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Q8C0J2

- A16L1_MOUSE

UniProt

Q8C0J2 - A16L1_MOUSE

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Protein

Autophagy-related protein 16-1

Gene

Atg16l1

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

Functioni

Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II. Thereby, controls the elongation of the nascent autophagosomal membrane.3 Publications

GO - Biological processi

  1. autophagic vacuole assembly Source: MGI
  2. negative stranded viral RNA replication Source: MGI
  3. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Autophagy-related protein 16-1
Alternative name(s):
APG16-like 1
Gene namesi
Name:Atg16l1
Synonyms:Apg16l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1924290. Atg16l1.

Subcellular locationi

Cytoplasm. Preautophagosomal structure membrane 1 Publication; Peripheral membrane protein Curated
Note: Recruited to omegasomes membranes by WIPI2. Omegasomes are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localized to preautophagosomal structure (PAS) where it is involved in the membrane targeting of ATG5. Localizes also to discrete punctae along the ciliary axoneme.1 Publication

GO - Cellular componenti

  1. autophagic vacuole Source: MGI
  2. autophagic vacuole membrane Source: MGI
  3. axoneme Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi299 – 2991D → E: Prevents cleavage by activated CASP3. 1 Publication
Mutagenesisi300 – 3001T → A: No effect on the stability of the protein. Enhances cleavage and degradation mediated by activated CASP3. Results in reduced autophagy and defective clearance of intestinal pathogens. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607Autophagy-related protein 16-1PRO_0000050849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei269 – 2691PhosphoserineBy similarity
Modified residuei287 – 2871PhosphoserineBy similarity

Post-translational modificationi

Proteolytic cleavage by activated CASP3 leads to degradation and may regulate autophagy upon cellular stress and apoptotic stimuli.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8C0J2.
PaxDbiQ8C0J2.
PRIDEiQ8C0J2.

2D gel databases

REPRODUCTION-2DPAGEQ8C0J2.

PTM databases

PhosphoSiteiQ8C0J2.

Expressioni

Tissue specificityi

Widely expressed. In the liver, isoform 2 is highly expressed and isoform 1 is weakly expressed. Isoform 3 is expressed in the brain.1 Publication

Gene expression databases

BgeeiQ8C0J2.
CleanExiMM_ATG16L1.
ExpressionAtlasiQ8C0J2. baseline and differential.
GenevestigatoriQ8C0J2.

Interactioni

Subunit structurei

Interacts with TMEM59, TLR2 and NOD2 (By similarity). Homooligomer. Interacts with WIPI2, FIP200 and ATG5. Part of either the minor and major complexes respectively composed of 4 sets of ATG12-ATG5 and ATG16L1 (400 kDa) or 8 sets of ATG12-ATG5 and ATG16L1 (800 kDa). Interacts with RAB33B.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rb1cc1Q9ESK93EBI-769195,EBI-647302

Protein-protein interaction databases

BioGridi218476. 5 interactions.
DIPiDIP-31966N.
IntActiQ8C0J2. 4 interactions.
MINTiMINT-136268.

Structurei

3D structure databases

ProteinModelPortaliQ8C0J2.
SMRiQ8C0J2. Positions 267-604.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati320 – 35940WD 1PROSITE-ProRule annotationAdd
BLAST
Repeati364 – 40340WD 2PROSITE-ProRule annotationAdd
BLAST
Repeati406 – 44540WD 3PROSITE-ProRule annotationAdd
BLAST
Repeati447 – 48438WD 4PROSITE-ProRule annotationAdd
BLAST
Repeati486 – 52540WD 5PROSITE-ProRule annotationAdd
BLAST
Repeati532 – 57342WD 6PROSITE-ProRule annotationAdd
BLAST
Repeati575 – 60733WD 7PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni207 – 23024WIPI2-bindingBy similarityAdd
BLAST
Regioni230 – 24213FIP200-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili79 – 230152Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi296 – 2994Caspase cleavage

Sequence similaritiesi

Belongs to the WD repeat ATG16 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000118869.
HOVERGENiHBG050534.
InParanoidiQ8C0J2.
KOiK17890.
OMAiLETECQE.
OrthoDBiEOG70CR6M.
PhylomeDBiQ8C0J2.
TreeFamiTF315541.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR013923. Autophagy-rel_prot_16.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08614. ATG16. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8C0J2-1) [UniParc]FASTAAdd to Basket

Also known as: Apg16Lbeta

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
MSSGLRAADF PRWKRHIAEE LRRRDRLQRQ AFEEIILQYT KLLEKSDLHS
60 70 80 90 100
VLTQKLQAEK HDMPNRHEIS PGHDGAWNDS QLQEMAQLRI KHQEELTELH
110 120 130 140 150
KKRGELAQLV IDLNNQMQQK DKEIQMNEAK ISEYLQTISD LETNCLDLRT
160 170 180 190 200
KLQDLEVANQ TLKDEYDALQ ITFTALEEKL RKTTEENQEL VTRWMAEKAQ
210 220 230 240 250
EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI EVIVDETSDH
260 270 280 290 300
TEETSPVRAV SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS IPVPQDIMDT
310 320 330 340 350
HPASGKDVRV PTTASYVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE
360 370 380 390 400
AFGDKCEFKG SLSGSNAGIT SIEFDSAGAY LLAASNDFAS RIWTVDDYRL
410 420 430 440 450
RHTLTGHSGK VLSAKFLLDN ARIVSGSHDR TLKLWDLRSK VCIKTVFAGS
460 470 480 490 500
SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES VVREMELLGK ITALDLNPER
510 520 530 540 550
TELLSCSRDD LLKVIDLRTN AVKQTFSAPG FKCGSDWTRV VFSPDGSYVA
560 570 580 590 600
AGSAEGSLYV WSVLTGKVEK VLSKQHSSSI NAVAWAPSGL HVVSVDKGSR

AVLWAQP
Length:607
Mass (Da):68,172
Last modified:March 1, 2003 - v1
Checksum:i63920320883A69DF
GO
Isoform 2 (identifier: Q8C0J2-2) [UniParc]FASTAAdd to Basket

Also known as: Apg16Lalpha

The sequence of this isoform differs from the canonical sequence as follows:
     266-284: Missing.

Note: No experimental confirmation available.

Show »
Length:588
Mass (Da):66,203
Checksum:iCE2AB829A7911274
GO
Isoform 3 (identifier: Q8C0J2-3) [UniParc]FASTAAdd to Basket

Also known as: Apg16Lgamma

The sequence of this isoform differs from the canonical sequence as follows:
     284-284: G → GLSESPLLGHHSSDAAR

Show »
Length:623
Mass (Da):69,831
Checksum:i823453BB5D7DE6FE
GO
Isoform 4 (identifier: Q8C0J2-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     284-284: G → GLSESPLLGHHSSDAAR
     443-452: IKTVFAGSSC → EEMQSLCVFM
     453-607: Missing.

Note: No experimental confirmation available.

Show »
Length:468
Mass (Da):53,024
Checksum:iFFB7AC4AE34DF8F7
GO
Isoform 5 (identifier: Q8C0J2-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     266-284: Missing.
     442-442: C → CEEMQSLCVLMVFGFLSG

Note: No experimental confirmation available.

Show »
Length:605
Mass (Da):68,075
Checksum:iB0BB8DE0748401B6
GO

Sequence cautioni

The sequence BAD21370.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831Q → H in BAC55090. (PubMed:12665549)Curated
Sequence conflicti83 – 831Q → H in BAC55091. (PubMed:12665549)Curated
Sequence conflicti83 – 831Q → H in BAC55092. (PubMed:12665549)Curated
Sequence conflicti83 – 831Q → H in BAB23866. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei266 – 28419Missing in isoform 2 and isoform 5. 2 PublicationsVSP_013391Add
BLAST
Alternative sequencei284 – 2841G → GLSESPLLGHHSSDAAR in isoform 3 and isoform 4. 3 PublicationsVSP_013392
Alternative sequencei442 – 4421C → CEEMQSLCVLMVFGFLSG in isoform 5. 1 PublicationVSP_013393
Alternative sequencei443 – 45210IKTVFAGSSC → EEMQSLCVFM in isoform 4. 1 PublicationVSP_013394
Alternative sequencei453 – 607155Missing in isoform 4. 1 PublicationVSP_013395Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB087879 mRNA. Translation: BAC55090.1.
AB087880 mRNA. Translation: BAC55091.1.
AB087881 mRNA. Translation: BAC55092.1.
AK005181 mRNA. Translation: BAB23866.1.
AK030983 mRNA. Translation: BAC27201.1.
AK131120 Transcribed RNA. Translation: BAD21370.1. Different initiation.
BC049122 mRNA. Translation: AAH49122.1.
CCDSiCCDS15136.1. [Q8C0J2-1]
CCDS56637.1. [Q8C0J2-3]
CCDS56638.1. [Q8C0J2-2]
RefSeqiNP_001192320.1. NM_001205391.1. [Q8C0J2-3]
NP_084122.2. NM_029846.4. [Q8C0J2-1]
UniGeneiMm.272972.
Mm.456099.

Genome annotation databases

EnsembliENSMUST00000027512; ENSMUSP00000027512; ENSMUSG00000026289. [Q8C0J2-1]
ENSMUST00000113186; ENSMUSP00000108811; ENSMUSG00000026289. [Q8C0J2-2]
ENSMUST00000113190; ENSMUSP00000108815; ENSMUSG00000026289. [Q8C0J2-3]
GeneIDi77040.
KEGGimmu:77040.
UCSCiuc007bxl.2. mouse. [Q8C0J2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB087879 mRNA. Translation: BAC55090.1 .
AB087880 mRNA. Translation: BAC55091.1 .
AB087881 mRNA. Translation: BAC55092.1 .
AK005181 mRNA. Translation: BAB23866.1 .
AK030983 mRNA. Translation: BAC27201.1 .
AK131120 Transcribed RNA. Translation: BAD21370.1 . Different initiation.
BC049122 mRNA. Translation: AAH49122.1 .
CCDSi CCDS15136.1. [Q8C0J2-1 ]
CCDS56637.1. [Q8C0J2-3 ]
CCDS56638.1. [Q8C0J2-2 ]
RefSeqi NP_001192320.1. NM_001205391.1. [Q8C0J2-3 ]
NP_084122.2. NM_029846.4. [Q8C0J2-1 ]
UniGenei Mm.272972.
Mm.456099.

3D structure databases

ProteinModelPortali Q8C0J2.
SMRi Q8C0J2. Positions 267-604.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 218476. 5 interactions.
DIPi DIP-31966N.
IntActi Q8C0J2. 4 interactions.
MINTi MINT-136268.

PTM databases

PhosphoSitei Q8C0J2.

2D gel databases

REPRODUCTION-2DPAGE Q8C0J2.

Proteomic databases

MaxQBi Q8C0J2.
PaxDbi Q8C0J2.
PRIDEi Q8C0J2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027512 ; ENSMUSP00000027512 ; ENSMUSG00000026289 . [Q8C0J2-1 ]
ENSMUST00000113186 ; ENSMUSP00000108811 ; ENSMUSG00000026289 . [Q8C0J2-2 ]
ENSMUST00000113190 ; ENSMUSP00000108815 ; ENSMUSG00000026289 . [Q8C0J2-3 ]
GeneIDi 77040.
KEGGi mmu:77040.
UCSCi uc007bxl.2. mouse. [Q8C0J2-1 ]

Organism-specific databases

CTDi 55054.
MGIi MGI:1924290. Atg16l1.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00760000118869.
HOVERGENi HBG050534.
InParanoidi Q8C0J2.
KOi K17890.
OMAi LETECQE.
OrthoDBi EOG70CR6M.
PhylomeDBi Q8C0J2.
TreeFami TF315541.

Miscellaneous databases

NextBioi 346354.
PROi Q8C0J2.
SOURCEi Search...

Gene expression databases

Bgeei Q8C0J2.
CleanExi MM_ATG16L1.
ExpressionAtlasi Q8C0J2. baseline and differential.
Genevestigatori Q8C0J2.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR013923. Autophagy-rel_prot_16.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF08614. ATG16. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view ]
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00320. WD40. 7 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate."
    Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M., Takao T., Natsume T., Ohsumi Y., Yoshimori T.
    J. Cell Sci. 116:1679-1688(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ATG5.
  2. "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] (ISOFORMS 1 AND 4).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Thymus.
  3. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Fetal brain.
  4. "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 3).
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation."
    Itoh T., Fujita N., Kanno E., Yamamoto A., Yoshimori T., Fukuda M.
    Mol. Biol. Cell 19:2916-2925(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB33B.
  6. Cited for: SUBCELLULAR LOCATION.
  7. Cited for: FUNCTION IN AUTOPHAGY, CLEAVAGE BY CASP3, MUTAGENESIS OF ASP-299 AND THR-300.
  8. "WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and pathogen clearance by recruiting Atg12-5-16L1."
    Dooley H.C., Razi M., Polson H.E., Girardin S.E., Wilson M.I., Tooze S.A.
    Mol. Cell 55:238-252(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH WIPI2 AND FIP200, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiA16L1_MOUSE
AccessioniPrimary (citable) accession number: Q8C0J2
Secondary accession number(s): Q6KAT7
, Q80U97, Q80U98, Q80U99, Q80Y53, Q9DB63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 108 of the entry and version 1 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