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Two-dimensional polyacrylamide gel electrophoresis database


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Searching in 'USC-OGP 2-DE database' for entry matching: Q99714




USC-OGP 2-DE database:  Q99714


Q99714


General information about the entry
View entry in simple text format
Entry nameHCD2_HUMAN
Primary accession numberQ99714
integrated into USC-OGP 2-DE database on January 17, 2017 (release 1)
2D Annotations were last modified onJanuary 17, 2017 (version 1)
General Annotations were last modified on April 5, 2017 (version 2)
Name and origin of the protein
DescriptionRecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2; EC=1.1.1.35; AltName: Full=17-beta-hydroxysteroid dehydrogenase 10; Short=17-beta-HSD 10; EC=1.1.1.51; AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase; EC=1.1.1.178; AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II; AltName: Full=Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; AltName: Full=Mitochondrial ribonuclease P protein 2; Short=Mitochondrial RNase P protein 2; AltName: Full=Short chain dehydrogenase/reductase family 5C member 1; AltName: Full=Short-chain type dehydrogenase/reductase XH98G2; AltName: Full=Type II HADH;.
Gene nameName=HSD17B10
Synonyms=ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
References
[1]   2D GEL CHARACTERIZATION
Author 1., Author 2.
Submitted (Mar-2011) to Current
2D PAGE maps for identified proteins
How to interpret a protein

UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10}
Homo sapiens (Human)
UVEAL_MELANOMA_3-10
  map experimental info
 
UVEAL_MELANOMA_3-10

MAP LOCATIONS:
pI=6.52; Mw=25485

Cross-references
UniProtKB/Swiss-ProtQ99714; HCD2_HUMAN.



2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 0.0
Entry nameHCD2_HUMAN
Primary accession numberQ99714
Secondary accession number(s) Q5H927 Q6IBS9 Q8TCV9 Q96HD5
Sequence was last modified on January 23, 2007 (version 3)
Annotations were last modified on March 15, 2017 (version 190)
Name and origin of the protein
DescriptionRecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2; EC=1.1.1.35; AltName: Full=17-beta-hydroxysteroid dehydrogenase 10; Short=17-beta-HSD 10; EC=1.1.1.51; AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase; EC=1.1.1.178; AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II; AltName: Full=Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; AltName: Full=Mitochondrial ribonuclease P protein 2; Short=Mitochondrial RNase P protein 2; AltName: Full=Short chain dehydrogenase/reductase family 5C member 1; AltName: Full=Short-chain type dehydrogenase/reductase XH98G2; AltName: Full=Type II HADH;
Gene nameName=HSD17B10
Synonyms=ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2
Encoded onName=HSD17B10; Synonyms=ERAB, HADH2, MRPP2, SCHAD, SDR5C1, XH98G2
Keywords3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement; Complete proteome; Disease mutation; Mental retardation; Mitochondrion; NAD; Oxidoreductase; Reference proteome; tRNA processing.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLU96132; AAC51812.1; -; mRNA
EMBLU73514; AAB68958.1; -; mRNA
EMBLAF069134; AAC39900.1; -; mRNA
EMBLAF035555; AAC15902.1; -; mRNA
EMBLAF037438; AAC16419.1; -; Genomic_DNA
EMBLCR456723; CAG33004.1; -; mRNA
EMBLZ97054; CAI42652.1; -; Genomic_DNA
EMBLZ97054; CAI42653.1; -; Genomic_DNA
EMBLCH471154; EAW93157.1; -; Genomic_DNA
EMBLCH471154; EAW93158.1; -; Genomic_DNA
EMBLBC000372; AAH00372.1; -; mRNA
EMBLBC008708; AAH08708.1; -; mRNA
EMBLAY092415; AAM18189.1; -; mRNA
CCDSCCDS14354.1; -. [Q99714-1]; .
CCDSCCDS35300.1; -. [Q99714-2]; .
RefSeqNP_001032900.1; NM_001037811.2. [Q99714-2]; .
RefSeqNP_004484.1; NM_004493.2. [Q99714-1]; .
UniGeneHs.171280; -; .
PDB1F67; Model; -; A=1-261
PDB1SO8; X-ray; 2.30 A; A=1-261
PDB1U7T; X-ray; 2.00 A; A/B/C/D=1-261
PDB2O23; X-ray; 1.20 A; A/B=1-261
PDBsum1F67; -; .
PDBsum1SO8; -; .
PDBsum1U7T; -; .
PDBsum2O23; -; .
ProteinModelPortalQ99714; -; .
SMRQ99714; -; .
BioGrid109278; 243; .
IntActQ99714; 26; .
MINTMINT-3059664; -; .
STRING9606.ENSP00000168216; -; .
ChEMBLCHEMBL4159; -; .
DrugBankDB00157; NADH; .
SwissLipidsSLP:000000787; -; .
iPTMnetQ99714; -; .
PhosphoSitePlusQ99714; -; .
SwissPalmQ99714; -; .
BioMutaHSD17B10; -; .
DMDM2492759; -; .
REPRODUCTION-2DPAGEIPI00017726; -; .
REPRODUCTION-2DPAGEQ99714; -; .
UCD-2DPAGEQ99714; -; .
EPDQ99714; -; .
MaxQBQ99714; -; .
PaxDbQ99714; -; .
PeptideAtlasQ99714; -; .
PRIDEQ99714; -; .
TopDownProteomicsQ99714-1; -. [Q99714-1]; .
TopDownProteomicsQ99714-2; -. [Q99714-2]; .
DNASU3028; -; .
EnsemblENST00000168216; ENSP00000168216; ENSG00000072506. [Q99714-1]; .
EnsemblENST00000375304; ENSP00000364453; ENSG00000072506. [Q99714-2]; .
GeneID3028; -; .
KEGGhsa:3028; -; .
UCSCuc004dsl.2; human. [Q99714-1]; .
CTD3028; -; .
DisGeNET3028; -; .
GeneCardsHSD17B10; -; .
HGNCHGNC:4800; HSD17B10; .
HPAHPA001432; -; .
MalaCardsHSD17B10; -; .
MIM300220; phenotype; .
MIM300256; gene; .
MIM300438; phenotype; .
MIM300705; phenotype; .
neXtProtNX_Q99714; -; .
OpenTargetsENSG00000072506; -; .
Orphanet85295; HSD10 disease; atypical type; .
Orphanet391428; HSD10 disease; infantile type; .
Orphanet391457; HSD10 disease; neonatal type; .
PharmGKBPA162391638; -; .
eggNOGKOG1199; Eukaryota; .
eggNOGENOG410XNNW; LUCA; .
GeneTreeENSGT00760000118868; -; .
HOVERGENHBG002145; -; .
InParanoidQ99714; -; .
KOK08683; -; .
OMALMGLVNC; -; .
OrthoDBEOG091G0G9O; -; .
PhylomeDBQ99714; -; .
TreeFamTF354307; -; .
BioCycMetaCyc:HS01071-MONOMER; -; .
BRENDA1.1.1.178; 2681; .
BRENDA1.1.1.35; 2681; .
ReactomeR-HSA-6785470; tRNA processing in the mitochondrion; .
ReactomeR-HSA-6787450; tRNA modification in the mitochondrion; .
ReactomeR-HSA-70895; Branched-chain amino acid catabolism; .
ReactomeR-HSA-8868766; rRNA processing in the mitochondrion; .
SABIO-RKQ99714; -; .
ChiTaRSHSD17B10; human; .
EvolutionaryTraceQ99714; -; .
GeneWikiHSD17B10; -; .
GenomeRNAi3028; -; .
PROPR:Q99714; -; .
ProteomesUP000005640; Chromosome X; .
BgeeENSG00000072506; -; .
CleanExHS_HSD17B10; -; .
ExpressionAtlasQ99714; baseline and differential; .
GenevisibleQ99714; HS; .
GOGO:0005737; C:cytoplasm; TAS:ProtInc; .
GOGO:0005759; C:mitochondrial matrix; TAS:Reactome; .
GOGO:0005739; C:mitochondrion; ISS:UniProtKB; .
GOGO:0005886; C:plasma membrane; TAS:ProtInc; .
GOGO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC; .
GOGO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; EXP:Reactome; .
GOGO:0008709; F:cholate 7-alpha-dehydrogenase activity; TAS:ProtInc; .
GOGO:0003723; F:RNA binding; IDA:UniProtKB; .
GOGO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC; .
GOGO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome; .
GOGO:0006629; P:lipid metabolic process; TAS:ProtInc; .
GOGO:0070901; P:mitochondrial tRNA methylation; TAS:Reactome; .
GOGO:0090646; P:mitochondrial tRNA processing; TAS:Reactome; .
Gene3D3.40.50.720; -; 1; .
InterProIPR016040; NAD(P)-bd_dom; .
InterProIPR020904; Sc_DH/Rdtase_CS; .
InterProIPR002347; SDR_fam; .
PfamPF00106; adh_short; 1; .
PRINTSPR00081; GDHRDH; .
PRINTSPR00080; SDRFAMILY; .
SUPFAMSSF51735; SSF51735; 1; .
PROSITEPS00061; ADH_SHORT; 1; .



USC-OGP 2-DE database image


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Database constructed and maintained by Angel Garcia, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server

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