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Protein Page:
ANXA7 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ANXA7 Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. Interacts with PDCD6. Isoform 1 is expressed in brain, heart and skeletal muscle. Isoform 2 is more abundant in liver, lung, kidney, spleen, fibroblasts and placenta. Belongs to the annexin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Calcium-binding protein; Lipid binding protein; Motility/polarity/chemotaxis
Cellular Component: plasma membrane; nuclear envelope; cytosol; vesicle
Molecular Function: protein binding; calcium-dependent phospholipid binding; calcium ion binding; calcium-dependent protein binding
Biological Process: cellular calcium ion homeostasis; regulation of cell shape; cell proliferation; cellular water homeostasis; hemostasis; social behavior; response to salt stress
Reference #:  P20073 (UniProtKB)
Alt. Names/Synonyms: Annexin A7; Annexin VII; Annexin-7; ANX7; ANXA7; SNX; Synexin
Gene Symbols: ANXA7
Molecular weight: 52,739 Da
Basal Isoelectric point: 5.52  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ANXA7

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K196-a RDAEILRkAMkGFGT
0 9 K199-u EILRkAMkGFGTDEQ
0 1 K228 QKIKAAFKTSYGkDL
0 1 K233-a AFKTSYGkDLIkDLK
0 1 K233-u AFKTSYGkDLIkDLK
0 3 K237-u SYGkDLIkDLKSELS
0 1 T286-p VLIEILCtRTNQEIR
0 1 K309 EFGRDLEKDIRSDTS
0 1 S336 GNRDENQSINHQMAQ
0 1 R377 TRSFPQLRATMEAYS
0 1 Y383 LRATMEAYSRMANRD
0 1 Y402 VSREFSGYVESGLKT
0 40 Y427-p FFAERLYyAMkGAGT
0 4 K430-u ERLYyAMkGAGTDDS
0 1 K455-u EIDLVQIkQMFAQMY
  mouse

 
K171 RDAEILRKAMkGFGT
K174-u EILRKAMkGFGTDEQ
K203-u QQIKAAFkTMYGKDL
K208 AFkTMYGKDLIkDLK
K208 AFkTMYGKDLIkDLK
K212-u MYGKDLIkDLKSELS
T261 VLIEILCTRTNQEIR
K284-u EFGRDLEkDIRSDTS
S311-p GNRDERQsVNHQMAQ
K352-u TRSFPQLkATMEAYS
Y358 LkATMEAYSRMANRD
Y377 VSREFSGYVESGLKT
Y402 FFAERLYYSMkGAGT
K405-u ERLYYSMkGAGTDDS
K430 EIDLVQIKQMFTQMY
  rat

 
K171 RDAEILRKAMKGFGT
K174 EILRKAMKGFGTDEQ
K203 QQIKAAFKTMYGKDL
K208 AFKTMYGKDLIKDLK
K208 AFKTMYGKDLIKDLK
K212 MYGKDLIKDLKSELS
T261 VLIEILCTRTNQEIR
R284 EFGRELERDIRSDTS
S311 GNRDESPSINHQMAQ
R352 TRSFPQLRATMEAyS
Y358-p LRATMEAySRMANRD
Y377-p VSREFSGyVESGLKT
Y402 FFAERLYYSMKGAGT
K405 ERLYYSMKGAGTDDS
K430 EIDLVQIKQMFTQMY
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