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Protein Page:
HADH2 (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
HADH2 Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD). Defects in HSD17B10 are the cause of 2-methyl-3- hydroxybutyryl-CoA dehydrogenase deficiency (MHBD deficiency). MHBD deficiency leads to neurological abnormalities, including psychomotor retardation, and, in virtually all patients, loss of mental and motor skills. Defects in HSD17B10 are the cause of mental retardation syndromic X-linked type 10 (MRXS10). MRXS10 is characterized by mild mental retardation, choreoathetosis and abnormal behavior. A chromosomal microduplication involving HSD17B10 and HUWE1 is the cause of mental retardation X-linked type 17 (MRX17); also known as mental retardation X-linked type 31 (MRX31). Mental retardation is characterized by significantly sub- average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. In contrast to syndromic or specific X- linked mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non- syndromic X-linked mental retardation. Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Oxidoreductase; Amino Acid Metabolism - valine, leucine and isoleucine degradation; EC 1.1.1.35; Mitochondrial; EC 1.1.1.178
Cellular Component: mitochondrion; mitochondrial matrix; endoplasmic reticulum; cytoplasm; mitochondrial inner membrane; plasma membrane
Molecular Function: 3(or 17)beta-hydroxysteroid dehydrogenase activity; protein binding; 7-alpha-hydroxysteroid dehydrogenase activity; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; 3-hydroxyacyl-CoA dehydrogenase activity
Biological Process: tRNA processing; branched chain family amino acid catabolic process; lipid metabolic process
Reference #:  Q99714 (UniProtKB)
Alt. Names/Synonyms: 17-beta-HSD 10; 17-beta-hydroxysteroid dehydrogenase 10; 17-beta-hydroxysteroid dehydrogenase type 10; 17b-HSD10; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase type II; 3-hydroxyacyl-CoA dehydrogenase type-2; AB-binding alcohol dehydrogenase; ABAD; amyloid-beta binding polypeptide; amyloid-beta peptide binding alcohol dehydrogenase; CAMR; DUPXp11.22; Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; ERAB; HADH2; HCD2; HSD17B10; hydroxysteroid (17-beta) dehydrogenase 10; mental retardation, X-linked, syndromic 10; mental retardation, X-linked, syndromic 11; MHBD; Mitochondrial ribonuclease P protein 2; Mitochondrial RNase P protein 2; MRPP2; MRX17; MRX31; MRXS10; SCHAD; SDR5C1; short chain dehydrogenase/reductase family 5C, member 1; short chain L-3-hydroxyacyl-CoA dehydrogenase type 2; short chain type dehydrogenase/reductase XH98G2; Short-chain type dehydrogenase/reductase XH98G2; type 10 17b-HSD; type 10 17beta-hydroxysteroid dehydrogenase; Type II HADH; XH98G2
Gene Symbols: HSD17B10
Molecular weight: 26,923 Da
Basal Isoelectric point: 7.65  Predict pI for various phosphorylation states
Select Structure to View Below

HADH2

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

 
1 4 K9 AAACRSVKGLVAVIT
0 1 K9 AAACRSVKGLVAVIT
0 28 E28 GLGLATAERLVGQGA
0 1 E28 GLGLATAERLVGQGA
0 1 S36-p RLVGQGAsAVLLDLP
0 3 S45-p VLLDLPNsGGEAQAk
0 42 K52-ac sGGEAQAkkLGNNCV
0 1 K52-ub sGGEAQAkkLGNNCV
0 1 K52-sc sGGEAQAkkLGNNCV
0 11 K53 GGEAQAkKLGNNCVF
0 2 K53-ub GGEAQAkkLGNNCVF
0 1 K53 GGEAQAkKLGNNCVF
0 2 K69-ac PADVTSEkDVQTALA
0 2 K69-sc PADVTSEkDVQTALA
0 1 K79 QTALALAKGKFGRVD
0 1 K79-ub QTALALAkGKFGRVD
0 1 K79-sc QTALALAkGKFGRVD
0 1 K99-ub AGIAVASkTYNLKKG
0 2 K99-sc AGIAVASkTYNLKKG
0 1 K104 ASkTYNLKKGQTHTL
0 12 Q107 TYNLKKGQTHTLEDF
0 2 Q107 TYNLKKGQTHTLEDF
0 1 T179-p KGGIVGMtLPIARDL
0 2 K212 LLTSLPEKVCNFLAs
0 1 K212 LLTSLPEKVCNFLAs
0 1 K212 LLTSLPEKVCNFLAs
0 1 S219-p KVCNFLAsQVPFPSR
  mouse

► Hide Isoforms
 
K9 AAAVRSVKGLVAVVT
K9 AAAVRSVKGLVAVVT
K28-ac GPWLATAkRLVGQGA
K28 GPWLATAKRLVGQGA
T36 RLVGQGATAVLLDVP
S45 VLLDVPDSEGESQAk
K52-ac SEGESQAkkLGESCI
K52 SEGESQAKkLGESCI
K52 SEGESQAKkLGESCI
K53 EGESQAkKLGESCIF
K53 EGESQAkKLGESCIF
K53-sc EGESQAkkLGESCIF
K69 PANVTSEKEIQAALT
K69-sc PANVTSEkEIQAALT
K79 QAALTLAKEKFGRID
K79 QAALTLAKEKFGRID
K79 QAALTLAKEKFGRID
K99 AGIAVAIKTYHQkKN
K99-sc AGIAVAIkTYHQkKN
K104-ac AIkTYHQkKNkIHTL
K107-ac TYHQkKNkIHTLEDF
K107-sc TYHQkKNkIHTLEDF
T179 KGGIDGMTLPIARDL
K212 LLTTLPEKVRNFLAS
K212 LLTTLPEKVRNFLAS
K212-sc LLTTLPEkVRNFLAS
S219 kVRNFLASQVPFPSR
  HADH2 iso5  
K9-ac AAAVRSVkGLVAVVT
K9-ub AAAVRSVkGLVAVVT
K28-ac GLGLATAkRLVGQGA
K28-sc GLGLATAkRLVGQGA
T36 RLVGQGATAVLLDVP
S45-p VLLDVPDsEGEAQAk
K52-ac sEGEAQAkkLGESCI
K52 sEGEAQAKkLGESCI
K52-sc sEGEAQAkkLGESCI
K53-ac EGEAQAkkLGESCIF
K53 EGEAQAkKLGESCIF
K53 EGEAQAkKLGESCIF
K69-ac PANVTSEkEIQAALT
K69 PANVTSEKEIQAALT
K79-ac QAALTLAkEKFGRID
K79 QAALTLAKEKFGRID
K79-sc QAALTLAkEKFGRID
K99 AGIAVAIKTYHQKKN
K99 AGIAVAIKTYHQKKN
K104 AIKTYHQKKNKIHTL
K107 TYHQKKNKIHTLEDF
K107 TYHQKKNKIHTLEDF
T179 KGGIVGMTLPIARDL
K212-ac LLTTLPEkVRNFLAS
K212-ub LLTTLPEkVRNFLAS
K212 LLTTLPEKVRNFLAS
S219 kVRNFLASQVPFPSR
  rat

 
K9-ac AAAVRSVkGLVAVIT
K9 AAAVRSVKGLVAVIT
K28 GLGLSTAKRLVGQGA
K28 GLGLSTAKRLVGQGA
T36 RLVGQGATAVLLDVP
S45 VLLDVPNSEGETEAK
K52 SEGETEAKKLGGNCI
K52 SEGETEAKKLGGNCI
K52 SEGETEAKKLGGNCI
K53 EGETEAKKLGGNCIF
K53 EGETEAKKLGGNCIF
K53 EGETEAKKLGGNCIF
K69 PANVTSEKEVQAALT
K69 PANVTSEKEVQAALT
K79 QAALTLAKEKFGRID
K79 QAALTLAKEKFGRID
K79 QAALTLAKEKFGRID
K99 AGIAVAIKTYHEKKN
K99 AGIAVAIKTYHEKKN
K104 AIKTYHEKKNQVHTL
Q107 TYHEKKNQVHTLEDF
Q107 TYHEKKNQVHTLEDF
T179 KGGIVGMTLPIARDL
K212 LLTTLPDKVRNFLAS
K212 LLTTLPDKVRNFLAS
K212 LLTTLPDKVRNFLAS
S219 KVRNFLASQVPFPSR
  pig

 
K9 AAACRSVKGLVAIIT
K9 AAACRSVKGLVAIIT
E28 GLGLATAERLVGQGA
E28 GLGLATAERLVGQGA
S36 RLVGQGASAVLLDLP
S45-p VLLDLPHsDGEAQAK
K52 sDGEAQAKKLGKSCA
K52 sDGEAQAKKLGKSCA
K52 sDGEAQAKKLGKSCA
K53 DGEAQAKKLGKSCAF
K53 DGEAQAKKLGKSCAF
K53 DGEAQAKKLGKSCAF
K69 PADVTSEKDVQAALT
K69 PADVTSEKDVQAALT
K79 QAALTLAKEKFGRVD
K79 QAALTLAKEKFGRVD
K79 QAALTLAKEKFGRVD
K99 AGIGVASKTYNLKKS
K99 AGIGVASKTYNLKKS
K104 ASKTYNLKKSQAHTL
Q107 TYNLKKSQAHTLEDF
Q107 TYNLKKSQAHTLEDF
T179 KGGIVSMTLPIARDL
K212 LLNTLPDKVRNFLAN
K212 LLNTLPDKVRNFLAN
K212 LLNTLPDKVRNFLAN
N219 KVRNFLANQVPFPSR
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