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P48036

- ANXA5_MOUSE

UniProt

P48036 - ANXA5_MOUSE

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Protein

Annexin A5

Gene

Anxa5

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

Functioni

This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
  2. negative regulation of coagulation Source: InterPro
  3. response to organic substance Source: MGI
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A5
Alternative name(s):
Anchorin CII
Annexin V
Annexin-5
Calphobindin I
Short name:
CBP-I
Endonexin II
Lipocortin V
Placental anticoagulant protein 4
Short name:
PP4
Placental anticoagulant protein I
Short name:
PAP-I
Thromboplastin inhibitor
Vascular anticoagulant-alpha
Short name:
VAC-alpha
Gene namesi
Name:Anxa5
Synonyms:Anx5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:106008. Anxa5.

Subcellular locationi

GO - Cellular componenti

  1. endothelial microparticle Source: BHF-UCL
  2. external side of plasma membrane Source: MGI
  3. extracellular vesicular exosome Source: Ensembl
  4. intracellular Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 319318Annexin A5PRO_0000067488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei68 – 681N6-acetyllysine1 Publication
Modified residuei74 – 741N6-acetyllysineBy similarity
Modified residuei77 – 771N6-acetyllysineBy similarity
Modified residuei95 – 951N6-acetyllysine1 Publication
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei288 – 2881N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP48036.
PaxDbiP48036.
PRIDEiP48036.

2D gel databases

COMPLUYEAST-2DPAGEP48036.
REPRODUCTION-2DPAGEIPI00317309.
SWISS-2DPAGEP48036.

PTM databases

PhosphoSiteiP48036.

Expressioni

Gene expression databases

BgeeiP48036.
CleanExiMM_ANXA5.
GenevestigatoriP48036.

Interactioni

Subunit structurei

Monomer. Binds ATRX and EIF5B (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Kcnma1Q084604EBI-1184119,EBI-1633915

Protein-protein interaction databases

BioGridi198111. 2 interactions.
IntActiP48036. 6 interactions.
MINTiMINT-1869281.

Structurei

3D structure databases

ProteinModelPortaliP48036.
SMRiP48036. Positions 2-319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati22 – 8261Annexin 1Add
BLAST
Repeati94 – 15461Annexin 2Add
BLAST
Repeati178 – 23861Annexin 3Add
BLAST
Repeati253 – 31361Annexin 4Add
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

eggNOGiNOG281174.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP48036.
KOiK16646.
OMAiWNKTLAN.
OrthoDBiEOG74XS72.
PhylomeDBiP48036.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR015473. Annexins_V.
IPR002392. AnnexinV.
[Graphical view]
PANTHERiPTHR10502:SF26. PTHR10502:SF26. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00201. ANNEXINV.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P48036-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATRGTVTDF PGFDGRADAE VLRKAMKGLG TDEDSILNLL TSRSNAQRQE
60 70 80 90 100
IAQEFKTLFG RDLVDDLKSE LTGKFEKLIV AMMKPSRLYD AYELKHALKG
110 120 130 140 150
AGTDEKVLTE IIASRTPEEL SAIKQVYEEE YGSNLEDDVV GDTSGYYQRM
160 170 180 190 200
LVVLLQANRD PDTAIDDAQV ELDAQALFQA GELKWGTDEE KFITIFGTRS
210 220 230 240 250
VSHLRRVFDK YMTISGFQIE ETIDRETSGN LEQLLLAVVK SIRSIPAYLA
260 270 280 290 300
ETLYYAMKGA GTDDHTLIRV VVSRSEIDLF NIRKEFRKNF ATSLYSMIKG
310
DTSGDYKKAL LLLCGGEDD
Length:319
Mass (Da):35,752
Last modified:February 1, 1996 - v1
Checksum:i55055BAF2E1C36B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421D → G in BAE28107. (PubMed:16141072)Curated
Sequence conflicti157 – 1571A → G in AAH03716. (PubMed:15489334)Curated
Sequence conflicti284 – 2841K → N in BAE31952. (PubMed:16141072)Curated
Sequence conflicti300 – 3001G → S in BAE32026. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29396 mRNA. Translation: AAC52530.1.
D63423 mRNA. Translation: BAA09728.1.
AJ230108
, AJ230110, AJ230111, AJ230114, AJ230116, AJ230118, AJ230119, AJ230120, AJ230121, AJ230122, AJ230123, AJ230124 Genomic DNA. Translation: CAA13092.1.
AK147740 mRNA. Translation: BAE28107.1.
AK152185 mRNA. Translation: BAE31016.1.
AK153388 mRNA. Translation: BAE31952.1.
AK153476 mRNA. Translation: BAE32026.1.
BC003716 mRNA. Translation: AAH03716.1.
CCDSiCCDS38416.1.
RefSeqiNP_033803.1. NM_009673.2.
XP_006535439.1. XM_006535376.1.
UniGeneiMm.1620.

Genome annotation databases

EnsembliENSMUST00000029266; ENSMUSP00000029266; ENSMUSG00000027712.
GeneIDi11747.
KEGGimmu:11747.
UCSCiuc008ozj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29396 mRNA. Translation: AAC52530.1 .
D63423 mRNA. Translation: BAA09728.1 .
AJ230108
, AJ230110 , AJ230111 , AJ230114 , AJ230116 , AJ230118 , AJ230119 , AJ230120 , AJ230121 , AJ230122 , AJ230123 , AJ230124 Genomic DNA. Translation: CAA13092.1 .
AK147740 mRNA. Translation: BAE28107.1 .
AK152185 mRNA. Translation: BAE31016.1 .
AK153388 mRNA. Translation: BAE31952.1 .
AK153476 mRNA. Translation: BAE32026.1 .
BC003716 mRNA. Translation: AAH03716.1 .
CCDSi CCDS38416.1.
RefSeqi NP_033803.1. NM_009673.2.
XP_006535439.1. XM_006535376.1.
UniGenei Mm.1620.

3D structure databases

ProteinModelPortali P48036.
SMRi P48036. Positions 2-319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198111. 2 interactions.
IntActi P48036. 6 interactions.
MINTi MINT-1869281.

PTM databases

PhosphoSitei P48036.

2D gel databases

COMPLUYEAST-2DPAGE P48036.
REPRODUCTION-2DPAGE IPI00317309.
SWISS-2DPAGE P48036.

Proteomic databases

MaxQBi P48036.
PaxDbi P48036.
PRIDEi P48036.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029266 ; ENSMUSP00000029266 ; ENSMUSG00000027712 .
GeneIDi 11747.
KEGGi mmu:11747.
UCSCi uc008ozj.2. mouse.

Organism-specific databases

CTDi 308.
MGIi MGI:106008. Anxa5.

Phylogenomic databases

eggNOGi NOG281174.
GeneTreei ENSGT00760000118972.
HOGENOMi HOG000158803.
HOVERGENi HBG061815.
InParanoidi P48036.
KOi K16646.
OMAi WNKTLAN.
OrthoDBi EOG74XS72.
PhylomeDBi P48036.
TreeFami TF105452.

Miscellaneous databases

NextBioi 279485.
PROi P48036.
SOURCEi Search...

Gene expression databases

Bgeei P48036.
CleanExi MM_ANXA5.
Genevestigatori P48036.

Family and domain databases

Gene3Di 1.10.220.10. 4 hits.
InterProi IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR015473. Annexins_V.
IPR002392. AnnexinV.
[Graphical view ]
PANTHERi PTHR10502:SF26. PTHR10502:SF26. 1 hit.
Pfami PF00191. Annexin. 4 hits.
[Graphical view ]
PRINTSi PR00196. ANNEXIN.
PR00201. ANNEXINV.
SMARTi SM00335. ANX. 4 hits.
[Graphical view ]
PROSITEi PS00223. ANNEXIN. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse annexin V chromosomal localization, cDNA sequence conservation, and molecular evolution."
    Rodriguez-Garcia M.I., Kozak C.A., Morgan R.O., Fernandez M.-P.
    Genomics 31:151-157(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Peritoneal cavity.
  2. Adachi T., Kojima K., Fukuoka S., Ogawa H., Matsumoto I.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Mouse annexin V genomic organization includes an endogenous retrovirus."
    Rodriguez-Garcia M.I., Morgan R.O., Fernandez M.R., Bances P., Fernandez M.-P.
    Biochem. J. 337:125-131(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
    Tissue: Liver.
  4. "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: Bone marrow.
  5. "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: Mammary gland.
  6. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 28-43; 62-74; 116-124; 192-199; 226-240 AND 275-283, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  7. "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-68 AND LYS-95, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiANXA5_MOUSE
AccessioniPrimary (citable) accession number: P48036
Secondary accession number(s): Q3U5Q1
, Q3U5X4, Q3U8K1, Q3UGV0, Q99LA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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