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Protein Page:
FETUA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
FETUA Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions. Alpha-2-HS glycoprotein derives from this precursor, when the connecting peptide is cleaved off. The two chains A and B are held together by a single disulfide bond. Synthesized in liver and selectively concentrated in bone matrix. Secreted in plasma. It is also found in dentin in much higher quantities than other plasma proteins. Belongs to the fetuin family. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted
Chromosomal Location of Human Ortholog: 3q27
Cellular Component: extracellular space; extracellular region
Molecular Function: kinase inhibitor activity; cysteine protease inhibitor activity
Biological Process: negative regulation of bone mineralization; pinocytosis; ossification; positive regulation of phagocytosis; regulation of inflammatory response; acute-phase response; negative regulation of phosphorylation; negative regulation of insulin receptor signaling pathway; regulation of bone mineralization; skeletal development
Reference #:  P02765 (UniProtKB)
Alt. Names/Synonyms: A2HS; AHS; AHSG; Alpha-2-HS-glycoprotein; Alpha-2-HS-glycoprotein chain A; Alpha-2-HS-glycoprotein chain B; Alpha-2-Z-globulin; Ba-alpha-2-glycoprotein; FETUA; Fetuin-A; HSGA
Gene Symbols: AHSG
Molecular weight: 39,325 Da
Basal Isoelectric point: 5.43  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

FETUA

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


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 E65 HTLNQIDEVKVWPQQ
0 1 - gap
0 1 K67 LNQIDEVKVWPQQPS
0 1 K120 DCDFQLLKLDGKFSV
0 1 A130 GKFSVVYAKCDssPD
0 7 S134-p VVYAKCDssPDsAED
0 15 S135-p VYAKCDssPDsAEDV
1 614 S138-p KCDssPDsAEDVRkV
0 1 K144-ac DsAEDVRkVCQDCPL
0 7 K225-ac KCNLLAEkQyGFCKA
0 2 K225-ub KCNLLAEkQyGFCKA
0 3 Y227-p NLLAEkQyGFCKATL
0 1 T319-p AHYDLRHtFMGVVSL
0 5 M321 YDLRHtFMGVVSLGs
1 33 S325 HtFMGVVSLGsPsGE
1 39 S328-p MGVVSLGsPsGEVsH
1 0 - gap
1 30 S330-p VVSLGsPsGEVsHPR
0 3 - gap
0 3 - gap
0 2 S334-p GsPsGEVsHPRKTRT
0 1 S346-ga TRTVVQPsVGAAAGP
0 1 K366 PGRIRHFKV______
  mouse

 
K65 QVLNQIDKVKVWSRR
K65-ub QVLNQIDkVKVWSRR
K67 LNQIDkVKVWSRRPF
K120 DCDFHILKQDGQFRV
T130-p GQFRVMHtQCHstPD
S134-p VMHtQCHstPDsAED
T135-p MHtQCHstPDsAEDV
S138-p QCHstPDsAEDVRKL
K144 DsAEDVRKLCPRCPL
K225 KCNLLAEKQHGFCKA
K225-ub KCNLLAEkQHGFCKA
H227 NLLAEkQHGFCKANL
A303 TYHDLRHAFsPVAsV
S305-p HDLRHAFsPVAsVEs
S309-p HAFsPVAsVEsAsGE
S312-p sPVAsVEsAsGEtLH
- gap
S314-p VAsVEsAsGEtLHsP
T317-p VEsAsGEtLHsPKVG
S320-p AsGEtLHsPKVGQPG
- gap
- gap
K344 PGRIRHFKI______
  rat

 
K65-ac QILNQIDkVkVWSRR
K65 QILNQIDKVkVWSRR
K67-ac LNQIDkVkVWSRRPF
K120-ac DCDFHILkQDGQFRV
A130 GQFRVLHAQCHstPD
S134-p VLHAQCHstPDsAED
T135-p LHAQCHstPDsAEDV
S138-p QCHstPDsAEDVRKF
K144 DsAEDVRKFCPRCPI
K225 KCNLLAEKQYGFCKA
K225 KCNLLAEKQYGFCKA
Y227 NLLAEKQYGFCKATL
A307 THHDLRHAFsPVAsV
S309-p HDLRHAFsPVAsVEs
S313-p HAFsPVAsVEsAsGE
S316-p sPVAsVEsAsGEVLH
- gap
S318-p VAsVEsAsGEVLHsP
V321 VEsAsGEVLHsPKVG
S324-p AsGEVLHsPKVGQPG
- gap
- gap
K351-ac PGRVRYFkI______
  cow

 
S65 HTLNQIDSVKVWPRR
- gap
K67 LNQIDSVKVWPRRPT
K120 DCDIHVLKQDGQFSV
T130 GQFSVLFTKCDSSPD
S134 VLFTKCDSSPDSAED
S135 LFTKCDSSPDSAEDV
S138 KCDSSPDSAEDVRKL
K144 DSAEDVRKLCPDCPL
K225 KCNLLAEKQYGFCKG
K225 KCNLLAEKQYGFCKG
Y227 NLLAEKQYGFCKGSV
T314 AHYDLRHTFSGVAsV
S316 YDLRHTFSGVAsVEs
S320-p HTFSGVAsVEssSGE
S323-p SGVAsVEssSGEAFH
S324-p GVAsVEssSGEAFHV
S325 VAsVEssSGEAFHVG
A328 VEssSGEAFHVGKTP
V331 sSGEAFHVGKTPIVG
- gap
- gap
K358 PGRIRYFKI______
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