Full text data of HDDC2
HDDC2
(C6orf74, NS5ATP2)
[Confidence: low (only semi-automatic identification from reviews)]
HD domain-containing protein 2 (Hepatitis C virus NS5A-transactivated protein 2; HCV NS5A-transactivated protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
HD domain-containing protein 2 (Hepatitis C virus NS5A-transactivated protein 2; HCV NS5A-transactivated protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q7Z4H3
ID HDDC2_HUMAN Reviewed; 204 AA.
AC Q7Z4H3; Q5TDQ4; Q6NZ49; Q9BTT2; Q9BV31; Q9Y3D1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2003, sequence version 1.
DT 22-JAN-2014, entry version 78.
DE RecName: Full=HD domain-containing protein 2;
DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 2;
DE Short=HCV NS5A-transactivated protein 2;
GN Name=HDDC2; Synonyms=C6orf74, NS5ATP2; ORFNames=CGI-130;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma;
RX PubMed=15188496;
RA Yang Q., Cheng J., Liu Y., Hong Y., Wang J.-J., Zhang S.-L.;
RT "Cloning and identification of NS5ATP2 gene and its spliced variant
RT transactivated by hepatitis C virus non-structural protein 5A.";
RL World J. Gastroenterol. 10:1735-1739(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RG Northeast structural genomics consortium (NESG);
RT "Northeast structural genomics consortium target HR6723.";
RL Submitted (APR-2012) to the PDB data bank.
CC -!- INTERACTION:
CC Q76353:- (xeno); NbExp=2; IntAct=EBI-6163836, EBI-6248077;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z4H3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4H3-2; Sequence=VSP_029556;
CC Name=3;
CC IsoId=Q7Z4H3-3; Sequence=VSP_029557, VSP_029558;
CC Note=No experimental confirmation available. May be produced at
CC very low levels due to a premature stop codon in the mRNA,
CC leading to nonsense-mediated mRNA decay;
CC -!- SIMILARITY: Belongs to the HDDC2 family.
CC -!- SIMILARITY: Contains 1 HD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34125.1; Type=Miscellaneous discrepancy; Note=Correction of a non-canonical splice junction;
CC Sequence=AAH03357.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF529363; AAQ09597.1; -; mRNA.
DR EMBL; AF151888; AAD34125.1; ALT_SEQ; mRNA.
DR EMBL; AL121938; CAI19646.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48138.1; -; Genomic_DNA.
DR EMBL; BC001671; AAH01671.1; -; mRNA.
DR EMBL; BC003357; AAH03357.2; ALT_INIT; mRNA.
DR EMBL; BC066332; AAH66332.1; -; mRNA.
DR RefSeq; NP_057147.2; NM_016063.2.
DR UniGene; Hs.32826; -.
DR PDB; 4DMB; X-ray; 1.90 A; A/B=1-204.
DR PDB; 4L1J; X-ray; 1.82 A; A/B=1-204.
DR PDB; 4L7E; X-ray; 2.23 A; A/B=1-204.
DR PDB; 4L7W; X-ray; 2.30 A; A=1-204.
DR PDBsum; 4DMB; -.
DR PDBsum; 4L1J; -.
DR PDBsum; 4L7E; -.
DR PDBsum; 4L7W; -.
DR ProteinModelPortal; Q7Z4H3; -.
DR SMR; Q7Z4H3; 11-200.
DR IntAct; Q7Z4H3; 1.
DR STRING; 9606.ENSP00000381220; -.
DR PhosphoSite; Q7Z4H3; -.
DR DMDM; 74713511; -.
DR REPRODUCTION-2DPAGE; IPI00386751; -.
DR PaxDb; Q7Z4H3; -.
DR PRIDE; Q7Z4H3; -.
DR Ensembl; ENST00000318787; ENSP00000316242; ENSG00000111906.
DR Ensembl; ENST00000368377; ENSP00000357361; ENSG00000111906.
DR Ensembl; ENST00000398153; ENSP00000381220; ENSG00000111906.
DR GeneID; 51020; -.
DR KEGG; hsa:51020; -.
DR UCSC; uc003qaa.1; human.
DR CTD; 51020; -.
DR GeneCards; GC06M125596; -.
DR HGNC; HGNC:21078; HDDC2.
DR HPA; HPA035677; -.
DR neXtProt; NX_Q7Z4H3; -.
DR PharmGKB; PA134943525; -.
DR eggNOG; COG1896; -.
DR HOGENOM; HOG000216981; -.
DR HOVERGEN; HBG097476; -.
DR InParanoid; Q7Z4H3; -.
DR KO; K07023; -.
DR OMA; PHCGVSD; -.
DR OrthoDB; EOG73NG4R; -.
DR PhylomeDB; Q7Z4H3; -.
DR ChiTaRS; HDDC2; human.
DR GenomeRNAi; 51020; -.
DR NextBio; 53540; -.
DR PRO; PR:Q7Z4H3; -.
DR ArrayExpress; Q7Z4H3; -.
DR Bgee; Q7Z4H3; -.
DR CleanEx; HS_HDDC2; -.
DR Genevestigator; Q7Z4H3; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR Gene3D; 1.10.3210.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR Pfam; PF13023; HD_3; 1.
DR SMART; SM00471; HDc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 204 HD domain-containing protein 2.
FT /FTId=PRO_0000311389.
FT DOMAIN 46 148 HD.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 70 103 Missing (in isoform 2).
FT /FTId=VSP_029556.
FT VAR_SEQ 70 71 CV -> KL (in isoform 3).
FT /FTId=VSP_029557.
FT VAR_SEQ 72 204 Missing (in isoform 3).
FT /FTId=VSP_029558.
FT VARIANT 64 64 R -> C (in dbSNP:rs12213371).
FT /FTId=VAR_037238.
FT CONFLICT 69 69 R -> P (in Ref. 2; AAD34125).
FT CONFLICT 131 131 Q -> R (in Ref. 5; AAH66332).
FT HELIX 14 25
FT HELIX 26 29
FT HELIX 33 36
FT TURN 37 39
FT HELIX 46 59
FT HELIX 67 76
FT TURN 77 80
FT HELIX 81 84
FT HELIX 89 91
FT HELIX 95 110
FT HELIX 115 130
FT HELIX 134 158
FT TURN 161 164
FT HELIX 165 171
FT HELIX 178 199
SQ SEQUENCE 204 AA; 23390 MW; E59D03224F8D6A16 CRC64;
MASVSSATFS GHGARSLLQF LRLVGQLKRV PRTGWVYRNV QRPESVSDHM YRMAVMAMVI
KDDRLNKDRC VRLALVHDMA ECIVGDIAPA DNIPKEEKHR REEEAMKQIT QLLPEDLRKE
LYELWEEYET QSSAEAKFVK QLDQCEMILQ ASEYEDLEHK PGRLQDFYDS TAGKFNHPEI
VQLVSELEAE RSTNIAAAAS EPHS
//
ID HDDC2_HUMAN Reviewed; 204 AA.
AC Q7Z4H3; Q5TDQ4; Q6NZ49; Q9BTT2; Q9BV31; Q9Y3D1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2003, sequence version 1.
DT 22-JAN-2014, entry version 78.
DE RecName: Full=HD domain-containing protein 2;
DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 2;
DE Short=HCV NS5A-transactivated protein 2;
GN Name=HDDC2; Synonyms=C6orf74, NS5ATP2; ORFNames=CGI-130;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma;
RX PubMed=15188496;
RA Yang Q., Cheng J., Liu Y., Hong Y., Wang J.-J., Zhang S.-L.;
RT "Cloning and identification of NS5ATP2 gene and its spliced variant
RT transactivated by hepatitis C virus non-structural protein 5A.";
RL World J. Gastroenterol. 10:1735-1739(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RG Northeast structural genomics consortium (NESG);
RT "Northeast structural genomics consortium target HR6723.";
RL Submitted (APR-2012) to the PDB data bank.
CC -!- INTERACTION:
CC Q76353:- (xeno); NbExp=2; IntAct=EBI-6163836, EBI-6248077;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z4H3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4H3-2; Sequence=VSP_029556;
CC Name=3;
CC IsoId=Q7Z4H3-3; Sequence=VSP_029557, VSP_029558;
CC Note=No experimental confirmation available. May be produced at
CC very low levels due to a premature stop codon in the mRNA,
CC leading to nonsense-mediated mRNA decay;
CC -!- SIMILARITY: Belongs to the HDDC2 family.
CC -!- SIMILARITY: Contains 1 HD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34125.1; Type=Miscellaneous discrepancy; Note=Correction of a non-canonical splice junction;
CC Sequence=AAH03357.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF529363; AAQ09597.1; -; mRNA.
DR EMBL; AF151888; AAD34125.1; ALT_SEQ; mRNA.
DR EMBL; AL121938; CAI19646.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48138.1; -; Genomic_DNA.
DR EMBL; BC001671; AAH01671.1; -; mRNA.
DR EMBL; BC003357; AAH03357.2; ALT_INIT; mRNA.
DR EMBL; BC066332; AAH66332.1; -; mRNA.
DR RefSeq; NP_057147.2; NM_016063.2.
DR UniGene; Hs.32826; -.
DR PDB; 4DMB; X-ray; 1.90 A; A/B=1-204.
DR PDB; 4L1J; X-ray; 1.82 A; A/B=1-204.
DR PDB; 4L7E; X-ray; 2.23 A; A/B=1-204.
DR PDB; 4L7W; X-ray; 2.30 A; A=1-204.
DR PDBsum; 4DMB; -.
DR PDBsum; 4L1J; -.
DR PDBsum; 4L7E; -.
DR PDBsum; 4L7W; -.
DR ProteinModelPortal; Q7Z4H3; -.
DR SMR; Q7Z4H3; 11-200.
DR IntAct; Q7Z4H3; 1.
DR STRING; 9606.ENSP00000381220; -.
DR PhosphoSite; Q7Z4H3; -.
DR DMDM; 74713511; -.
DR REPRODUCTION-2DPAGE; IPI00386751; -.
DR PaxDb; Q7Z4H3; -.
DR PRIDE; Q7Z4H3; -.
DR Ensembl; ENST00000318787; ENSP00000316242; ENSG00000111906.
DR Ensembl; ENST00000368377; ENSP00000357361; ENSG00000111906.
DR Ensembl; ENST00000398153; ENSP00000381220; ENSG00000111906.
DR GeneID; 51020; -.
DR KEGG; hsa:51020; -.
DR UCSC; uc003qaa.1; human.
DR CTD; 51020; -.
DR GeneCards; GC06M125596; -.
DR HGNC; HGNC:21078; HDDC2.
DR HPA; HPA035677; -.
DR neXtProt; NX_Q7Z4H3; -.
DR PharmGKB; PA134943525; -.
DR eggNOG; COG1896; -.
DR HOGENOM; HOG000216981; -.
DR HOVERGEN; HBG097476; -.
DR InParanoid; Q7Z4H3; -.
DR KO; K07023; -.
DR OMA; PHCGVSD; -.
DR OrthoDB; EOG73NG4R; -.
DR PhylomeDB; Q7Z4H3; -.
DR ChiTaRS; HDDC2; human.
DR GenomeRNAi; 51020; -.
DR NextBio; 53540; -.
DR PRO; PR:Q7Z4H3; -.
DR ArrayExpress; Q7Z4H3; -.
DR Bgee; Q7Z4H3; -.
DR CleanEx; HS_HDDC2; -.
DR Genevestigator; Q7Z4H3; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR Gene3D; 1.10.3210.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR Pfam; PF13023; HD_3; 1.
DR SMART; SM00471; HDc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 204 HD domain-containing protein 2.
FT /FTId=PRO_0000311389.
FT DOMAIN 46 148 HD.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 70 103 Missing (in isoform 2).
FT /FTId=VSP_029556.
FT VAR_SEQ 70 71 CV -> KL (in isoform 3).
FT /FTId=VSP_029557.
FT VAR_SEQ 72 204 Missing (in isoform 3).
FT /FTId=VSP_029558.
FT VARIANT 64 64 R -> C (in dbSNP:rs12213371).
FT /FTId=VAR_037238.
FT CONFLICT 69 69 R -> P (in Ref. 2; AAD34125).
FT CONFLICT 131 131 Q -> R (in Ref. 5; AAH66332).
FT HELIX 14 25
FT HELIX 26 29
FT HELIX 33 36
FT TURN 37 39
FT HELIX 46 59
FT HELIX 67 76
FT TURN 77 80
FT HELIX 81 84
FT HELIX 89 91
FT HELIX 95 110
FT HELIX 115 130
FT HELIX 134 158
FT TURN 161 164
FT HELIX 165 171
FT HELIX 178 199
SQ SEQUENCE 204 AA; 23390 MW; E59D03224F8D6A16 CRC64;
MASVSSATFS GHGARSLLQF LRLVGQLKRV PRTGWVYRNV QRPESVSDHM YRMAVMAMVI
KDDRLNKDRC VRLALVHDMA ECIVGDIAPA DNIPKEEKHR REEEAMKQIT QLLPEDLRKE
LYELWEEYET QSSAEAKFVK QLDQCEMILQ ASEYEDLEHK PGRLQDFYDS TAGKFNHPEI
VQLVSELEAE RSTNIAAAAS EPHS
//