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Protein

Annexin

Gene

ANXA1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro
  3. phospholipase inhibitor activity Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Calcium, Calcium/phospholipid-bindingUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
AnnexinUniRule annotation
Gene namesi
Name:ANXA1Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:533. ANXA1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. plasma membrane Source: HPA
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiQ5T3N1.

Expressioni

Gene expression databases

BgeeiQ5T3N1.
ExpressionAtlasiQ5T3N1. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliQ5T3N1.
SMRiQ5T3N1. Positions 13-204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the annexin family.UniRule annotation
Contains 2 annexin repeats.UniRule annotation

Keywords - Domaini

AnnexinUniRule annotationSAAS annotation, RepeatUniRule annotationSAAS annotation

Phylogenomic databases

GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.

Family and domain databases

Gene3Di1.10.220.10. 2 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 2 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 2 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q5T3N1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLILRYTFS KMAMVSEFLK QAWFIENEEQ EYVQTVKSSK GGPGSAVSPY
60 70 80 90 100
PTFNPSSDVA ALHKAIMVKG VDEATIIDIL TKRNNAQRQQ IKAAYLQETG
110 120 130 140 150
KPLDETLKKA LTGHLEEVVL ALLKTPAQFD ADELRAAMKG LGTDEDTLIE
160 170 180 190 200
ILASRTNKEI RDINRVYREE LKRDLAKDIT SDTSGDFRNA LLSLAKGDRS

EDFG
Length:204
Mass (Da):22,755
Last modified:December 21, 2004 - v1
Checksum:i3605CD624033D5C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei204 – 2041Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL359997 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000456643; ENSP00000412489; ENSG00000135046.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL359997 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliQ5T3N1.
SMRiQ5T3N1. Positions 13-204.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5T3N1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000456643; ENSP00000412489; ENSG00000135046.

Organism-specific databases

HGNCiHGNC:533. ANXA1.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.

Miscellaneous databases

ChiTaRSiANXA1. human.

Gene expression databases

BgeeiQ5T3N1.
ExpressionAtlasiQ5T3N1. baseline and differential.

Family and domain databases

Gene3Di1.10.220.10. 2 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 2 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 2 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  7. "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].

Entry informationi

Entry nameiQ5T3N1_HUMAN
AccessioniPrimary (citable) accession number: Q5T3N1
Entry historyi
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: April 29, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.