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Q3TDX8

- NB5R4_MOUSE

UniProt

Q3TDX8 - NB5R4_MOUSE

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Protein
Cytochrome b5 reductase 4
Gene
Cyb5r4, Ncb5or
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS).1 Publication

Catalytic activityi

NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.

Cofactori

FAD By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Iron (heme axial ligand) By similarity
Metal bindingi112 – 1121Iron (heme axial ligand) By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi372 – 38716FAD By similarity
Add
BLAST
Nucleotide bindingi399 – 43133FAD By similarity
Add
BLAST

GO - Molecular functioni

  1. NAD(P)H oxidase activity Source: Ensembl
  2. NADPH-hemoprotein reductase activity Source: Ensembl
  3. cytochrome-b5 reductase activity, acting on NAD(P)H Source: MGI
  4. flavin adenine dinucleotide binding Source: Ensembl
  5. heme binding Source: MGI
  6. metal ion binding Source: UniProtKB-KW
  7. protein binding Source: MGI

GO - Biological processi

  1. NADP metabolic process Source: Ensembl
  2. cell development Source: MGI
  3. generation of precursor metabolites and energy Source: Ensembl
  4. glucose homeostasis Source: MGI
  5. heme metabolic process Source: MGI
  6. insulin secretion Source: MGI
  7. response to antibiotic Source: MGI
  8. superoxide metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b5 reductase 4 (EC:1.6.2.2)
Alternative name(s):
Flavohemoprotein b5/b5R
Short name:
b5+b5R
N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein
cb5/cb5R
Gene namesi
Name:Cyb5r4
Synonyms:Ncb5or
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:2386848. Cyb5r4.

Subcellular locationi

Endoplasmic reticulum
Note: Soluble protein By similarity.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. endoplasmic reticulum Source: MGI
  3. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Mice display insulin-deficient diabetes. Embryos and fetus develop normally. At 4 weeks of age, mice show have normal blood glucose levels but impaired glucose tolerance. Isolated islets have markedly impaired glucose- or arginine-stimulated insulin secretion. By 7 weeks of age, they develop severe hyperglycemia with markedly decreased serum insulin levels and nearly normal insulin tolerance. As the animals age, there is a progressive loss of beta cells in pancreatic islets, but there is no loss of alpha, delta, or PP cells. 4 week-old mice have enhanced sensitivity to the diabetogenic agent streptozotocin.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528Cytochrome b5 reductase 4
PRO_0000410469Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ3TDX8.

PTM databases

PhosphoSiteiQ3TDX8.

Expressioni

Tissue specificityi

Ubiquitously expressed. Isoform 2 is expressed in testis, brain, skeletal muscle and in the male germline.2 Publications

Gene expression databases

BgeeiQ3TDX8.
CleanExiMM_CYB5R4.
GenevestigatoriQ3TDX8.

Interactioni

Protein-protein interaction databases

IntActiQ3TDX8. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ3TDX8.
SMRiQ3TDX8. Positions 51-137, 282-502.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 13077Cytochrome b5 heme-binding
Add
BLAST
Domaini172 – 26392CS
Add
BLAST
Domaini280 – 392113FAD-binding FR-type
Add
BLAST

Sequence similaritiesi

Contains 1 CS domain.

Phylogenomic databases

eggNOGiCOG0543.
GeneTreeiENSGT00390000008881.
HOVERGENiHBG108174.
InParanoidiQ3TDX8.
OMAiKDYHEEK.
OrthoDBiEOG718KBZ.
TreeFamiTF313874.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
3.10.120.10. 1 hit.
InterProiIPR007052. CS_dom.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR008978. HSP20-like_chaperone.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
SUPFAMiSSF49764. SSF49764. 1 hit.
SSF55856. SSF55856. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51203. CS. 1 hit.
PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3TDX8-4) [UniParc]FASTAAdd to Basket

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

MLNVPSQAFP APGSQQRVSS QGRSKVPLKQ GRSLMDWIRL TKSGKDLTGL    50
KGGLIEVTEE ELKKHNKKED CWICIRGFVY NVSPYMEYHP GGEDELMRAA 100
GADGTDLFNE VHRWVNYESM LKECLVGRMA VKPAVPKDCH EGKRVLNGML 150
PKSQMSDTLP RDVTDTLPRE DLSSPSYDWF QTESSVTIVV YTKQKNISLD 200
SVIVDLQDDS LRAEAVIKDH SYLVHVGLSH EVQENFSVRV IENVGKIEIV 250
LQKKESVSWQ CLGDHLEKHD SFIPKKDTGL YYRRCQLISK EDVTHDTRLF 300
CLMLPPSTHL QVPVGQHVYL KLSVTGAEIV KPYTPVSDSL LSDFKEPVLS 350
PNKYICFLIK IYPAGLFTPE LDRLQIGDFI SVSGPEGDFK VSKLQEVEDL 400
FLLAAGTGFT PMVTVLNYAL SHMSSLRKVK LMFFNKTEDD IIWRCQLEKL 450
ALREKRFDVE FVLSAPSPEW NGKQGHISRA LLSEFLQRSS ENSRAFLCIC 500
GPTPFTDEGI RLLHDLNFSD DEIHGFTA 528
Length:528
Mass (Da):59,716
Last modified:June 28, 2011 - v3
Checksum:i8CF34CE865980A66
GO
Isoform 2 (identifier: Q3TDX8-5) [UniParc]FASTAAdd to Basket

Also known as: cb5/cb5rDelta12

The sequence of this isoform differs from the canonical sequence as follows:
     326-376: Missing.

Show »
Length:477
Mass (Da):53,994
Checksum:i4F809037109F6B5D
GO

Sequence cautioni

The sequence AAH25438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAC41118.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAE34044.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAE42908.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti156 – 1561S → SDTLPRDVT.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei326 – 37651Missing in isoform 2.
VSP_041453Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711D → G in BAE34044. 1 Publication
Sequence conflicti171 – 1711D → G in BAE41470. 1 Publication
Sequence conflicti171 – 1711D → G in BAE42908. 1 Publication
Sequence conflicti171 – 1711D → G in AAK08116. 1 Publication
Sequence conflicti171 – 1711D → G in AAQ83900. 1 Publication
Sequence conflicti171 – 1711D → G in AAQ83901. 1 Publication
Sequence conflicti216 – 2161V → I in AAH25438. 1 Publication
Sequence conflicti300 – 3001F → L in BAE34044. 1 Publication
Sequence conflicti300 – 3001F → L in BAE41470. 1 Publication
Sequence conflicti300 – 3001F → L in BAE42908. 1 Publication
Sequence conflicti300 – 3001F → L in AAH02170. 1 Publication
Sequence conflicti300 – 3001F → L in AAK08116. 1 Publication
Sequence conflicti300 – 3001F → L in AAQ83900. 1 Publication
Sequence conflicti300 – 3001F → L in AAQ83901. 1 Publication
Sequence conflicti336 – 3361V → L in BAE34044. 1 Publication
Sequence conflicti339 – 3391S → P in BAE41470. 1 Publication
Sequence conflicti356 – 3561C → Y in BAE34044. 1 Publication
Sequence conflicti356 – 3561C → Y in BAE41470. 1 Publication
Sequence conflicti356 – 3561C → Y in BAE42908. 1 Publication
Sequence conflicti356 – 3561C → Y in AAH02170. 1 Publication
Sequence conflicti356 – 3561C → Y in AAH25438. 1 Publication
Sequence conflicti356 – 3561C → Y in AAK08116. 1 Publication
Sequence conflicti356 – 3561C → Y in AAQ83900. 1 Publication
Sequence conflicti388 – 3881D → N in BAE34044. 1 Publication
Sequence conflicti388 – 3881D → N in BAE41470. 1 Publication
Sequence conflicti388 – 3881D → N in BAE42908. 1 Publication
Sequence conflicti388 – 3881D → N in AAH02170. 1 Publication
Sequence conflicti388 – 3881D → N in AAH25438. 1 Publication
Sequence conflicti388 – 3881D → N in AAK08116. 1 Publication
Sequence conflicti388 – 3881D → N in AAQ83900. 1 Publication
Sequence conflicti388 – 3881D → N in AAQ83901. 1 Publication
Sequence conflicti393 – 3931K → T in AAH25438. 1 Publication
Sequence conflicti438 – 4381E → D in BAC37357. 1 Publication
Sequence conflicti504 – 5041P → Q in BAE39522. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK078682 mRNA. Translation: BAC37357.1.
AK090159 mRNA. Translation: BAC41118.1. Different initiation.
AK157312 mRNA. Translation: BAE34044.1. Different initiation.
AK167436 mRNA. Translation: BAE39522.1.
AK169937 mRNA. Translation: BAE41470.1.
AK172252 mRNA. Translation: BAE42908.1. Different initiation.
AC156793 Genomic DNA. No translation available.
BC025438 mRNA. Translation: AAH25438.1. Different initiation.
BC002170 mRNA. Translation: AAH02170.1.
AF338818 mRNA. Translation: AAK08116.1.
AY321368 mRNA. Translation: AAQ83900.1.
AY321369 mRNA. Translation: AAQ83901.1.
CCDSiCCDS40716.2. [Q3TDX8-4]
RefSeqiNP_077157.2. NM_024195.2. [Q3TDX8-4]
XP_006511262.1. XM_006511199.1. [Q3TDX8-5]
UniGeneiMm.30166.

Genome annotation databases

EnsembliENSMUST00000168529; ENSMUSP00000126119; ENSMUSG00000032872. [Q3TDX8-4]
ENSMUST00000173126; ENSMUSP00000134460; ENSMUSG00000032872. [Q3TDX8-5]
GeneIDi266690.
KEGGimmu:266690.
UCSCiuc009qyc.2. mouse. [Q3TDX8-4]
uc009qyf.2. mouse. [Q3TDX8-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK078682 mRNA. Translation: BAC37357.1 .
AK090159 mRNA. Translation: BAC41118.1 . Different initiation.
AK157312 mRNA. Translation: BAE34044.1 . Different initiation.
AK167436 mRNA. Translation: BAE39522.1 .
AK169937 mRNA. Translation: BAE41470.1 .
AK172252 mRNA. Translation: BAE42908.1 . Different initiation.
AC156793 Genomic DNA. No translation available.
BC025438 mRNA. Translation: AAH25438.1 . Different initiation.
BC002170 mRNA. Translation: AAH02170.1 .
AF338818 mRNA. Translation: AAK08116.1 .
AY321368 mRNA. Translation: AAQ83900.1 .
AY321369 mRNA. Translation: AAQ83901.1 .
CCDSi CCDS40716.2. [Q3TDX8-4 ]
RefSeqi NP_077157.2. NM_024195.2. [Q3TDX8-4 ]
XP_006511262.1. XM_006511199.1. [Q3TDX8-5 ]
UniGenei Mm.30166.

3D structure databases

ProteinModelPortali Q3TDX8.
SMRi Q3TDX8. Positions 51-137, 282-502.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q3TDX8. 1 interaction.

PTM databases

PhosphoSitei Q3TDX8.

Proteomic databases

PRIDEi Q3TDX8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000168529 ; ENSMUSP00000126119 ; ENSMUSG00000032872 . [Q3TDX8-4 ]
ENSMUST00000173126 ; ENSMUSP00000134460 ; ENSMUSG00000032872 . [Q3TDX8-5 ]
GeneIDi 266690.
KEGGi mmu:266690.
UCSCi uc009qyc.2. mouse. [Q3TDX8-4 ]
uc009qyf.2. mouse. [Q3TDX8-5 ]

Organism-specific databases

CTDi 51167.
MGIi MGI:2386848. Cyb5r4.

Phylogenomic databases

eggNOGi COG0543.
GeneTreei ENSGT00390000008881.
HOVERGENi HBG108174.
InParanoidi Q3TDX8.
OMAi KDYHEEK.
OrthoDBi EOG718KBZ.
TreeFami TF313874.

Miscellaneous databases

ChiTaRSi CYB5R4. mouse.
NextBioi 392180.
PROi Q3TDX8.
SOURCEi Search...

Gene expression databases

Bgeei Q3TDX8.
CleanExi MM_CYB5R4.
Genevestigatori Q3TDX8.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
3.10.120.10. 1 hit.
InterProi IPR007052. CS_dom.
IPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR008978. HSP20-like_chaperone.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF04969. CS. 1 hit.
PF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PRINTSi PR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
SUPFAMi SSF49764. SSF49764. 1 hit.
SSF55856. SSF55856. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51203. CS. 1 hit.
PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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] (ISOFORM 1), VARIANT ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS.
    Strain: C57BL/6J and NOD.
    Tissue: Eye, Liver, Spinal cord and Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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), VARIANT ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS.
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor.
  4. "Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously expressed in human cells."
    Zhu H., Qiu H., Yoon H.-W., Huang S., Bunn H.F.
    Proc. Natl. Acad. Sci. U.S.A. 96:14742-14747(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-528 (ISOFORM 1), VARIANT ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS.
  5. "Identification and characterization of a novel splice variant of mouse and rat cytochrome b5/cytochrome b5 reductase."
    Curry B.J., Roman S.D., Wallace C.A., Scott R., Miriami E., Aitken R.J.
    Genomics 83:425-438(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-528 (ISOFORMS 1 AND 2), VARIANT ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS, TISSUE SPECIFICITY.
    Strain: Swiss.
    Tissue: Testis.
  6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Promoter characterization and transcriptional regulation of Ncb5or, a novel reductase necessary for pancreatic beta-cell maintenance."
    Larade K., Bunn H.F.
    Biochim. Biophys. Acta 1759:257-262(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiNB5R4_MOUSE
AccessioniPrimary (citable) accession number: Q3TDX8
Secondary accession number(s): E9Q129
, Q3TJH3, Q3U012, Q6VXY4, Q6VXY5, Q8BJV8, Q8BTI5, Q8R3H8, Q99LY4, Q99P29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 90 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi