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Protein

Annexin A2

Gene

ANXA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:24808179, PubMed:22848640).3 Publications

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium-dependent protein binding Source: AgBase
  • calcium ion binding Source: InterPro
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • phospholipase A2 inhibitor activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • body fluid secretion Source: Ensembl
  • collagen fibril organization Source: Ensembl
  • fibrinolysis Source: Ensembl
  • membrane budding Source: UniProtKB
  • membrane raft assembly Source: UniProtKB
  • negative regulation of catalytic activity Source: GOC
  • negative regulation of low-density lipoprotein particle receptor catabolic process Source: BHF-UCL
  • negative regulation of receptor binding Source: BHF-UCL
  • negative regulation of receptor internalization Source: BHF-UCL
  • osteoclast development Source: UniProtKB
  • positive regulation of binding Source: Ensembl
  • positive regulation of fibroblast proliferation Source: Ensembl
  • positive regulation of protein phosphorylation Source: Ensembl
  • positive regulation of receptor activity Source: BHF-UCL
  • positive regulation of vesicle fusion Source: UniProtKB
  • protein heterotetramerization Source: UniProtKB
  • protein targeting to plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_17044. Muscle contraction.
REACT_641. Dissolution of Fibrin Clot.

Protein family/group databases

TCDBi1.A.31.1.4. the annexin (annexin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A2
Alternative name(s):
Annexin II
Annexin-2
Calpactin I heavy chain
Calpactin-1 heavy chain
Chromobindin-8
Lipocortin II
Placental anticoagulant protein IV
Short name:
PAP-IV
Protein I
p36
Gene namesi
Name:ANXA2
Synonyms:ANX2, ANX2L4, CAL1H, LPC2D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:537. ANXA2.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB-SubCell
  • basolateral plasma membrane Source: BHF-UCL
  • cell cortex Source: Ensembl
  • cell surface Source: UniProtKB
  • early endosome Source: Ensembl
  • endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extrinsic component of plasma membrane Source: Ensembl
  • late endosome membrane Source: UniProtKB
  • lipid particle Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • macropinosome Source: Ensembl
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • midbody Source: UniProtKB
  • myelin sheath adaxonal region Source: Ensembl
  • nucleus Source: UniProtKB
  • PCSK9-AnxA2 complex Source: BHF-UCL
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: BHF-UCL
  • ruffle Source: Ensembl
  • sarcolemma Source: Ensembl
  • Schmidt-Lanterman incisure Source: Ensembl
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241Y → A: Abolishes heat stress-induced cell surface localization. 1 Publication
Mutagenesisi28 – 369KAYTNFDAE → SAYTNFNAS: No effect on interaction with PCSK9. 1 Publication
Mutagenesisi37 – 4711RDALNIETAIK → SDALNIHTAIM: Slightly decreases interaction with PCSK9. 1 PublicationAdd
BLAST
Mutagenesisi77 – 815RRTKK → AATAA: Strongly decreases interaction with PCSK9. 2 Publications
Mutagenesisi77 – 804RRTK → AATA: Decreases interaction with PCSK9. 1 Publication
Mutagenesisi80 – 845KKELA → GKPLD: No effect on interaction with PCSK9. 1 Publication
Mutagenesisi88 – 881K → A: Strongly decreases interaction with PCSK9; when associated with 77-A--A-81. 1 Publication

Organism-specific databases

PharmGKBiPA24827.

Chemistry

DrugBankiDB00031. Tenecteplase.

Polymorphism and mutation databases

BioMutaiANXA2.
DMDMi113950.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 339338Annexin A2PRO_0000067470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei24 – 241Phosphotyrosine; by SRC1 Publication
Modified residuei26 – 261Phosphoserine; by PKC1 Publication
Modified residuei49 – 491N6-acetyllysineBy similarity
Modified residuei152 – 1521N6-acetyllysineBy similarity
Modified residuei199 – 1991PhosphotyrosineBy similarity
Modified residuei227 – 2271N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylation of Tyr-24 enhances heat stress-induced translocation to the cell surface.2 Publications
ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP07355.
PaxDbiP07355.
PRIDEiP07355.

2D gel databases

DOSAC-COBS-2DPAGEP07355.
REPRODUCTION-2DPAGEIPI00455315.
P07355.
UCD-2DPAGEP07355.

PTM databases

PhosphoSiteiP07355.

Expressioni

Gene expression databases

BgeeiP07355.
CleanExiHS_ANXA2.
ExpressionAtlasiP07355. baseline and differential.
GenevisibleiP07355. HS.

Organism-specific databases

HPAiCAB004311.

Interactioni

Subunit structurei

Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36. Interacts with ATP1B1 and DYSF (By similarity). Interacts with COCH (PubMed:21886777). Interacts (via repeat Annexin 1) with PCSK9 (via the C-terminal domain); the interaction inhibits the degradation of LDLR (PubMed:18799458). Interacts with human cytomegalovirus (HCMV) (PubMed:8117306).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB85EBI-352622,EBI-6927873From a different organism.
MLH1P406927EBI-352622,EBI-744248
PCSK9Q8NBP77EBI-352622,EBI-7539251

Protein-protein interaction databases

BioGridi106799. 73 interactions.
IntActiP07355. 31 interactions.
MINTiMINT-1213203.
STRINGi9606.ENSP00000346032.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 86Combined sources
Helixi35 – 4713Combined sources
Helixi53 – 608Combined sources
Helixi65 – 7915Combined sources
Helixi83 – 908Combined sources
Helixi93 – 10311Combined sources
Helixi106 – 11712Combined sources
Beta strandi120 – 1223Combined sources
Helixi125 – 13410Combined sources
Helixi137 – 15115Combined sources
Helixi155 – 1617Combined sources
Helixi165 – 17511Combined sources
Helixi188 – 20013Combined sources
Turni201 – 2044Combined sources
Beta strandi205 – 2073Combined sources
Helixi210 – 21910Combined sources
Helixi222 – 23211Combined sources
Turni233 – 2353Combined sources
Helixi240 – 2478Combined sources
Helixi250 – 26415Combined sources
Helixi266 – 27813Combined sources
Beta strandi279 – 2824Combined sources
Helixi285 – 29511Combined sources
Turni296 – 2983Combined sources
Helixi300 – 31112Combined sources
Helixi315 – 3228Combined sources
Helixi325 – 33511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W7BX-ray1.52A1-339[»]
1XJLX-ray2.59A/B21-339[»]
2HYUX-ray1.86A32-339[»]
2HYVX-ray1.42A32-339[»]
2HYWX-ray2.10A/B32-339[»]
4DRWX-ray3.50A/B/C/D2-16[»]
4FTGX-ray2.51C/D2-16[»]
4HRHX-ray3.00A/B2-16[»]
ProteinModelPortaliP07355.
SMRiP07355. Positions 32-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07355.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati42 – 10261Annexin 1Add
BLAST
Repeati114 – 17461Annexin 2Add
BLAST
Repeati199 – 25961Annexin 3Add
BLAST
Repeati274 – 33461Annexin 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2423S100A10-binding siteSequence AnalysisAdd
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 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiNOG259189.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP07355.
KOiK17092.
OMAiFIQQDTK.
OrthoDBiEOG74XS72.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002389. AnnexinII.
[Graphical view]
PANTHERiPTHR10502:SF18. PTHR10502:SF18. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00198. ANNEXINII.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P07355-1) [UniParc]FASTAAdd to basket

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
MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG
60 70 80 90 100
VDEVTIVNIL TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL
110 120 130 140 150
GLLKTPAQYD ASELKASMKG LGTDEDSLIE IICSRTNQEL QEINRVYKEM
160 170 180 190 200
YKTDLEKDII SDTSGDFRKL MVALAKGRRA EDGSVIDYEL IDQDARDLYD
210 220 230 240 250
AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM LESIRKEVKG
260 270 280 290 300
DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
310 320 330
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD
Length:339
Mass (Da):38,604
Last modified:January 23, 2007 - v2
Checksum:i5126E1337A0CBEA1
GO
Isoform 2 (identifier: P07355-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGRQLAGCGDAGKKASFKM

Show »
Length:357
Mass (Da):40,411
Checksum:i2AA081CB4E7AC75C
GO

Sequence cautioni

The sequence AAH66955.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291A → P AA sequence (PubMed:8110754).Curated
Sequence conflicti166 – 1661D → G in CAE45704 (PubMed:17974005).Curated
Sequence conflicti293 – 2931V → A in AAH23990 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981V → L Lowers levels of circulating total cholesterol. 2 Publications
Corresponds to variant rs17845226 [ dbSNP | Ensembl ].
VAR_012982

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGRQLAGCGDAGKKASFKM in isoform 2. 1 PublicationVSP_038091

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00017 mRNA. Translation: BAA00013.1.
BT007432 mRNA. Translation: AAP36100.1.
BX640598 mRNA. Translation: CAE45704.1.
AC087385 Genomic DNA. No translation available.
BC001388 mRNA. Translation: AAH01388.1.
BC009564 mRNA. Translation: AAH09564.1.
BC015834 mRNA. Translation: AAH15834.1.
BC016774 mRNA. Translation: AAH16774.1.
BC021114 mRNA. Translation: AAH21114.1.
BC023990 mRNA. Translation: AAH23990.1.
BC052558 mRNA. Translation: AAH52558.1.
BC052567 mRNA. Translation: AAH52567.1.
BC066955 mRNA. Translation: AAH66955.2. Different initiation.
BC068065 mRNA. Translation: AAH68065.1.
BC093056 mRNA. Translation: AAH93056.1.
CCDSiCCDS10175.1. [P07355-1]
CCDS32256.1. [P07355-2]
PIRiA23942. LUHU36.
RefSeqiNP_001002857.1. NM_001002857.1. [P07355-1]
NP_001002858.1. NM_001002858.2. [P07355-2]
NP_001129487.1. NM_001136015.2. [P07355-1]
NP_004030.1. NM_004039.2. [P07355-1]
XP_011519777.1. XM_011521475.1. [P07355-1]
XP_011519778.1. XM_011521476.1. [P07355-1]
UniGeneiHs.511605.

Genome annotation databases

EnsembliENST00000332680; ENSP00000346032; ENSG00000182718. [P07355-2]
ENST00000396024; ENSP00000379342; ENSG00000182718.
ENST00000421017; ENSP00000411352; ENSG00000182718.
ENST00000451270; ENSP00000387545; ENSG00000182718.
GeneIDi302.
KEGGihsa:302.
UCSCiuc002agk.3. human. [P07355-1]
uc002agm.3. human. [P07355-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

Red velvet - Issue 86 of September 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00017 mRNA. Translation: BAA00013.1.
BT007432 mRNA. Translation: AAP36100.1.
BX640598 mRNA. Translation: CAE45704.1.
AC087385 Genomic DNA. No translation available.
BC001388 mRNA. Translation: AAH01388.1.
BC009564 mRNA. Translation: AAH09564.1.
BC015834 mRNA. Translation: AAH15834.1.
BC016774 mRNA. Translation: AAH16774.1.
BC021114 mRNA. Translation: AAH21114.1.
BC023990 mRNA. Translation: AAH23990.1.
BC052558 mRNA. Translation: AAH52558.1.
BC052567 mRNA. Translation: AAH52567.1.
BC066955 mRNA. Translation: AAH66955.2. Different initiation.
BC068065 mRNA. Translation: AAH68065.1.
BC093056 mRNA. Translation: AAH93056.1.
CCDSiCCDS10175.1. [P07355-1]
CCDS32256.1. [P07355-2]
PIRiA23942. LUHU36.
RefSeqiNP_001002857.1. NM_001002857.1. [P07355-1]
NP_001002858.1. NM_001002858.2. [P07355-2]
NP_001129487.1. NM_001136015.2. [P07355-1]
NP_004030.1. NM_004039.2. [P07355-1]
XP_011519777.1. XM_011521475.1. [P07355-1]
XP_011519778.1. XM_011521476.1. [P07355-1]
UniGeneiHs.511605.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W7BX-ray1.52A1-339[»]
1XJLX-ray2.59A/B21-339[»]
2HYUX-ray1.86A32-339[»]
2HYVX-ray1.42A32-339[»]
2HYWX-ray2.10A/B32-339[»]
4DRWX-ray3.50A/B/C/D2-16[»]
4FTGX-ray2.51C/D2-16[»]
4HRHX-ray3.00A/B2-16[»]
ProteinModelPortaliP07355.
SMRiP07355. Positions 32-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106799. 73 interactions.
IntActiP07355. 31 interactions.
MINTiMINT-1213203.
STRINGi9606.ENSP00000346032.

Chemistry

ChEMBLiCHEMBL2111435.
DrugBankiDB00031. Tenecteplase.

Protein family/group databases

TCDBi1.A.31.1.4. the annexin (annexin) family.

PTM databases

PhosphoSiteiP07355.

Polymorphism and mutation databases

BioMutaiANXA2.
DMDMi113950.

2D gel databases

DOSAC-COBS-2DPAGEP07355.
REPRODUCTION-2DPAGEIPI00455315.
P07355.
UCD-2DPAGEP07355.

Proteomic databases

MaxQBiP07355.
PaxDbiP07355.
PRIDEiP07355.

Protocols and materials databases

DNASUi302.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332680; ENSP00000346032; ENSG00000182718. [P07355-2]
ENST00000396024; ENSP00000379342; ENSG00000182718.
ENST00000421017; ENSP00000411352; ENSG00000182718.
ENST00000451270; ENSP00000387545; ENSG00000182718.
GeneIDi302.
KEGGihsa:302.
UCSCiuc002agk.3. human. [P07355-1]
uc002agm.3. human. [P07355-2]

Organism-specific databases

CTDi302.
GeneCardsiGC15M060639.
HGNCiHGNC:537. ANXA2.
HPAiCAB004311.
MIMi151740. gene.
neXtProtiNX_P07355.
PharmGKBiPA24827.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG259189.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP07355.
KOiK17092.
OMAiFIQQDTK.
OrthoDBiEOG74XS72.
TreeFamiTF105452.

Enzyme and pathway databases

ReactomeiREACT_17044. Muscle contraction.
REACT_641. Dissolution of Fibrin Clot.

Miscellaneous databases

ChiTaRSiANXA2. human.
EvolutionaryTraceiP07355.
GeneWikiiAnnexin_A2.
GenomeRNAii302.
NextBioi1217.
PROiP07355.
SOURCEiSearch...

Gene expression databases

BgeeiP07355.
CleanExiHS_ANXA2.
ExpressionAtlasiP07355. baseline and differential.
GenevisibleiP07355. HS.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002389. AnnexinII.
[Graphical view]
PANTHERiPTHR10502:SF18. PTHR10502:SF18. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00198. ANNEXINII.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase."
    Huang K.-S., Wallner B.P., Mattaliano R.J., Tizard R., Burne C., Frey A., Hession C., McGray P., Sinclair L.K., Chow E.P., Browning J.L., Ramachandran K.L., Tang J., Smart J.E., Pepinsky R.B.
    Cell 46:191-199(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication."
    Spano F., Raugei G., Palla E., Colella C., Melli M.
    Gene 95:243-251(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Colon endothelium.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), VARIANT LEU-98.
    Tissue: Brain, Colon, Pancreas, Prostate, Skin, Testis and Urinary bladder.
  7. Cited for: PROTEIN SEQUENCE OF 2-10; 38-47; 50-63; 69-77; 89-115; 153-169 AND 213-220, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon adenocarcinoma and Osteosarcoma.
  8. "The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha."
    Jindal H.K., Chaney W.G., Anderson C.W., Davis R.G., Vishwanatha J.K.
    J. Biol. Chem. 266:5169-5176(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 11-27; 49-62; 68-77; 120-135; 314-323 AND 329-339.
  9. "Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells."
    Hyatt S.L., Liao L., Chapline C., Jaken S.
    Biochemistry 33:1223-1228(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-40 AND 50-63.
  10. "An endothelial cell-surface form of annexin II binds human cytomegalovirus."
    Wright J.F., Kurosky A., Wasi S.
    Biochem. Biophys. Res. Commun. 198:983-989(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-37; 119-126; 172-191 AND 301-307, INTERACTION WITH HCMV.
    Tissue: Umbilical vein endothelial cell.
  11. "Annexin II is a major component of fusogenic endosomal vesicles."
    Emans N., Gorvel J.P., Walter C., Gerke V., Kellner R., Griffiths G., Gruenberg J.
    J. Cell Biol. 120:1357-1369(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 234-241 AND 252-261.
  12. "The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo."
    Gould K.L., Woodgett J.R., Isacke C.M., Hunter T.
    Mol. Cell. Biol. 6:2738-2744(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-26.
  13. "An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface."
    Deora A.B., Kreitzer G., Jacovina A.T., Hajjar K.A.
    J. Biol. Chem. 279:43411-43418(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-24, MUTAGENESIS OF TYR-24.
  14. Cited for: ISGYLATION.
  15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  16. "Annexin A2 is a C-terminal PCSK9-binding protein that regulates endogenous low density lipoprotein receptor levels."
    Mayer G., Poirier S., Seidah N.G.
    J. Biol. Chem. 283:31791-31801(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PCSK9, MUTAGENESIS OF 77-ARG--LYS-81; 80-LYS--ALA-84 AND LYS-88.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Cochlin induced TREK-1 co-expression and annexin A2 secretion: role in trabecular meshwork cell elongation and motility."
    Goel M., Sienkiewicz A.E., Picciani R., Lee R.K., Bhattacharya S.K.
    PLoS ONE 6:E23070-E23070(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COCH.
  19. "Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced LDL receptor degradation."
    Seidah N.G., Poirier S., Denis M., Parker R., Miao B., Mapelli C., Prat A., Wassef H., Davignon J., Hajjar K.A., Mayer G.
    PLoS ONE 7:E41865-E41865(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, VARIANT LEU-98, CHARACTERIZATION OF VARIANT LEU-98, MUTAGENESIS OF 28-LYS--GLU-36; 37-ARG--LYS-47; 77-ARG--LYS-80 AND 77-ARG--LYS-81.
  20. "Annexin A2 reduces PCSK9 protein levels via a translational mechanism and interacts with the M1 and M2 domains of PCSK9."
    Ly K., Saavedra Y.G., Canuel M., Routhier S., Desjardins R., Hamelin J., Mayne J., Lazure C., Seidah N.G., Day R.
    J. Biol. Chem. 289:17732-17746(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PCSK9, RNA-BINDING.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein."
    Burger A., Berendes R., Liemann S., Benz J., Hofmann A., Goettig P., Huber R., Gerke V., Tiel C., Roemisch J., Weber K.
    J. Mol. Biol. 257:839-847(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiANXA2_HUMAN
AccessioniPrimary (citable) accession number: P07355
Secondary accession number(s): Q567R4
, Q6N0B3, Q8TBV2, Q96DD5, Q9UDH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 192 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

It may cross-link plasma membrane phospholipids with actin and the cytoskeleton and be involved with exocytosis.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. 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.