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P50995 (ANX11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Annexin A11
Alternative name(s):
56 kDa autoantigen
Annexin XI
Annexin-11
Calcyclin-associated annexin 50
Short name=CAP-50
Gene names
Name:ANXA11
Synonyms:ANX11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds specifically to calcyclin in a calcium-dependent manner By similarity. Required for midbody formation and completion of the terminal phase of cytokinesis. Ref.7

Subunit structure

Interacts with S100A6 By similarity. Interacts with PDCD6 in a calcium-dependent manner. Interacts with KIF23 during cytokinesis. Ref.4 Ref.7 Ref.9

Subcellular location

Cytoplasm. Melanosome. Nucleus envelope. Nucleusnucleoplasm. Cytoplasmcytoskeletonspindle. Note: Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus By similarity. Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent. Ref.5 Ref.6 Ref.7 Ref.8

Domain

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

Sequence similarities

Belongs to the annexin family.

Contains 4 annexin repeats.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis, completion of separation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

phagocytosis

Inferred from expression pattern PubMed 9188810. Source: UniProtKB

response to calcium ion

Inferred from direct assay Ref.5PubMed 9188810. Source: UniProtKB

   Cellular_componentazurophil granule

Inferred from direct assay PubMed 9188810. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.5Ref.6Ref.1. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay Ref.7. Source: UniProtKB

nuclear envelope

Inferred from direct assay Ref.5Ref.7. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.5Ref.7Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

phagocytic vesicle

Inferred from direct assay PubMed 9188810. Source: UniProtKB

specific granule

Inferred from direct assay PubMed 9188810. Source: UniProtKB

spindle

Inferred from direct assay Ref.6Ref.7. Source: UniProtKB

   Molecular_functionMHC class II protein complex binding

Inferred from direct assay PubMed 20458337. Source: UniProt

S100 protein binding

Inferred from physical interaction PubMed 12577318PubMed 19724273. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

calcium-dependent phospholipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-dependent protein binding

Inferred from physical interaction Ref.4PubMed 12445460. Source: UniProtKB

phosphatidylethanolamine binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Annexin A11
PRO_0000067510

Regions

Repeat209 – 26961Annexin 1
Repeat281 – 34161Annexin 2
Repeat365 – 42561Annexin 3
Repeat440 – 50061Annexin 4

Amino acid modifications

Modified residue2481N6-acetyllysine Ref.10
Modified residue2551N6-acetyllysine Ref.10
Modified residue4791N6-acetyllysine Ref.10

Natural variations

Natural variant1911R → Q.
Corresponds to variant rs2229554 [ dbSNP | Ensembl ].
VAR_048259
Natural variant2301R → C.
Corresponds to variant rs1049550 [ dbSNP | Ensembl ].
VAR_012006
Natural variant4571I → V.
Corresponds to variant rs1802932 [ dbSNP | Ensembl ].
VAR_012007

Sequences

Sequence LengthMass (Da)Tools
P50995 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4ADCAC8F270BFEE4

FASTA50554,390
        10         20         30         40         50         60 
MSYPGYPPPP GGYPPAAPGG GPWGGAAYPP PPSMPPIGLD NVATYAGQFN QDYLSGMAAN 

        70         80         90        100        110        120 
MSGTFGGANM PNLYPGAPGA GYPPVPPGGF GQPPSAQQPV PPYGMYPPPG GNPPSRMPSY 

       130        140        150        160        170        180 
PPYPGAPVPG QPMPPPGQQP PGAYPGQPPV TYPGQPPVPL PGQQQPVPSY PGYPGSGTVT 

       190        200        210        220        230        240 
PAVPPTQFGS RGTITDAPGF DPLRDAEVLR KAMKGFGTDE QAIIDCLGSR SNKQRQQILL 

       250        260        270        280        290        300 
SFKTAYGKDL IKDLKSELSG NFEKTILALM KTPVLFDIYE IKEAIKGVGT DEACLIEILA 

       310        320        330        340        350        360 
SRSNEHIREL NRAYKAEFKK TLEEAIRSDT SGHFQRLLIS LSQGNRDEST NVDMSLAQRD 

       370        380        390        400        410        420 
AQELYAAGEN RLGTDESKFN AVLCSRSRAH LVAVFNEYQR MTGRDIEKSI CREMSGDLEE 

       430        440        450        460        470        480 
GMLAVVKCLK NTPAFFAERL NKAMRGAGTK DRTLIRIMVS RSETDLLDIR SEYKRMYGKS 

       490        500 
LYHDISGDTS GDYRKILLKI CGGND 

« Hide

References

« Hide 'large scale' references
[1]"The 56K autoantigen is identical to human annexin XI."
Misaki Y., Pruijn G.J.M., van der Kemp A.W., van Venrooij W.J.
J. Biol. Chem. 269:4240-4246(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Teratocarcinoma.
[2]"Annexin A11 (ANXA11) gene structure as the progenitor of paralogous annexins and source of orthologous cDNA isoforms."
Bances P., Fernandez M.R., Rodriguez-Garcia M.I., Morgan R.O., Fernandez M.-P.
Genomics 69:95-103(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Lymph.
[4]"ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner."
Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.
Biochem. Biophys. Res. Commun. 291:1166-1172(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6.
[5]"Calcium- and cell cycle-dependent association of annexin 11 with the nuclear envelope."
Tomas A., Moss S.E.
J. Biol. Chem. 278:20210-20216(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"Dissecting the cellular functions of annexin XI using recombinant human annexin XI-specific autoantibodies cloned by phage display."
Farnaes L., Ditzel H.J.
J. Biol. Chem. 278:33120-33126(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis."
Tomas A., Futter C., Moss S.E.
J. Cell Biol. 165:813-822(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF23.
[8]"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.
[9]"Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants."
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6.
[10]"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-248; LYS-255 AND LYS-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19605 mRNA. Translation: AAA19734.1.
AJ278463 mRNA. Translation: CAB94995.1.
AJ278464 mRNA. Translation: CAB94996.1.
AJ278465 mRNA. Translation: CAB94997.1.
BC007564 mRNA. Translation: AAH07564.1.
PIRA53152.
RefSeqNP_001148.1. NM_001157.2.
NP_001265336.1. NM_001278407.1.
NP_001265337.1. NM_001278408.1.
NP_001265338.1. NM_001278409.1.
NP_665875.1. NM_145868.1.
NP_665876.1. NM_145869.1.
UniGeneHs.530291.

3D structure databases

ProteinModelPortalP50995.
SMRP50995. Positions 197-505.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106808. 20 interactions.
IntActP50995. 8 interactions.
MINTMINT-4998941.
STRING9606.ENSP00000265447.

PTM databases

PhosphoSiteP50995.

Polymorphism databases

DMDM1703322.

2D gel databases

REPRODUCTION-2DPAGEP50995.

Proteomic databases

PaxDbP50995.
PeptideAtlasP50995.
PRIDEP50995.

Protocols and materials databases

DNASU311.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265447; ENSP00000265447; ENSG00000122359.
ENST00000360615; ENSP00000353827; ENSG00000122359.
ENST00000372231; ENSP00000361305; ENSG00000122359.
ENST00000422982; ENSP00000404412; ENSG00000122359.
ENST00000438331; ENSP00000398610; ENSG00000122359.
ENST00000535999; ENSP00000441748; ENSG00000122359.
GeneID311.
KEGGhsa:311.
UCSCuc001kbq.1. human.

Organism-specific databases

CTD311.
GeneCardsGC10M081904.
HGNCHGNC:535. ANXA11.
HPACAB004851.
HPA027545.
MIM602572. gene.
neXtProtNX_P50995.
PharmGKBPA24825.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267770.
HOVERGENHBG061815.
InParanoidP50995.
KOK17095.
OMANMYPGAP.
OrthoDBEOG74XS72.
PhylomeDBP50995.
TreeFamTF105452.

Gene expression databases

ArrayExpressP50995.
BgeeP50995.
CleanExHS_ANXA11.
GenevestigatorP50995.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR008157. AnnexinXI.
[Graphical view]
PANTHERPTHR10502:SF29. PTHR10502:SF29. 1 hit.
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR01810. ANNEXINXI.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANXA11. human.
GeneWikiANXA11.
GenomeRNAi311.
NextBio1259.
PROP50995.
SOURCESearch...

Entry information

Entry nameANX11_HUMAN
AccessionPrimary (citable) accession number: P50995
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 127 of the entry and version 1 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM