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Protein Page:
CA2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CA2 Essential for bone resorption and osteoclast differentiation. Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity. Activated by X-ray, histamine, L-adrenaline, L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-Ala- His (carnosine). Competitively inhibited by saccharin, thioxolone, coumarins, 667-coumate, celecoxib (Celebrex), valdecoxib (Bextra), SC-125, SC-560, diclofenac, acetate, azide, bromide, sulfonamide derivatives such as acetazolamide (AZA), methazolamide (MZA), ethoxzolamide (EZA), dichlorophenamide (DCP), brinzolamide, dansylamide, thiabendazole-5-sulfonamide, trifluoromethane sulfonamide and N-hydroxysulfamide, fructose-based sugar sulfamate RWJ-37497, and Foscarnet (phosphonoformate trisodium salt). Repressed strongly by hydrogen sulfide(HS) and weakly by nitrate (NO(3)). Esterase activity weakly reduced by cyanamide. N- hydroxyurea interfers with zinc binding and inhibit activity. Belongs to the alpha-carbonic anhydrase family. Note: This description may include information from UniProtKB.
Protein type: Energy Metabolism - nitrogen; EC 4.2.1.1; Lyase
Cellular Component: extracellular space; microvillus; apical part of cell; axon; basolateral plasma membrane; cytoplasm; plasma membrane; cytosol
Molecular Function: protein binding; carbonate dehydratase activity; zinc ion binding
Biological Process: secretion; positive regulation of osteoclast differentiation; carbon dioxide transport; positive regulation of cellular pH reduction; one-carbon compound metabolic process; odontogenesis of dentine-containing teeth; response to zinc ion; bicarbonate transport; response to estrogen stimulus; regulation of intracellular pH; positive regulation of bone resorption; morphogenesis of an epithelium; kidney development; response to pH
Reference #:  P00918 (UniProtKB)
Alt. Names/Synonyms: CA-II; CA2; CAC; CAH2; CAII; Car2; Carbonate dehydratase II; Carbonic anhydrase 2; carbonic anhydrase B; Carbonic anhydrase C; Carbonic anhydrase II
Gene Symbols: CA2
Molecular weight: 29,246 Da
Basal Isoelectric point: 6.87  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CA2

Protein Structure Not Found.


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12CA
1A42
1AM6
1AVN
1BCD
1BIC
1BN1
1BN3
1BN4
1BNM
1BNN
1BNQ
1BNT
1BNU
1BNV
1BNW
1BV3
1CA2
1CA3
1CAH
1CAI
1CAJ
1CAK
1CAL
1CAM
1CAN
1CAO
1CAY
1CAZ
1CCS
1CCT
1CCU
1CIL
1CIM
1CIN
1CNB
1CNC
1CNG
1CNH
1CNI
1CNJ
1CNK
1CNW
1CNX
1CNY
1CRA
1CVA
1CVB
1CVC
1CVD
1CVE
1CVF
1CVH
1DCA
1DCB
1EOU
1F2W
1FQL
1FQM
1FQN
1FQR
1FR4
1FR7
1FSN
1FSQ
1FSR
1G0E
1G0F
1G1D
1G3Z
1G45
1G46
1G48
1G4J
1G4O
1G52
1G53
1G54
1H4N
1H9N
1H9Q
1HCA
1HEA
1HEB
1HEC
1HED
1HVA
1I8Z
1I90
1I91
1I9L
1I9M
1I9N
1I9O
1I9P
1I9Q
1IF4
1IF5
1IF6
1IF7
1IF8
1IF9
1KWQ
1KWR
1LG5
1LG6
1LGD
1LUG
1LZV
1MOO
1MUA
1OKL
1OKM
1OKN
1OQ5
1RAY
1RAZ
1RZA
1RZB
1RZC
1RZD
1RZE
1T9N
1TB0
1TBT
1TE3
1TEQ
1TEU
1TG3
1TG9
1TH9
1THK
1TTM
1UGA
1UGB
1UGC
1UGD
1UGE
1UGF
1UGG
1XEG
1XEV
1XPZ
1XQ0
1YDA
1YDB
1YDC
1YDD
1YO0
1YO1
1YO2
1Z9Y
1ZE8
1ZFK
1ZFQ
1ZGE
1ZGF
1ZH9
1ZSA
1ZSB
1ZSC
2ABE
2AW1
2AX2
2CA2
2CBA
2CBB
2CBC
2CBD
2CBE
2EU2
2EU3
2EZ7
2F14
2FMG
2FMZ
2FNK
2FNM
2FNN
2FOQ
2FOS
2FOU
2FOV
2GD8
2GEH
2H15
2H4N
2HD6
2HKK
2HL4
2HNC
2HOC
2ILI
2NNG
2NNO
2NNS
2NNV
2NWO
2NWP
2NWY
2NWZ
2NXR
2NXS
2NXT
2O4Z
2OSF
2OSM
2POU
2POV
2POW
2Q1B
2Q1Q
2Q38
2QO8
2QOA
2QP6
2VVA
2VVB
2WD2
2WD3
2WEG
2WEH
2WEJ
2WEO
2X7S
2X7T
2X7U
3B4F
3BET
3BL0
3BL1
3C7P
3CA2
3CAJ
3CYU
3D8W
3D92
3D93
3D9Z
3DAZ
3DBU
3DC3
3DC9
3DCC
3DCS
3DCW
3DD0
3DD8
3DV7
3DVB
3DVC
3DVD
3EFI
3EFT
3F4X
3F8E
3FFP
3GZ0
3HFP
3HKN
3HKQ
3HKT
3HKU
3HLJ
3HS4
3IBI
3IBL
3IBN
3IBU
3IEO
3IGP
3IQK
3K2F
3K34
3K7K
3KIG
3KKX
3KNE
3KOI
3KOK
3KON
3KS3
3KWA
3L14
3M04
3M14
3M1J
3M1K
3M1Q
3M1W
3M2N
3M2X
3M2Y
3M2Z
3M3X
3M40
3M5E
3M5S
3M5T
3M67
3M96
3M98
3MHC
3MHI
3MHL
3MHM
3MHO
3ML2
3MMF
3MNA
3MNH
3MNI
3MNJ
3MNK
3MNU
3MWO
3MYQ
3MZC
3N0N
3N2P
3N3J
3N4B
3NB5
3NI5
3NJ9
3OIK
3OIL
3OIM
3OKU
3OKV
3OY0
3OYQ
3OYS
3P25
3P29
3P3H
3P3J
3P44
3P4V
3P55
3P58
3P5A
3P5L
3PJJ
3PO6
3PYK
3QYK
3R16
3R17
3RG3
3RG4
3RGE
3RJ7
3RLD
3RYJ
3RYV
3RYX
3RYY
3RYZ
3RZ0
3RZ1
3RZ5
3RZ7
3RZ8
3S71
3S72
3S73
3S74
3S75
3S76
3S77
3S78
3S8X
3S9T
3SAP
3SAX
3SBH
3SBI
3T5U
3T5Z
3T82
3T83
3T84
3T85
3TMJ
3TVN
3TVO
3U3A
3U45
3U47
3U7C
3V2J
3V2M
3V3F
3V3G
3V3H
3V3I
3V3J
3V5G
3V7X
3VBD
3ZP9
4BCW
4BF1
4BF6
4CA2
4CAC
4CQ0
4DZ7
4DZ9
4E3D
4E3F
4E3G
4E3H
4E49
4E4A
4E5Q
4FIK
4FL7
4FPT
4FRC
4FU5
4FVN
4FVO
4G0C
4GGE
4GL1
4HBA
4HEW
4HEY
4HEZ
4HF3
4HT0
4IDR
4ILX
4ITO
4ITP
4IWZ
4JS6
4JSA
4JSS
4JSW
4JSZ
4K0S
4K0T
4K0Z
4K13
4K1Q
4KAP
4KNI
4KNJ
4KUV
4KUW
4KUY
4KV0
4L5U
4L5V
4L5W
4LHI
4LP6
4M2R
4M2U
4M2V
4M2W
4MDG
4MDL
4MDM
4MLT
4MLX
4MO8
4MTY
4N0X
4N16
4PQ7
4QEF
4R59
4R5A
4R5B
5CA2
5CAC
6CA2
7CA2
8CA2
9CA2
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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 K9 SHHWGYGKHNGPEHW
0 4 K18-ac NGPEHWHkDFPIAKG
0 2 K18-ub NGPEHWHkDFPIAKG
0 1 S29-p IAKGERQsPVDIDtH
0 2 T35-p QsPVDIDtHTAkyDP
0 1 K39-ub DIDtHTAkyDPSLkP
0 1 Y40-p IDtHTAkyDPSLkPL
0 1 K45-ub AkyDPSLkPLSVsyD
0 1 S50-p SLkPLSVsyDQATSL
0 3 Y51-p LkPLSVsyDQATSLR
0 2 Q53 PLSVsyDQATSLRIL
0 1 L57 syDQATSLRILNNGH
0 2 K80-ub SQDKAVLkGGPLDGT
0 2 D85 VLkGGPLDGTYRLIQ
0 4 T87 kGGPLDGTYRLIQFH
0 3 S99-p QFHFHWGsLDGQGSE
0 1 Y114-p HTVDKKKyAAELHLV
0 1 K132 TKYGDFGKAVQQPDG
0 1 K153 FLKVGSAKPGLQkVV
0 2 K158-ub SAKPGLQkVVDVLDs
0 2 S165-p kVVDVLDsIKTKGKs
0 1 K167 VDVLDsIKTKGKsAD
0 1 S172-p sIKTKGKsADFTNFD
0 1 K224-ub VSSEQVLkFRKLNFN
  mouse

 
K9-ub SHHWGYSkHNGPENW
K18-ac NGPENWHkDFPIANG
K18-ub NGPENWHkDFPIANG
S29 IANGDRQSPVDIDTA
T35 QSPVDIDTATAQHDP
Q39 DIDTATAQHDPALQP
H40 IDTATAQHDPALQPL
Q45 AQHDPALQPLLISYD
S50 ALQPLLISYDkAASk
Y51 LQPLLISYDkAASkS
K53-ub PLLISYDkAASkSIV
K57-ub SYDkAASkSIVNNGH
K80-ub SQDNAVLkGGPLsDs
S85-p VLkGGPLsDsYRLIQ
S87-p kGGPLsDsYRLIQFH
S99 QFHFHWGSSDGQGSE
Y114 HTVNKKKYAAELHLV
K132-ub TKYGDFGkAVQQPDG
S153-p FLKIGPAsQGLQkVL
K158-ub PAsQGLQkVLEALHS
S165 kVLEALHSIkTKGKR
K167-ub LEALHSIkTKGKRAA
R172 SIkTKGKRAAFANFD
H224 VSSEQMSHFRTLNFN
  rat

 
K9 SHHWGYSKSNGPENW
K18-ac NGPENWHkEFPIANG
K18 NGPENWHKEFPIANG
S29 IANGDRQSPVDIDTG
T35 QSPVDIDTGTAQHDP
Q39 DIDTGTAQHDPSLQP
H40 IDTGTAQHDPSLQPL
Q45 AQHDPSLQPLLICYD
C50 SLQPLLICYDkVASK
Y51 LQPLLICYDkVASKS
K53-ub PLLICYDkVASKSIV
K57 CYDkVASKSIVNNGH
K80 SQDFAVLKEGPLsGs
S85-p VLKEGPLsGsYRLIQ
S87-p KEGPLsGsYRLIQFH
S99 QFHFHWGSSDGQGSE
Y114 HTVNKKKYAAELHLV
K132 TKYGDFGKAVQHPDG
S153 FLKIGPASQGLQKIT
K158 PASQGLQKITEALHS
S165 KITEALHSIKTKGKR
K167 TEALHSIKTKGKRAA
R172 SIKTKGKRAAFANFD
H224 VSSEQMSHFRKLNFN
  cow

 
K9 SHHWGYGKHNGPEHW
K18 NGPEHWHKDFPIANG
K18 NGPEHWHKDFPIANG
S29 IANGERQSPVDIDTK
T35 QSPVDIDTKAVVQDP
V39 DIDTKAVVQDPALKP
Q40 IDTKAVVQDPALKPL
K45 VVQDPALKPLALVYG
V50 ALKPLALVYGEATSR
Y51 LKPLALVYGEATSRR
E53 PLALVYGEATSRRMV
R57 VYGEATSRRMVNNGH
K80 SQDKAVLKDGPLTGT
T85 VLKDGPLTGTYRLVQ
T87 KDGPLTGTYRLVQFH
S99 QFHFHWGSSDDQGSE
Y114 HTVDRKKYAAELHLV
T132 TKYGDFGTAAQQPDG
N153 FLKVGDANPALQKVL
K158 DANPALQKVLDALDS
S165 KVLDALDSIKTKGKS
K167 LDALDSIKTKGKSTD
S172 SIKTKGKSTDFPNFD
K224 VSSQQMLKFRTLNFN
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