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Protein

Annexin A6

Gene

Anxa6

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

Functioni

May associate with CD21. May regulate the release of Ca2+ from intracellular stores.

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: MGI
  2. calcium-dependent protein binding Source: MGI
  3. calcium ion binding Source: InterPro
  4. cholesterol binding Source: MGI
  5. GTP binding Source: MGI
  6. ligand-gated ion channel activity Source: MGI
  7. lipid binding Source: MGI
  8. protein homodimerization activity Source: MGI

GO - Biological processi

  1. apoptotic signaling pathway Source: CACAO
  2. calcium ion transport Source: MGI
  3. ion transmembrane transport Source: MGI
  4. mitochondrial calcium ion homeostasis Source: CACAO
  5. protein homooligomerization Source: MGI
  6. regulation of muscle contraction Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A6
Alternative name(s):
67 kDa calelectrin
Annexin VI
Annexin-6
Calphobindin-II
Short name:
CPB-II
Chromobindin-20
Lipocortin VI
Protein III
p68
p70
Gene namesi
Name:Anxa6
Synonyms:Anx6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:88255. Anxa6.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Melanosome By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. focal adhesion Source: MGI
  3. late endosome membrane Source: MGI
  4. lysosomal membrane Source: MGI
  5. melanosome Source: UniProtKB-SubCell
  6. membrane Source: MGI
  7. perinuclear region of cytoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 673672Annexin A6PRO_0000067495Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei30 – 301Phosphotyrosine1 Publication
Modified residuei63 – 631N6-acetyllysineBy similarity
Modified residuei68 – 681N6-acetyllysineBy similarity
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei81 – 811N6-acetyllysineBy similarity
Modified residuei201 – 2011Phosphotyrosine1 Publication
Modified residuei306 – 3061N6-acetyllysineBy similarity
Modified residuei370 – 3701N6-acetyllysineBy similarity
Modified residuei418 – 4181N6-acetyllysineBy similarity
Modified residuei483 – 4831N6-acetyllysineBy similarity
Modified residuei537 – 5371PhosphoserineBy similarity
Modified residuei620 – 6201N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14824.
PaxDbiP14824.
PRIDEiP14824.

PTM databases

PhosphoSiteiP14824.

Expressioni

Gene expression databases

BgeeiP14824.
CleanExiMM_ANXA6.
ExpressionAtlasiP14824. baseline and differential.
GenevestigatoriP14824.

Interactioni

Protein-protein interaction databases

BioGridi198112. 4 interactions.
IntActiP14824. 3 interactions.
MINTiMINT-1862250.

Structurei

3D structure databases

ProteinModelPortaliP14824.
SMRiP14824. Positions 10-673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati29 – 8961Annexin 1Add
BLAST
Repeati101 – 16161Annexin 2Add
BLAST
Repeati185 – 24561Annexin 3Add
BLAST
Repeati260 – 32061Annexin 4Add
BLAST
Repeati372 – 43261Annexin 5Add
BLAST
Repeati444 – 50461Annexin 6Add
BLAST
Repeati533 – 59361Annexin 7Add
BLAST
Repeati608 – 66861Annexin 8Add
BLAST

Domaini

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Sequence similaritiesi

Belongs to the annexin family.Curated
Contains 8 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiNOG267770.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP14824.
KOiK17094.
OMAiEKSLYSM.
OrthoDBiEOG74XS72.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 8 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002393. AnnexinVI.
[Graphical view]
PANTHERiPTHR10502:SF19. PTHR10502:SF19. 1 hit.
PfamiPF00191. Annexin. 8 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00202. ANNEXINVI.
SMARTiSM00335. ANX. 8 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14824-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIAQGAMY RGSVHDFPEF DANQDAEALY TAMKGFGSDK ESILELITSR
60 70 80 90 100
SNKQRQEICQ NYKSLYGKDL IEDLKYELTG KFERLIVNLM RPLAYCDAKE
110 120 130 140 150
IKDAISGVGT DEKCLIEILA SRTNEQMHQL VAAYKDAYER DLESDIIGDT
160 170 180 190 200
SGHFQKMLVV LLQGTRENDD VVSEDLVQQD VQDLYEAGEL KWGTDEAQFI
210 220 230 240 250
YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK LMLAVVKCIR
260 270 280 290 300
STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS
310 320 330 340 350
LYSMIKNDTS GEYKKALLKL CGGDDDAAGQ FFPEAAQVAY QMWELSAVSR
360 370 380 390 400
VELKGTVCAA NDFNPDADAK ALRKAMKGIG TDEATIIDIV THRSNAQRQQ
410 420 430 440 450
IRQTFKSHFG RDLMADLKSE ISGDLARLIL GLMMPPAHYD AKQLKKAMEG
460 470 480 490 500
AGTDEKTLIE ILATRTNAEI RAINEAYKED YHKSLEDALS SDTSGHFRRI
510 520 530 540 550
LISLATGNRE EGGENRDQAQ EDAQVAAEIL EIADTPSGDK TSLETRFMTV
560 570 580 590 600
LCTRSYPHLR RVFQEFIKKT NYDIEHVIKK EMSGDVKDAF VAIVQSVKNK
610 620 630 640 650
PLFFADKLYK SMKGAGTDEK TLTRVMVSRS EIDLLNIRRE FIEKYDKSLH
660 670
QAIEGDTSGD FMKALLALCG GED
Length:673
Mass (Da):75,885
Last modified:July 27, 2011 - v3
Checksum:iDCC5FC56CBD88809
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611N → S in CAA31808 (PubMed:2972541).Curated
Sequence conflicti108 – 1081V → I in CAA31808 (PubMed:2972541).Curated
Sequence conflicti329 – 3291G → A in CAA31808 (PubMed:2972541).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13460 mRNA. Translation: CAA31808.1.
AK030728 mRNA. Translation: BAC27101.1.
AK146509 mRNA. Translation: BAE27222.1.
AK146592 mRNA. Translation: BAE27287.1.
CCDSiCCDS24705.1.
PIRiS01786.
RefSeqiNP_001103681.1. NM_001110211.1.
NP_038500.2. NM_013472.4.
UniGeneiMm.265347.

Genome annotation databases

EnsembliENSMUST00000108883; ENSMUSP00000104511; ENSMUSG00000018340.
GeneIDi11749.
KEGGimmu:11749.
UCSCiuc007iyr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13460 mRNA. Translation: CAA31808.1.
AK030728 mRNA. Translation: BAC27101.1.
AK146509 mRNA. Translation: BAE27222.1.
AK146592 mRNA. Translation: BAE27287.1.
CCDSiCCDS24705.1.
PIRiS01786.
RefSeqiNP_001103681.1. NM_001110211.1.
NP_038500.2. NM_013472.4.
UniGeneiMm.265347.

3D structure databases

ProteinModelPortaliP14824.
SMRiP14824. Positions 10-673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198112. 4 interactions.
IntActiP14824. 3 interactions.
MINTiMINT-1862250.

PTM databases

PhosphoSiteiP14824.

Proteomic databases

MaxQBiP14824.
PaxDbiP14824.
PRIDEiP14824.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108883; ENSMUSP00000104511; ENSMUSG00000018340.
GeneIDi11749.
KEGGimmu:11749.
UCSCiuc007iyr.2. mouse.

Organism-specific databases

CTDi309.
MGIiMGI:88255. Anxa6.

Phylogenomic databases

eggNOGiNOG267770.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP14824.
KOiK17094.
OMAiEKSLYSM.
OrthoDBiEOG74XS72.
TreeFamiTF105452.

Miscellaneous databases

NextBioi279489.
PROiP14824.
SOURCEiSearch...

Gene expression databases

BgeeiP14824.
CleanExiMM_ANXA6.
ExpressionAtlasiP14824. baseline and differential.
GenevestigatoriP14824.

Family and domain databases

Gene3Di1.10.220.10. 8 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002393. AnnexinVI.
[Graphical view]
PANTHERiPTHR10502:SF19. PTHR10502:SF19. 1 hit.
PfamiPF00191. Annexin. 8 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00202. ANNEXINVI.
SMARTiSM00335. ANX. 8 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of murine p68, a Ca2+-binding protein of the lipocortin family."
    Moss S.E., Crompton M.R., Crumpton M.J.
    Eur. J. Biochem. 177:21-27(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  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].
    Strain: C57BL/6J.
    Tissue: Embryo and Heart.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 35-50; 69-81; 123-135; 282-290; 378-393; 457-465; 484-498; 500-509 AND 630-638, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  5. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-620, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiANXA6_MOUSE
AccessioniPrimary (citable) accession number: P14824
Secondary accession number(s): Q8BSS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: April 29, 2015
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Seems to bind one calcium ion with high affinity.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

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 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.