Full text data of ANXA11
ANXA11
(ANX11)
[Confidence: low (only semi-automatic identification from reviews)]
Annexin A11 (56 kDa autoantigen; Annexin XI; Annexin-11; Calcyclin-associated annexin 50; CAP-50)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Annexin A11 (56 kDa autoantigen; Annexin XI; Annexin-11; Calcyclin-associated annexin 50; CAP-50)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P50995
ID ANX11_HUMAN Reviewed; 505 AA.
AC P50995;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Annexin A11;
DE AltName: Full=56 kDa autoantigen;
DE AltName: Full=Annexin XI;
DE AltName: Full=Annexin-11;
DE AltName: Full=Calcyclin-associated annexin 50;
DE Short=CAP-50;
GN Name=ANXA11; Synonyms=ANX11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=7508441;
RA Misaki Y., Pruijn G.J.M., van der Kemp A.W., van Venrooij W.J.;
RT "The 56K autoantigen is identical to human annexin XI.";
RL J. Biol. Chem. 269:4240-4246(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11013079; DOI=10.1006/geno.2000.6309;
RA Bances P., Fernandez M.R., Rodriguez-Garcia M.I., Morgan R.O.,
RA Fernandez M.-P.;
RT "Annexin A11 (ANXA11) gene structure as the progenitor of paralogous
RT annexins and source of orthologous cDNA isoforms.";
RL Genomics 69:95-103(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH PDCD6.
RX PubMed=11883939; DOI=10.1006/bbrc.2002.6600;
RA Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.;
RT "ALG-2 interacts with the amino-terminal domain of annexin XI in a
RT Ca(2+)-dependent manner.";
RL Biochem. Biophys. Res. Commun. 291:1166-1172(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12601007; DOI=10.1074/jbc.M212669200;
RA Tomas A., Moss S.E.;
RT "Calcium- and cell cycle-dependent association of annexin 11 with the
RT nuclear envelope.";
RL J. Biol. Chem. 278:20210-20216(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12805373; DOI=10.1074/jbc.M210852200;
RA Farnaes L., Ditzel H.J.;
RT "Dissecting the cellular functions of annexin XI using recombinant
RT human annexin XI-specific autoantibodies cloned by phage display.";
RL J. Biol. Chem. 278:33120-33126(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF23.
RX PubMed=15197175; DOI=10.1083/jcb.200311054;
RA Tomas A., Futter C., Moss S.E.;
RT "Annexin 11 is required for midbody formation and completion of the
RT terminal phase of cytokinesis.";
RL J. Cell Biol. 165:813-822(2004).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [9]
RP INTERACTION WITH PDCD6.
RX PubMed=18256029; DOI=10.1074/jbc.M800717200;
RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA Maki M.;
RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in
RT human phospholipid scramblase 3: differential binding to an
RT alternatively spliced isoform and amino acid-substituted mutants.";
RL J. Biol. Chem. 283:9623-9632(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-248; LYS-255 AND LYS-479,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binds specifically to calcyclin in a calcium-dependent
CC manner (By similarity). Required for midbody formation and
CC completion of the terminal phase of cytokinesis.
CC -!- SUBUNIT: Interacts with S100A6 (By similarity). Interacts with
CC PDCD6 in a calcium-dependent manner. Interacts with KIF23 during
CC cytokinesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Nucleus envelope.
CC Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Note=Found
CC throughout the nucleoplasm at interphase and during mitosis
CC concentrates around the mitotic apparatus (By similarity).
CC Elevation of intracellular calcium causes relocalization from the
CC nucleoplasm to the nuclear envelope, with little effect on the
CC cytoplasmic pool. Localization to the nuclear envelope is cell-
CC cycle dependent.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for
CC calcium and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin family.
CC -!- SIMILARITY: Contains 4 annexin repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L19605; AAA19734.1; -; mRNA.
DR EMBL; AJ278463; CAB94995.1; -; mRNA.
DR EMBL; AJ278464; CAB94996.1; -; mRNA.
DR EMBL; AJ278465; CAB94997.1; -; mRNA.
DR EMBL; BC007564; AAH07564.1; -; mRNA.
DR PIR; A53152; A53152.
DR RefSeq; NP_001148.1; NM_001157.2.
DR RefSeq; NP_001265336.1; NM_001278407.1.
DR RefSeq; NP_001265337.1; NM_001278408.1.
DR RefSeq; NP_001265338.1; NM_001278409.1.
DR RefSeq; NP_665875.1; NM_145868.1.
DR RefSeq; NP_665876.1; NM_145869.1.
DR UniGene; Hs.530291; -.
DR ProteinModelPortal; P50995; -.
DR SMR; P50995; 197-505.
DR IntAct; P50995; 8.
DR MINT; MINT-4998941; -.
DR STRING; 9606.ENSP00000265447; -.
DR PhosphoSite; P50995; -.
DR DMDM; 1703322; -.
DR REPRODUCTION-2DPAGE; P50995; -.
DR PaxDb; P50995; -.
DR PeptideAtlas; P50995; -.
DR PRIDE; P50995; -.
DR DNASU; 311; -.
DR Ensembl; ENST00000265447; ENSP00000265447; ENSG00000122359.
DR Ensembl; ENST00000360615; ENSP00000353827; ENSG00000122359.
DR Ensembl; ENST00000372231; ENSP00000361305; ENSG00000122359.
DR Ensembl; ENST00000422982; ENSP00000404412; ENSG00000122359.
DR Ensembl; ENST00000438331; ENSP00000398610; ENSG00000122359.
DR Ensembl; ENST00000535999; ENSP00000441748; ENSG00000122359.
DR GeneID; 311; -.
DR KEGG; hsa:311; -.
DR UCSC; uc001kbq.1; human.
DR CTD; 311; -.
DR GeneCards; GC10M081904; -.
DR HGNC; HGNC:535; ANXA11.
DR HPA; CAB004851; -.
DR HPA; HPA027545; -.
DR MIM; 602572; gene.
DR neXtProt; NX_P50995; -.
DR PharmGKB; PA24825; -.
DR eggNOG; NOG267770; -.
DR HOVERGEN; HBG061815; -.
DR InParanoid; P50995; -.
DR KO; K17095; -.
DR OMA; NMYPGAP; -.
DR OrthoDB; EOG74XS72; -.
DR ChiTaRS; ANXA11; human.
DR GeneWiki; ANXA11; -.
DR GenomeRNAi; 311; -.
DR NextBio; 1259; -.
DR PRO; PR:P50995; -.
DR ArrayExpress; P50995; -.
DR Bgee; P50995; -.
DR CleanEx; HS_ANXA11; -.
DR Genevestigator; P50995; -.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IEA:Ensembl.
DR GO; GO:0007109; P:cytokinesis, completion of separation; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEP:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR008157; AnnexinXI.
DR PANTHER; PTHR10502:SF29; PTHR10502:SF29; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01810; ANNEXINXI.
DR SMART; SM00335; ANX; 4.
DR PROSITE; PS00223; ANNEXIN; 4.
PE 1: Evidence at protein level;
KW Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
KW Nucleus; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 505 Annexin A11.
FT /FTId=PRO_0000067510.
FT REPEAT 209 269 Annexin 1.
FT REPEAT 281 341 Annexin 2.
FT REPEAT 365 425 Annexin 3.
FT REPEAT 440 500 Annexin 4.
FT MOD_RES 248 248 N6-acetyllysine.
FT MOD_RES 255 255 N6-acetyllysine.
FT MOD_RES 479 479 N6-acetyllysine.
FT VARIANT 191 191 R -> Q (in dbSNP:rs2229554).
FT /FTId=VAR_048259.
FT VARIANT 230 230 R -> C (in dbSNP:rs1049550).
FT /FTId=VAR_012006.
FT VARIANT 457 457 I -> V (in dbSNP:rs1802932).
FT /FTId=VAR_012007.
SQ SEQUENCE 505 AA; 54390 MW; 4ADCAC8F270BFEE4 CRC64;
MSYPGYPPPP GGYPPAAPGG GPWGGAAYPP PPSMPPIGLD NVATYAGQFN QDYLSGMAAN
MSGTFGGANM PNLYPGAPGA GYPPVPPGGF GQPPSAQQPV PPYGMYPPPG GNPPSRMPSY
PPYPGAPVPG QPMPPPGQQP PGAYPGQPPV TYPGQPPVPL PGQQQPVPSY PGYPGSGTVT
PAVPPTQFGS RGTITDAPGF DPLRDAEVLR KAMKGFGTDE QAIIDCLGSR SNKQRQQILL
SFKTAYGKDL IKDLKSELSG NFEKTILALM KTPVLFDIYE IKEAIKGVGT DEACLIEILA
SRSNEHIREL NRAYKAEFKK TLEEAIRSDT SGHFQRLLIS LSQGNRDEST NVDMSLAQRD
AQELYAAGEN RLGTDESKFN AVLCSRSRAH LVAVFNEYQR MTGRDIEKSI CREMSGDLEE
GMLAVVKCLK NTPAFFAERL NKAMRGAGTK DRTLIRIMVS RSETDLLDIR SEYKRMYGKS
LYHDISGDTS GDYRKILLKI CGGND
//
ID ANX11_HUMAN Reviewed; 505 AA.
AC P50995;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Annexin A11;
DE AltName: Full=56 kDa autoantigen;
DE AltName: Full=Annexin XI;
DE AltName: Full=Annexin-11;
DE AltName: Full=Calcyclin-associated annexin 50;
DE Short=CAP-50;
GN Name=ANXA11; Synonyms=ANX11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=7508441;
RA Misaki Y., Pruijn G.J.M., van der Kemp A.W., van Venrooij W.J.;
RT "The 56K autoantigen is identical to human annexin XI.";
RL J. Biol. Chem. 269:4240-4246(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11013079; DOI=10.1006/geno.2000.6309;
RA Bances P., Fernandez M.R., Rodriguez-Garcia M.I., Morgan R.O.,
RA Fernandez M.-P.;
RT "Annexin A11 (ANXA11) gene structure as the progenitor of paralogous
RT annexins and source of orthologous cDNA isoforms.";
RL Genomics 69:95-103(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH PDCD6.
RX PubMed=11883939; DOI=10.1006/bbrc.2002.6600;
RA Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.;
RT "ALG-2 interacts with the amino-terminal domain of annexin XI in a
RT Ca(2+)-dependent manner.";
RL Biochem. Biophys. Res. Commun. 291:1166-1172(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12601007; DOI=10.1074/jbc.M212669200;
RA Tomas A., Moss S.E.;
RT "Calcium- and cell cycle-dependent association of annexin 11 with the
RT nuclear envelope.";
RL J. Biol. Chem. 278:20210-20216(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12805373; DOI=10.1074/jbc.M210852200;
RA Farnaes L., Ditzel H.J.;
RT "Dissecting the cellular functions of annexin XI using recombinant
RT human annexin XI-specific autoantibodies cloned by phage display.";
RL J. Biol. Chem. 278:33120-33126(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF23.
RX PubMed=15197175; DOI=10.1083/jcb.200311054;
RA Tomas A., Futter C., Moss S.E.;
RT "Annexin 11 is required for midbody formation and completion of the
RT terminal phase of cytokinesis.";
RL J. Cell Biol. 165:813-822(2004).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [9]
RP INTERACTION WITH PDCD6.
RX PubMed=18256029; DOI=10.1074/jbc.M800717200;
RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA Maki M.;
RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in
RT human phospholipid scramblase 3: differential binding to an
RT alternatively spliced isoform and amino acid-substituted mutants.";
RL J. Biol. Chem. 283:9623-9632(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-248; LYS-255 AND LYS-479,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binds specifically to calcyclin in a calcium-dependent
CC manner (By similarity). Required for midbody formation and
CC completion of the terminal phase of cytokinesis.
CC -!- SUBUNIT: Interacts with S100A6 (By similarity). Interacts with
CC PDCD6 in a calcium-dependent manner. Interacts with KIF23 during
CC cytokinesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Nucleus envelope.
CC Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Note=Found
CC throughout the nucleoplasm at interphase and during mitosis
CC concentrates around the mitotic apparatus (By similarity).
CC Elevation of intracellular calcium causes relocalization from the
CC nucleoplasm to the nuclear envelope, with little effect on the
CC cytoplasmic pool. Localization to the nuclear envelope is cell-
CC cycle dependent.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for
CC calcium and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin family.
CC -!- SIMILARITY: Contains 4 annexin repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L19605; AAA19734.1; -; mRNA.
DR EMBL; AJ278463; CAB94995.1; -; mRNA.
DR EMBL; AJ278464; CAB94996.1; -; mRNA.
DR EMBL; AJ278465; CAB94997.1; -; mRNA.
DR EMBL; BC007564; AAH07564.1; -; mRNA.
DR PIR; A53152; A53152.
DR RefSeq; NP_001148.1; NM_001157.2.
DR RefSeq; NP_001265336.1; NM_001278407.1.
DR RefSeq; NP_001265337.1; NM_001278408.1.
DR RefSeq; NP_001265338.1; NM_001278409.1.
DR RefSeq; NP_665875.1; NM_145868.1.
DR RefSeq; NP_665876.1; NM_145869.1.
DR UniGene; Hs.530291; -.
DR ProteinModelPortal; P50995; -.
DR SMR; P50995; 197-505.
DR IntAct; P50995; 8.
DR MINT; MINT-4998941; -.
DR STRING; 9606.ENSP00000265447; -.
DR PhosphoSite; P50995; -.
DR DMDM; 1703322; -.
DR REPRODUCTION-2DPAGE; P50995; -.
DR PaxDb; P50995; -.
DR PeptideAtlas; P50995; -.
DR PRIDE; P50995; -.
DR DNASU; 311; -.
DR Ensembl; ENST00000265447; ENSP00000265447; ENSG00000122359.
DR Ensembl; ENST00000360615; ENSP00000353827; ENSG00000122359.
DR Ensembl; ENST00000372231; ENSP00000361305; ENSG00000122359.
DR Ensembl; ENST00000422982; ENSP00000404412; ENSG00000122359.
DR Ensembl; ENST00000438331; ENSP00000398610; ENSG00000122359.
DR Ensembl; ENST00000535999; ENSP00000441748; ENSG00000122359.
DR GeneID; 311; -.
DR KEGG; hsa:311; -.
DR UCSC; uc001kbq.1; human.
DR CTD; 311; -.
DR GeneCards; GC10M081904; -.
DR HGNC; HGNC:535; ANXA11.
DR HPA; CAB004851; -.
DR HPA; HPA027545; -.
DR MIM; 602572; gene.
DR neXtProt; NX_P50995; -.
DR PharmGKB; PA24825; -.
DR eggNOG; NOG267770; -.
DR HOVERGEN; HBG061815; -.
DR InParanoid; P50995; -.
DR KO; K17095; -.
DR OMA; NMYPGAP; -.
DR OrthoDB; EOG74XS72; -.
DR ChiTaRS; ANXA11; human.
DR GeneWiki; ANXA11; -.
DR GenomeRNAi; 311; -.
DR NextBio; 1259; -.
DR PRO; PR:P50995; -.
DR ArrayExpress; P50995; -.
DR Bgee; P50995; -.
DR CleanEx; HS_ANXA11; -.
DR Genevestigator; P50995; -.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IEA:Ensembl.
DR GO; GO:0007109; P:cytokinesis, completion of separation; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEP:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR008157; AnnexinXI.
DR PANTHER; PTHR10502:SF29; PTHR10502:SF29; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01810; ANNEXINXI.
DR SMART; SM00335; ANX; 4.
DR PROSITE; PS00223; ANNEXIN; 4.
PE 1: Evidence at protein level;
KW Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
KW Nucleus; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 505 Annexin A11.
FT /FTId=PRO_0000067510.
FT REPEAT 209 269 Annexin 1.
FT REPEAT 281 341 Annexin 2.
FT REPEAT 365 425 Annexin 3.
FT REPEAT 440 500 Annexin 4.
FT MOD_RES 248 248 N6-acetyllysine.
FT MOD_RES 255 255 N6-acetyllysine.
FT MOD_RES 479 479 N6-acetyllysine.
FT VARIANT 191 191 R -> Q (in dbSNP:rs2229554).
FT /FTId=VAR_048259.
FT VARIANT 230 230 R -> C (in dbSNP:rs1049550).
FT /FTId=VAR_012006.
FT VARIANT 457 457 I -> V (in dbSNP:rs1802932).
FT /FTId=VAR_012007.
SQ SEQUENCE 505 AA; 54390 MW; 4ADCAC8F270BFEE4 CRC64;
MSYPGYPPPP GGYPPAAPGG GPWGGAAYPP PPSMPPIGLD NVATYAGQFN QDYLSGMAAN
MSGTFGGANM PNLYPGAPGA GYPPVPPGGF GQPPSAQQPV PPYGMYPPPG GNPPSRMPSY
PPYPGAPVPG QPMPPPGQQP PGAYPGQPPV TYPGQPPVPL PGQQQPVPSY PGYPGSGTVT
PAVPPTQFGS RGTITDAPGF DPLRDAEVLR KAMKGFGTDE QAIIDCLGSR SNKQRQQILL
SFKTAYGKDL IKDLKSELSG NFEKTILALM KTPVLFDIYE IKEAIKGVGT DEACLIEILA
SRSNEHIREL NRAYKAEFKK TLEEAIRSDT SGHFQRLLIS LSQGNRDEST NVDMSLAQRD
AQELYAAGEN RLGTDESKFN AVLCSRSRAH LVAVFNEYQR MTGRDIEKSI CREMSGDLEE
GMLAVVKCLK NTPAFFAERL NKAMRGAGTK DRTLIRIMVS RSETDLLDIR SEYKRMYGKS
LYHDISGDTS GDYRKILLKI CGGND
//
MIM
602572
*RECORD*
*FIELD* NO
602572
*FIELD* TI
*602572 ANNEXIN A11; ANXA11
;;ANNEXIN XI; ANX11;;
AUTOANTIGEN, 56-KD
*FIELD* TX
DESCRIPTION
read more
ANXA11 is a member of the annexin family of calcium-dependent
phospholipid-binding proteins. Annexins have unique N-terminal domains
and homologous C-terminal domains containing the calcium-dependent
phospholipid-binding sites.
CLONING
To identify a 56-kD antigen recognized by sera from patients with
autoimmune diseases, Misaki et al. (1994) screened a human
teratocarcinoma cDNA expression library with the anti-56-kD antigen
autoantibodies. They isolated a cDNA predicting a 505-amino acid protein
with 60% identity to other annexins in the conserved C-terminal domain
and 92.5% identity to bovine annexin XI over the entire protein. Misaki
et al. (1994) concluded that the 56-kD autoantigen is human annexin XI,
or ANXA11.
GENE STRUCTURE
Bances et al. (2000) determined that the mouse Anxa11 gene contains 15
exons and spans 40 kB. Exon 1 is untranslated, and intron 1 spans about
20 kb. The human ANXA11 gene has the same general structure as the mouse
gene; however, EST database analysis indicated that human ANXA11
transcripts also use variably spliced exons 1b and 1c, which can
lengthen the 5-prime UTR. The intronic sequences of the mouse and human
ANXA11 genes contain several types of repetitive elements, including
retroviral long terminal repeats. The mouse promoter region contains a
remnant LINE-1 insertion not found in the human gene. The 5-prime
flanking region of the ANXA11 gene contains a CpG island and MYOD
(159970), SP1 (189906), and glucocorticoid response elements, but no
proximal TATA or CAAT boxes.
MOLECULAR GENETICS
For discussion of a possible association between variation in the ANXA11
gene and susceptibility to sarcoidosis, see SS3 (612388).
MAPPING
Morgan et al. (1998) mapped the ANXA11 gene to 10q22.3-q23.1 by
fluorescence in situ hybridization.
By genomic sequence analysis, Bances et al. (2000) mapped the mouse
Anxa11 gene to chromosome 14.
*FIELD* RF
1. Bances, P.; Fernandez, M.-R.; Rodriguez-Garcia, M.-I.; Morgan,
R. O.; Fernandez, M.-P.: Annexin A11 (ANXA11) gene structure as the
progenitor of paralogous annexins and source of orthologous cDNA isoforms. Genomics 69:
95-103, 2000.
2. Misaki, Y.; Pruijn, G. J. M.; van der Kemp, A. W. C. M.; van Venrooij,
W. J.: The 56K autoantigen is identical to human annexin XI. J.
Biol. Chem. 269: 4240-4246, 1994.
3. Morgan, R. O.; Bell, D. W.; Testa, J. R.; Fernandez, M. P.: Genomic
locations of ANX11 and ANX13 and the evolutionary genetics of human
annexins. Genomics 48: 100-110, 1998.
*FIELD* CN
Ada Hamosh - updated: 10/22/2008
Patricia A. Hartz - updated: 6/7/2005
*FIELD* CD
Rebekah S. Rasooly: 4/27/1998
*FIELD* ED
carol: 11/30/2009
carol: 6/16/2009
terry: 6/12/2009
terry: 10/22/2008
wwang: 6/22/2005
wwang: 6/17/2005
terry: 6/7/2005
carol: 8/4/2003
mgross: 9/17/1999
psherman: 4/27/1998
*RECORD*
*FIELD* NO
602572
*FIELD* TI
*602572 ANNEXIN A11; ANXA11
;;ANNEXIN XI; ANX11;;
AUTOANTIGEN, 56-KD
*FIELD* TX
DESCRIPTION
read more
ANXA11 is a member of the annexin family of calcium-dependent
phospholipid-binding proteins. Annexins have unique N-terminal domains
and homologous C-terminal domains containing the calcium-dependent
phospholipid-binding sites.
CLONING
To identify a 56-kD antigen recognized by sera from patients with
autoimmune diseases, Misaki et al. (1994) screened a human
teratocarcinoma cDNA expression library with the anti-56-kD antigen
autoantibodies. They isolated a cDNA predicting a 505-amino acid protein
with 60% identity to other annexins in the conserved C-terminal domain
and 92.5% identity to bovine annexin XI over the entire protein. Misaki
et al. (1994) concluded that the 56-kD autoantigen is human annexin XI,
or ANXA11.
GENE STRUCTURE
Bances et al. (2000) determined that the mouse Anxa11 gene contains 15
exons and spans 40 kB. Exon 1 is untranslated, and intron 1 spans about
20 kb. The human ANXA11 gene has the same general structure as the mouse
gene; however, EST database analysis indicated that human ANXA11
transcripts also use variably spliced exons 1b and 1c, which can
lengthen the 5-prime UTR. The intronic sequences of the mouse and human
ANXA11 genes contain several types of repetitive elements, including
retroviral long terminal repeats. The mouse promoter region contains a
remnant LINE-1 insertion not found in the human gene. The 5-prime
flanking region of the ANXA11 gene contains a CpG island and MYOD
(159970), SP1 (189906), and glucocorticoid response elements, but no
proximal TATA or CAAT boxes.
MOLECULAR GENETICS
For discussion of a possible association between variation in the ANXA11
gene and susceptibility to sarcoidosis, see SS3 (612388).
MAPPING
Morgan et al. (1998) mapped the ANXA11 gene to 10q22.3-q23.1 by
fluorescence in situ hybridization.
By genomic sequence analysis, Bances et al. (2000) mapped the mouse
Anxa11 gene to chromosome 14.
*FIELD* RF
1. Bances, P.; Fernandez, M.-R.; Rodriguez-Garcia, M.-I.; Morgan,
R. O.; Fernandez, M.-P.: Annexin A11 (ANXA11) gene structure as the
progenitor of paralogous annexins and source of orthologous cDNA isoforms. Genomics 69:
95-103, 2000.
2. Misaki, Y.; Pruijn, G. J. M.; van der Kemp, A. W. C. M.; van Venrooij,
W. J.: The 56K autoantigen is identical to human annexin XI. J.
Biol. Chem. 269: 4240-4246, 1994.
3. Morgan, R. O.; Bell, D. W.; Testa, J. R.; Fernandez, M. P.: Genomic
locations of ANX11 and ANX13 and the evolutionary genetics of human
annexins. Genomics 48: 100-110, 1998.
*FIELD* CN
Ada Hamosh - updated: 10/22/2008
Patricia A. Hartz - updated: 6/7/2005
*FIELD* CD
Rebekah S. Rasooly: 4/27/1998
*FIELD* ED
carol: 11/30/2009
carol: 6/16/2009
terry: 6/12/2009
terry: 10/22/2008
wwang: 6/22/2005
wwang: 6/17/2005
terry: 6/7/2005
carol: 8/4/2003
mgross: 9/17/1999
psherman: 4/27/1998