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Protein Page:
AKR1C2 (human)
rdtyret
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
AKR1C2 Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha- DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability. Defects in AKR1C2 are a cause of 46,XY sex reversal type 8 (SRXY8). A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females. Belongs to the aldo/keto reductase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 1.1.1.357; Xenobiotic Metabolism - metabolism by cytochrome P450; Oxidoreductase; EC 1.3.1.20
Chromosomal Location of Human Ortholog: 10p15-p14
Cellular Component: cytoplasm
Molecular Function: aldehyde reductase activity; bile acid binding; carboxylic acid binding; ketosteroid monooxygenase activity; oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor; phenanthrene 9,10-monooxygenase activity; trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity
Biological Process: digestion; epithelial cell differentiation; G-protein coupled receptor protein signaling pathway; positive regulation of cell proliferation; positive regulation of protein kinase B signaling cascade; progesterone metabolic process; prostaglandin metabolic process; steroid metabolic process
Disease: 46,xy Sex Reversal 8
Reference #:  P52895 (UniProtKB)
Alt. Names/Synonyms: 3-alpha hydroxysteroid dehydrogenase, type III); 3-alpha-HSD3; AK1C2; AKR1C-pseudo; AKR1C2; Aldo-keto reductase family 1 member C2; aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 2; BABP; bile acid binding protein; Chlordecone reductase homolog HAKRD; DD; DD-2; DD/BABP; DD2; DDH2; Dihydrodiol dehydrogenase 2; Dihydrodiol dehydrogenase/bile acid-binding protein; FLJ53800; HAKRD; HBAB; MCDR2; pseudo-chlordecone reductase; Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; type II dihydrodiol dehydrogenase; Type III 3-alpha-hydroxysteroid dehydrogenase
Gene Symbols: AKR1C2
Molecular weight: 36,735 Da
Basal Isoelectric point: 7.13  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

AKR1C2

Protein Structure Not Found.


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Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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 2 K9‑ub DSKYQCVkLNDGHFM
0 61 Y24‑p PVLGFGTyAPAEVPk
0 6 K31‑ub yAPAEVPkSkALEAV
0 5 K33‑ub PAEVPkSkALEAVKL
0 1 K39 SkALEAVKLAIEAGF
0 4 K68‑ub VGLAIRSkIADGSVk
0 3 K75‑ub kIADGSVkREDIFyT
0 34 Y81‑p VkREDIFyTSKLWSN
0 1 N88 yTSKLWSNSHRPELV
0 1 S89 TSKLWSNSHRPELVR
0 5 K104‑ub PALERSLkNLQLDyV
0 17 Y110‑p LkNLQLDyVDLYLIH
0 2 K123‑ub IHFPVSVkPGEEVIP
0 1 K161‑ac CKDAGLAksIGVSNF
0 8 K161‑ub CKDAGLAksIGVSNF
0 1 S162‑p KDAGLAksIGVSNFN
0 2 K179‑ac LLEMILNkPGLkYkP
0 7 K179‑ub LLEMILNkPGLkYkP
0 2 K183‑ub ILNkPGLkYkPVCNQ
0 8 K185‑ub NkPGLkYkPVCNQVE
0 67 Y196‑p NQVECHPyFNQRkLL
0 2 K201‑ub HPyFNQRkLLDFCks
0 5 K207‑ub RkLLDFCkskDIVLV
0 3 S208‑p kLLDFCkskDIVLVA
0 1 K209‑ub LLDFCkskDIVLVAY
0 1 Y216 kDIVLVAYSALGSHR
0 1 S221 VAYSALGSHREEPWV
0 12 K246‑ac PVLCALAkkHKRTPA
0 2 K246‑ub PVLCALAkkHKRTPA
0 1 K247‑ac VLCALAkkHKRTPAL
0 1 K247‑ub VLCALAkkHKRTPAL
0 2 K270‑ac RGVVVLAkSYNEQRI
0 6 K270‑ub RGVVVLAkSYNEQRI
0 1 N273 VVLAkSYNEQRIRQN
0 1 R278 SYNEQRIRQNVQVFE
0 1 K294 QLTSEEMKAIDGLNR
0 4 Y305‑p GLNRNVRyLTLDIFA
0 4 Y317‑p IFAGPPNyPFSDEY_
  mouse

 
I9 NSKCHCVILNDGNFI
A24 PVLGFGTALPLECPK
K31 ALPLECPKSKAKELT
K33 PLECPKSKAKELTkI
K39‑ub SKAKELTkIAIDAGF
K68 VGEAIRSKIADGTVR
R75 KIADGTVRREDIFYT
Y81 VRREDIFYTSKVWCt
T88‑p YTSKVWCtsLHPELV
S89‑p TSKVWCtsLHPELVR
Q104 ASLERSLQKLQFDYV
Y110 LQKLQFDYVDLYLIH
K123 IHYPMALKPGEENFP
K161 CKDAGLTKSIGVSNF
K161‑ub CKDAGLTkSIGVSNF
S162 KDAGLTkSIGVSNFN
K179 QLEMILNKPGLKYkP
K179‑ub QLEMILNkPGLKYkP
K183 ILNkPGLKYkPVCNQ
K185‑ub NkPGLKYkPVCNQVE
Y196 NQVECHPYLNQMKLL
K201 HPYLNQMKLLDFCKs
K207 MKLLDFCKsKDIVLV
S208‑p KLLDFCKsKDIVLVA
K209 LLDFCKsKDIVLVAy
Y216‑p KDIVLVAyGVLGtQR
T221‑p VAyGVLGtQRYGGWV
K246 PVLGSMAKKYNRTPA
K246‑ub PVLGSMAkKYNRTPA
K247 VLGSMAkKYNRTPAL
K247 VLGSMAkKYNRTPAL
T270 RGIVVLNTSLkEERI
T270 RGIVVLNTSLkEERI
K273‑ub VVLNTSLkEERIkEN
K278‑ub SLkEERIkENMQVFE
K294‑ub QLSSEDMkVLDGLNR
Y305 GLNRNMRYIPAAIFK
W317 IFKGHPNWPFLDEY_
  rat

 
K9 NSKCHCVKLNDGHFI
A24 PVLGFGTAMPSELPK
K31 AMPSELPKSKAKEVT
K33 PSELPKSKAKEVTKI
K39 SKAKEVTKIAIDAGF
K68 VGEAIREKIANGTTR
R75 KIANGTTRREDIFYT
Y81 TRREDIFYTSKLWCT
T88 YTSKLWCTSLHPELV
S89 TSKLWCTSLHPELVR
K104 SSLECSLKKLQLDYV
Y110 LKKLQLDYVDLYLIH
K123 IHFPMALKPGDENFP
K161 CKDAGLAKSIGVSNF
K161 CKDAGLAKSIGVSNF
S162 KDAGLAKSIGVSNFN
K179‑ac QLEKILNkPGLKYKP
K179 QLEKILNKPGLKYKP
K183 ILNkPGLKYKPVCNQ
K185 NkPGLKYKPVCNQVE
Y196 NQVECHLYLNQMKLL
K201 HLYLNQMKLLDFCKT
K207 MKLLDFCKTNGIILV
T208 KLLDFCKTNGIILVA
N209 LLDFCKTNGIILVAY
Y216 NGIILVAYGVLGTQR
T221 VAYGVLGTQRYNGWV
K246 PVLSSMAKKYNQTPA
K246 PVLSSMAKKYNQTPA
K247 VLSSMAKKYNQTPAL
K247 VLSSMAKKYNQTPAL
T270 RGIVVLNTSLKEERI
T270 RGIVVLNTSLKEERI
K273 VVLNTSLKEERIKEN
K278 SLKEERIKENMKLSP
K289 KLSPEDMKVLDDLNR
Y300 DLNRNLRYIAGGIFE
F312 IFEGHPNFPFLDEY_
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