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P08133 (ANXA6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ANXA6
Synonyms:ANX6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Cytoplasm By similarity. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.10

Induction

By Epstein-Barr virus (EBV).

Domain

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

Post-translational modification

Phosphorylated in response to growth factor stimulation.

Miscellaneous

Seems to bind one calcium ion with high affinity.

Sequence similarities

Belongs to the annexin family.

Contains 8 annexin repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08133-1)

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: P08133-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.14
Chain2 – 673672Annexin A6
PRO_0000067494

Regions

Repeat29 – 8961Annexin 1
Repeat101 – 16161Annexin 2
Repeat185 – 24561Annexin 3
Repeat260 – 32061Annexin 4
Repeat372 – 43261Annexin 5
Repeat444 – 50461Annexin 6
Repeat533 – 59361Annexin 7
Repeat608 – 66861Annexin 8

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.14
Modified residue301Phosphotyrosine Ref.11
Modified residue631N6-acetyllysine Ref.12
Modified residue681N6-acetyllysine Ref.12
Modified residue751N6-acetyllysine Ref.12
Modified residue811N6-acetyllysine Ref.12
Modified residue2011Phosphotyrosine By similarity
Modified residue3061N6-acetyllysine Ref.12
Modified residue3701N6-acetyllysine Ref.12
Modified residue4181N6-acetyllysine Ref.12
Modified residue4831N6-acetyllysine Ref.12
Modified residue6201N6-acetyllysine Ref.12

Natural variations

Alternative sequence1 – 3232Missing in isoform 2.
VSP_045480

Experimental info

Sequence conflict2211T → A in BAH13893. Ref.4
Sequence conflict226 – 2272IE → MK in AAA35656. Ref.2
Sequence conflict2481C → R in BAC86715. Ref.4
Sequence conflict5551S → T in AAA35656. Ref.2
Sequence conflict6191E → D in CAA68286. Ref.1

Secondary structure

................................................................................................. 673
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 90F47474F7F6D7B6

FASTA67375,873
        10         20         30         40         50         60 
MAKPAQGAKY RGSIHDFPGF DPNQDAEALY TAMKGFGSDK EAILDIITSR SNRQRQEVCQ 

        70         80         90        100        110        120 
SYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYCDAKE IKDAISGIGT DEKCLIEILA 

       130        140        150        160        170        180 
SRTNEQMHQL VAAYKDAYER DLEADIIGDT SGHFQKMLVV LLQGTREEDD VVSEDLVQQD 

       190        200        210        220        230        240 
VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK 

       250        260        270        280        290        300 
LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS 

       310        320        330        340        350        360 
LYSMIKNDTS GEYKKTLLKL SGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA 

       370        380        390        400        410        420 
NDFNPDADAK ALRKAMKGLG TDEDTIIDII THRSNVQRQQ IRQTFKSHFG RDLMTDLKSE 

       430        440        450        460        470        480 
ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI RAINEAYKED 

       490        500        510        520        530        540 
YHKSLEDALS SDTSGHFRRI LISLATGHRE EGGENLDQAR EDAQVAAEIL EIADTPSGDK 

       550        560        570        580        590        600 
TSLETRFMTI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDAF VAIVQSVKNK 

       610        620        630        640        650        660 
PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD 

       670 
FLKALLALCG GED 

« Hide

Isoform 2 [UniParc].

Checksum: 61E3E5CAF66A51E3
Show »

FASTA64172,423

References

« Hide 'large scale' references
[1]"Primary structure of the human, membrane-associated Ca2+-binding protein p68 a novel member of a protein family."
Crompton M.R., Owens R.J., Totty N.F., Moss S.E., Waterfield M.D., Crumpton M.J.
EMBO J. 7:21-27(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins."
Suedhof T.C., Slaughter C.A., Leznicki I., Barjon P., Reynolds G.A.
Proc. Natl. Acad. Sci. U.S.A. 85:664-668(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[3]"Structure and expression of cDNA for calphobindin II, a human placental coagulation inhibitor."
Iwasaki A., Suda M., Watanabe M., Nakao H., Hattori Y., Nagoya T., Saino Y., Shidara Y., Maki M.
J. Biochem. 106:43-49(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Amygdala and Thymus.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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).
Tissue: Uterus.
[8]"Structure and properties of calphobindin II, an anticoagulant protein from human placenta."
Yoshizaki H., Mizoguchi T., Arai K., Shiratsuchi M., Shidara Y., Maki M.
J. Biochem. 107:43-50(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-673.
[9]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 485-499.
Tissue: Adipocyte.
[10]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-68; LYS-75; LYS-81; LYS-306; LYS-370; LYS-418; LYS-483 AND LYS-620, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"The structure of recombinant human annexin VI in crystals and membrane-bound."
Benz J., Bergner A., Hofmann A., Demange P., Goettig P., Liemann S., Huber R., Voges D.
J. Mol. Biol. 260:638-643(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00097 mRNA. Translation: CAA68286.1.
J03578 mRNA. Translation: AAA35656.1.
D00510 mRNA. Translation: BAA00400.1.
AK126836 mRNA. Translation: BAC86715.1. Sequence problems.
AK303078 mRNA. Translation: BAH13893.1.
AC008641 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61684.1.
CH471062 Genomic DNA. Translation: EAW61686.1.
BC017046 mRNA. Translation: AAH17046.1.
PIRAQHU68. JU0032.
RefSeqNP_001146.2. NM_001155.4.
NP_001180473.1. NM_001193544.1.
UniGeneHs.412117.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M9IX-ray2.65A2-673[»]
ProteinModelPortalP08133.
SMRP08133. Positions 10-673.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106806. 27 interactions.
IntActP08133. 10 interactions.
MINTMINT-4999263.
STRING9606.ENSP00000346550.

Protein family/group databases

TCDB1.A.31.1.2. the annexin (annexin) family.

PTM databases

PhosphoSiteP08133.

2D gel databases

REPRODUCTION-2DPAGEIPI00221226.
UCD-2DPAGEP08133.

Proteomic databases

PaxDbP08133.
PRIDEP08133.

Protocols and materials databases

DNASU309.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354546; ENSP00000346550; ENSG00000197043. [P08133-1]
ENST00000523714; ENSP00000430517; ENSG00000197043. [P08133-2]
GeneID309.
KEGGhsa:309.
UCSCuc003ltl.2. human. [P08133-1]

Organism-specific databases

CTD309.
GeneCardsGC05M150460.
HGNCHGNC:544. ANXA6.
HPACAB005077.
HPA002462.
HPA009650.
MIM114070. gene.
neXtProtNX_P08133.
PharmGKBPA24834.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267770.
HOGENOMHOG000158803.
HOVERGENHBG061815.
InParanoidP08133.
KOK17094.
OMAEKSLYSM.
OrthoDBEOG74XS72.
PhylomeDBP08133.
TreeFamTF105452.

Gene expression databases

ArrayExpressP08133.
BgeeP08133.
CleanExHS_ANXA6.
GenevestigatorP08133.

Family and domain databases

Gene3D1.10.220.10. 8 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002393. AnnexinVI.
[Graphical view]
PfamPF00191. Annexin. 8 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00202. ANNEXINVI.
SMARTSM00335. ANX. 8 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANXA6. human.
EvolutionaryTraceP08133.
GeneWikiANXA6.
GenomeRNAi309.
NextBio1247.
PROP08133.
SOURCESearch...

Entry information

Entry nameANXA6_HUMAN
AccessionPrimary (citable) accession number: P08133
Secondary accession number(s): B7Z8A7 expand/collapse secondary AC list , D3DQH4, E9PGK1, Q6ZT79
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM