3
Sequence conflict2101N → D in BAE42224. Ref.3
Sequence conflict2101N → D in BAE32222. Ref.3
Sequence conflict2101N → D in BAE34517. Ref.3
Sequence conflict3151E → K in BAC37010. Ref.3

Secondary structure

.................................... 378
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 656ED19097ACE4C8

FASTA37842,830
        10         20         30         40         50         60 
MPYSNLHPAI PRPRGHRSKY VALIFLVASL MILWVAKDPP NHTLKYLALH LASHELGLLL 

        70         80         90        100        110        120 
KNLCCLAEEL CHVQSRYQGS YWKAVRACLG CPIHCMAMIL LSSYFYFLQN TADIYLSWMF 

       130        140        150        160        170        180 
GLLVLYKSLS MLLGLQSLTP AEVSAVCEEK KLNVAHGLAW SYYIGYLRLI LPGLQARIRM 

       190        200        210        220        230        240 
FNQLHNNMLS GAGSRRLYIL FPLDCGVPDN LSVVDPNIRF RDMLPQQNID RAGIKNRVYS 

       250        260        270        280        290        300 
NSVYEILENG QPAGVCILEY ATPLQTLFAM SQDAKAGFSR EDRLEQAKLF CRTLEEILED 

       310        320        330        340        350        360 
VPESRNNCRL IVYQEPTDGN SFSLSQEVLR HIRQEEKEEV TMNAPMTSVA PPPSVLSQEP 

       370 
RLLISGMDQP LPLRTDLI 

« Hide

Isoform 2 [UniParc].

Checksum: CC362C808C035BE9
Show »

FASTA42748,151
Isoform 3 [UniParc].

Checksum: 9F25E302E7E0FCE8
Show »

FASTA33738,036

References

« Hide 'large scale' references
[1]"The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation."
Zhong B., Yang Y., Li S., Wang Y.-Y., Li Y., Diao F., Lei C., He X., Zhang L., Tien P., Shu H.-B.
Immunity 29:538-550(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"MPYS, a novel membrane tetraspanner, is associated with major histocompatibility complex class II and mediates transduction of apoptotic signals."
Jin L., Waterman P.M., Jonscher K.R., Short C.M., Reisdorph N.A., Cambier J.C.
Mol. Cell. Biol. 28:5014-5026(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J.
Tissue: Embryo, Inner ear, Spleen and Thymus.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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).
Strain: Czech II and FVB/N.
Tissue: Mammary gland.
[6]"STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling."
Ishikawa H., Barber G.N.
Nature 455:674-678(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity."
Ishikawa H., Ma Z., Barber G.N.
Nature 461:788-792(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[8]"ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization."
Sun W., Li Y., Chen L., Chen H., You F., Zhou X., Zhou Y., Zhai Z., Chen D., Jiang Z.
Proc. Natl. Acad. Sci. U.S.A. 106:8653-8658(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"cGAS produces a 2'-5'-linked cyclic dinucleotide second messenger that activates STING."
Ablasser A., Goldeck M., Cavlar T., Deimling T., Witte G., Rohl I., Hopfner K.P., Ludwig J., Hornung V.
Nature 498:380-384(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA."
Wu J., Sun L., Chen X., Du F., Shi H., Chen C., Chen Z.J.
Science 339:826-830(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CGAMP-BINDING, MUTAGENESIS OF SER-161; TYR-239 AND ASN-241.
[11]"Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING."
Chin K.H., Tu Z.L., Su Y.C., Yu Y.J., Chen H.C., Lo Y.C., Chen C.P., Barber G.N., Chuah M.L., Liang Z.X., Chou S.H.
Acta Crystallogr. D 69:352-366(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 138-344 IN COMPLEX WITH CYCLIC DIGUANOSINE MONOPHOSPHATE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ222242 mRNA. Translation: ACI46649.1.
DQ910493 mRNA. Translation: ABI78935.1.
AK012006 mRNA. Translation: BAB27972.1.
AK077788 mRNA. Translation: BAC37010.1. Sequence problems.
AK089405 mRNA. Translation: BAC40870.1.
AK146284 mRNA. Translation: BAE27042.1.
AK153868 mRNA. Translation: BAE32222.1.
AK157370 mRNA. Translation: BAE34068.1.
AK158458 mRNA. Translation: BAE34517.1.
AK170724 mRNA. Translation: BAE41981.1.
AK171065 mRNA. Translation: BAE42224.1.
AK171203 mRNA. Translation: BAE42310.1.
AK171612 mRNA. Translation: BAE42563.1. Frameshift.
CH466557 Genomic DNA. Translation: EDK97142.1.
BC027757 mRNA. Translation: AAH27757.1. Different initiation.
BC046640 mRNA. Translation: AAH46640.1.
CCDSCCDS50253.1. [Q3TBT3-1]
RefSeqNP_001276520.1. NM_001289591.1. [Q3TBT3-2]
NP_001276521.1. NM_001289592.1. [Q3TBT3-3]
NP_082537.1. NM_028261.1. [Q3TBT3-1]
XP_006526346.1. XM_006526283.1. [Q3TBT3-1]
UniGeneMm.45995.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4JC5X-ray2.75A/B149-348[»]
4KBYX-ray2.36A/B138-344[»]
4KC0X-ray2.20A/B138-344[»]
4LOJX-ray1.77A/B154-340[»]
4LOKX-ray2.07A/B154-340[»]
4LOLX-ray2.43A/B154-340[»]
ProteinModelPortalQ3TBT3.
SMRQ3TBT3. Positions 155-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59959N.
IntActQ3TBT3. 4 interactions.

PTM databases

PhosphoSiteQ3TBT3.

Proteomic databases

PaxDbQ3TBT3.
PRIDEQ3TBT3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000115728; ENSMUSP00000111393; ENSMUSG00000024349. [Q3TBT3-1]
GeneID72512.
KEGGmmu:72512.
UCSCuc008emt.3. mouse. [Q3TBT3-1]
uc008emu.3. mouse. [Q3TBT3-3]
uc008emv.3. mouse. [Q3TBT3-2]

Organism-specific databases

CTD340061.
MGIMGI:1919762. Tmem173.

Phylogenomic databases

eggNOGNOG43926.
GeneTreeENSGT00390000008582.
HOVERGENHBG094065.
InParanoidA7YGY9.
KOK12654.
OMALAWSYYI.
OrthoDBEOG79GT88.
PhylomeDBQ3TBT3.
TreeFamTF324444.

Gene expression databases

BgeeQ3TBT3.
CleanExMM_TMEM173.
GenevestigatorQ3TBT3.

Family and domain databases

InterProIPR029158. STING.
[Graphical view]
PfamPF15009. TMEM173. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio336376.
PROQ3TBT3.
SOURCESearch...

Entry information

Entry nameSTING_MOUSE
AccessionPrimary (citable) accession number: Q3TBT3
Secondary accession number(s): A7YGY9 expand/collapse secondary AC list , Q3TAV5, Q3TYP5, Q3TZY8, Q3UJW3, Q8C227, Q8C5Q3, Q8K393, Q9CZY7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot