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Protein

Annexin A4

Gene

ANXA4

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

Functioni

Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.By similarity

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium-dependent protein binding Source: AgBase
  • calcium ion binding Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • NF-kappaB binding Source: BHF-UCL
  • phospholipase inhibitor activity Source: UniProtKB

GO - Biological processi

  • epithelial cell differentiation Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of catalytic activity Source: GOC
  • negative regulation of interleukin-8 secretion Source: BHF-UCL
  • negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  • Notch signaling pathway Source: Ensembl
  • regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A4
Alternative name(s):
35-beta calcimedin
Annexin IV
Annexin-4
Carbohydrate-binding protein p33/p41
Chromobindin-4
Endonexin I
Lipocortin IV
P32.5
PP4-X
Placental anticoagulant protein II
Short name:
PAP-II
Protein II
Gene namesi
Name:ANXA4
Synonyms:ANX4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:542. ANXA4.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nuclear membrane Source: BHF-UCL
  • nucleus Source: BHF-UCL
  • perinuclear region of cytoplasm Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • vesicle membrane Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24832.

Polymorphism and mutation databases

BioMutaiANXA4.
DMDMi1703319.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 319318Annexin A4PRO_0000067482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei7 – 71PhosphothreonineBy similarity
Modified residuei12 – 121PhosphoserineCombined sources
Modified residuei213 – 2131N6-acetyllysineCombined sources
Modified residuei293 – 2931N6-acetyllysineCombined sources
Modified residuei300 – 3001N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP09525.
MaxQBiP09525.
PaxDbiP09525.
PRIDEiP09525.

2D gel databases

DOSAC-COBS-2DPAGEP09525.
OGPiP09525.
REPRODUCTION-2DPAGEIPI00793199.
P09525.
SWISS-2DPAGEP09525.

PTM databases

iPTMnetiP09525.
PhosphoSiteiP09525.
SwissPalmiP09525.

Expressioni

Gene expression databases

BgeeiP09525.
CleanExiHS_ANXA4.
ExpressionAtlasiP09525. baseline and differential.
GenevisibleiP09525. HS.

Organism-specific databases

HPAiCAB005076.
CAB017560.
HPA007393.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TINF2Q9BSI42EBI-2556852,EBI-717399

GO - Molecular functioni

  • calcium-dependent protein binding Source: AgBase
  • identical protein binding Source: BHF-UCL
  • NF-kappaB binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106804. 17 interactions.
IntActiP09525. 6 interactions.
MINTiMINT-4528752.
STRINGi9606.ENSP00000377833.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 2611Combined sources
Beta strandi28 – 314Combined sources
Helixi34 – 418Combined sources
Helixi46 – 5914Combined sources
Helixi64 – 718Combined sources
Helixi74 – 8411Combined sources
Helixi87 – 9913Combined sources
Beta strandi100 – 1034Combined sources
Helixi106 – 11510Combined sources
Helixi118 – 13215Combined sources
Helixi136 – 1438Combined sources
Helixi146 – 15510Combined sources
Turni156 – 1583Combined sources
Helixi168 – 18114Combined sources
Turni182 – 1843Combined sources
Beta strandi185 – 1873Combined sources
Helixi190 – 19910Combined sources
Helixi202 – 21615Combined sources
Helixi220 – 2278Combined sources
Helixi230 – 24415Combined sources
Helixi246 – 25813Combined sources
Beta strandi259 – 2624Combined sources
Helixi265 – 27511Combined sources
Turni276 – 2794Combined sources
Helixi280 – 29112Combined sources
Helixi295 – 3028Combined sources
Helixi305 – 31511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZOCX-ray2.00A/B1-319[»]
ProteinModelPortaliP09525.
SMRiP09525. Positions 1-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09525.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati23 – 8361Annexin 1Add
BLAST
Repeati95 – 15561Annexin 2Add
BLAST
Repeati179 – 23961Annexin 3Add
BLAST
Repeati254 – 31461Annexin 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

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOVERGENiHBG061815.
InParanoidiP09525.
KOiK17093.
PhylomeDBiP09525.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002391. AnnexinIV.
[Graphical view]
PANTHERiPTHR10502:SF28. PTHR10502:SF28. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
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: P09525-1) [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
MATKGGTVKA ASGFNAMEDA QTLRKAMKGL GTDEDAIISV LAYRNTAQRQ
60 70 80 90 100
EIRTAYKSTI GRDLIDDLKS ELSGNFEQVI VGMMTPTVLY DVQELRRAMK
110 120 130 140 150
GAGTDEGCLI EILASRTPEE IRRISQTYQQ QYGRSLEDDI RSDTSFMFQR
160 170 180 190 200
VLVSLSAGGR DEGNYLDDAL VRQDAQDLYE AGEKKWGTDE VKFLTVLCSR
210 220 230 240 250
NRNHLLHVFD EYKRISQKDI EQSIKSETSG SFEDALLAIV KCMRNKSAYF
260 270 280 290 300
AEKLYKSMKG LGTDDNTLIR VMVSRAEIDM LDIRAHFKRL YGKSLYSFIK
310
GDTSGDYRKV LLVLCGGDD
Length:319
Mass (Da):35,883
Last modified:January 23, 2007 - v4
Checksum:i3799FE80A93AB215
GO
Isoform 2 (identifier: P09525-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.

Note: No experimental confirmation available.
Show »
Length:237
Mass (Da):27,063
Checksum:iC512EFA927DBDD7D
GO

Sequence cautioni

The sequence AAC41689.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH00182.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH11659.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA11227.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961R → Q in AAC41689 (PubMed:2970257).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851T → M.
Corresponds to variant rs2228203 [ dbSNP | Ensembl ].
VAR_055500

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8282Missing in isoform 2. 1 PublicationVSP_056396Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19383 mRNA. Translation: AAC41689.1. Different initiation.
M82809 mRNA. Translation: AAA51740.1.
D78152 mRNA. Translation: BAA11227.1. Different initiation.
AK293177 mRNA. Translation: BAG56720.1.
AC019206 Genomic DNA. No translation available.
AC092431 Genomic DNA. No translation available.
AC112787 Genomic DNA. No translation available.
BC000182 mRNA. Translation: AAH00182.1. Different initiation.
BC011659 mRNA. Translation: AAH11659.1. Different initiation.
PIRiA42077.
RefSeqiNP_001144.1. NM_001153.4.
NP_001307627.1. NM_001320698.1.
NP_001307629.1. NM_001320700.1.
NP_001307631.1. NM_001320702.1.
UniGeneiHs.422986.

Genome annotation databases

EnsembliENST00000394295; ENSP00000377833; ENSG00000196975.
ENST00000536030; ENSP00000441931; ENSG00000196975.
GeneIDi307.
KEGGihsa:307.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19383 mRNA. Translation: AAC41689.1. Different initiation.
M82809 mRNA. Translation: AAA51740.1.
D78152 mRNA. Translation: BAA11227.1. Different initiation.
AK293177 mRNA. Translation: BAG56720.1.
AC019206 Genomic DNA. No translation available.
AC092431 Genomic DNA. No translation available.
AC112787 Genomic DNA. No translation available.
BC000182 mRNA. Translation: AAH00182.1. Different initiation.
BC011659 mRNA. Translation: AAH11659.1. Different initiation.
PIRiA42077.
RefSeqiNP_001144.1. NM_001153.4.
NP_001307627.1. NM_001320698.1.
NP_001307629.1. NM_001320700.1.
NP_001307631.1. NM_001320702.1.
UniGeneiHs.422986.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZOCX-ray2.00A/B1-319[»]
ProteinModelPortaliP09525.
SMRiP09525. Positions 1-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106804. 17 interactions.
IntActiP09525. 6 interactions.
MINTiMINT-4528752.
STRINGi9606.ENSP00000377833.

PTM databases

iPTMnetiP09525.
PhosphoSiteiP09525.
SwissPalmiP09525.

Polymorphism and mutation databases

BioMutaiANXA4.
DMDMi1703319.

2D gel databases

DOSAC-COBS-2DPAGEP09525.
OGPiP09525.
REPRODUCTION-2DPAGEIPI00793199.
P09525.
SWISS-2DPAGEP09525.

Proteomic databases

EPDiP09525.
MaxQBiP09525.
PaxDbiP09525.
PRIDEiP09525.

Protocols and materials databases

DNASUi307.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394295; ENSP00000377833; ENSG00000196975.
ENST00000536030; ENSP00000441931; ENSG00000196975.
GeneIDi307.
KEGGihsa:307.

Organism-specific databases

CTDi307.
GeneCardsiANXA4.
HGNCiHGNC:542. ANXA4.
HPAiCAB005076.
CAB017560.
HPA007393.
MIMi106491. gene.
neXtProtiNX_P09525.
PharmGKBiPA24832.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOVERGENiHBG061815.
InParanoidiP09525.
KOiK17093.
PhylomeDBiP09525.
TreeFamiTF105452.

Miscellaneous databases

ChiTaRSiANXA4. human.
EvolutionaryTraceiP09525.
GeneWikiiANXA4.
GenomeRNAii307.
NextBioi1239.
PROiP09525.
SOURCEiSearch...

Gene expression databases

BgeeiP09525.
CleanExiHS_ANXA4.
ExpressionAtlasiP09525. baseline and differential.
GenevisibleiP09525. HS.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002391. AnnexinIV.
[Graphical view]
PANTHERiPTHR10502:SF28. PTHR10502:SF28. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and expression of cDNA coding for a new member of the phospholipase A2 inhibitor family."
    Grundmann U., Amann E., Abel K.-J., Kuepper H.A.
    Behring Inst. Mitt. 82:59-67(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Chromosomal mapping of the human annexin IV (ANX4) gene."
    Tait J.F., Smith C., Frankenberry D.A., Miao C.H., Adler D.A., Disteche C.M.
    Genomics 12:313-318(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Characterization of human p33/41 (annexin IV), a Ca2+ dependent carbohydrate-binding protein with monoclonal anti-annexin IV antibodies, AS11 and AS17."
    Satoh A., Takayama E., Kojima K., Ogawa H., Katsura Y., Kina T., Matsumoto I.
    Biol. Pharm. Bull. 20:224-229(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Adrenal gland.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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).
    Tissue: Eye and Uterus.
  7. "Placental anticoagulant proteins: isolation and comparative characterization four members of the lipocortin family."
    Tait J.F., Sakata M., McMullen B.A., Miao C.H., Funakoshi T., Hendrickson L.E., Fujikawa K.
    Biochemistry 27:6268-6276(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15; 28-72; 100-144 AND 281-319.
  8. "Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor."
    Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W., de Haen C.
    J. Biol. Chem. 263:18657-18663(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-56; 99-124 AND 280-308.
    Tissue: Placenta.
  9. "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-213; LYS-293 AND LYS-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Crystallization and preliminary X-ray crystallographic studies of human placental annexin IV."
    Freemont P.S., Driessen H.P.C., Verbi W., Crumpton M.J.
    J. Mol. Biol. 216:219-221(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiANXA4_HUMAN
AccessioniPrimary (citable) accession number: P09525
Secondary accession number(s): B4DDF9, Q96F33, Q9BWK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 176 of the entry and version 4 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

Seems to bind one calcium ion with high affinity.

Keywords - Technical termi

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

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.