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Q8N465

- D2HDH_HUMAN

UniProt

Q8N465 - D2HDH_HUMAN

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Protein

D-2-hydroxyglutarate dehydrogenase, mitochondrial

Gene
D2HGDH, D2HGD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate.1 Publication

Catalytic activityi

(R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor.

Cofactori

FAD Reviewed prediction.

Enzyme regulationi

Activated by zinc and cobalt.1 Publication

GO - Molecular functioni

  1. (R)-2-hydroxyglutarate dehydrogenase activity Source: HGNC
  2. flavin adenine dinucleotide binding Source: InterPro
  3. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: Reactome
  2. cellular metabolic process Source: Reactome
  3. cellular protein metabolic process Source: HGNC
  4. response to cobalt ion Source: HGNC
  5. response to manganese ion Source: HGNC
  6. response to zinc ion Source: HGNC
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_25367. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

Names & Taxonomyi

Protein namesi
Recommended name:
D-2-hydroxyglutarate dehydrogenase, mitochondrial (EC:1.1.99.-)
Gene namesi
Name:D2HGDH
Synonyms:D2HGD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:28358. D2HGDH.

Subcellular locationi

Mitochondrion Inferred 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

D-2-hydroxyglutaric aciduria 1 (D2HGA1) [MIM:600721]: A rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti147 – 1471I → S in D2HGA1; severe phenotype; loss of catalytic activity. 1 Publication
VAR_025890
Natural varianti375 – 3751D → Y in D2HGA1. 1 Publication
VAR_025891
Natural varianti439 – 4391N → D in D2HGA1; mild phenotype; altered catalytic activity. 1 Publication
VAR_025893
Natural varianti444 – 4441V → A in D2HGA1; severe phenotype; altered catalytic activity. 1 Publication
VAR_025894

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi600721. phenotype.
Orphaneti79315. D-2-hydroxyglutaric aciduria.
PharmGKBiPA143485446.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1313Mitochondrion Reviewed predictionAdd
BLAST
Chaini14 – 521508D-2-hydroxyglutarate dehydrogenase, mitochondrialPRO_0000231674Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-succinyllysine By similarity

Proteomic databases

MaxQBiQ8N465.
PaxDbiQ8N465.
PeptideAtlasiQ8N465.
PRIDEiQ8N465.

PTM databases

PhosphoSiteiQ8N465.

Expressioni

Gene expression databases

ArrayExpressiQ8N465.
BgeeiQ8N465.
CleanExiHS_D2HGDH.
GenevestigatoriQ8N465.

Organism-specific databases

HPAiHPA056216.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RAB25P577351EBI-1053783,EBI-1050500

Protein-protein interaction databases

BioGridi608722. 3 interactions.
STRINGi9606.ENSP00000315351.

Structurei

3D structure databases

ProteinModelPortaliQ8N465.
SMRiQ8N465. Positions 61-517.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 275180FAD-binding PCMH-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0277.
HOGENOMiHOG000230997.
HOVERGENiHBG079809.
InParanoidiQ8N465.
OMAiVYEWTAR.
OrthoDBiEOG7BS49D.
PhylomeDBiQ8N465.
TreeFamiTF323342.

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N465-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MLPRRPLAWP AWLLRGAPGA AGSWGRPVGP LARRGCCSAP GTPEVPLTRE    50
RYPVRRLPFS TVSKQDLAAF ERIVPGGVVT DPEALQAPNV DWLRTLRGCS 100
KVLLRPRTSE EVSHILRHCH ERNLAVNPQG GNTGMVGGSV PVFDEIILST 150
ARMNRVLSFH SVSGILVCQA GCVLEELSRY VEERDFIMPL DLGAKGSCHI 200
GGNVATNAGG LRFLRYGSLH GTVLGLEVVL ADGTVLDCLT SLRKDNTGYD 250
LKQLFIGSEG TLGIITTVSI LCPPKPRAVN VAFLGCPGFA EVLQTFSTCK 300
GMLGEILSAF EFMDAVCMQL VGRHLHLASP VQESPFYVLI ETSGSNAGHD 350
AEKLGHFLEH ALGSGLVTDG TMATDQRKVK MLWALRERIT EALSRDGYVY 400
KYDLSLPVER LYDIVTDLRA RLGPHAKHVV GYGHLGDGNL HLNVTAEAFS 450
PSLLAALEPH VYEWTAGQQG SVSAEHGVGF RKRDVLGYSK PPGALQLMQQ 500
LKALLDPKGI LNPYKTLPSQ A 521
Length:521
Mass (Da):56,416
Last modified:April 4, 2006 - v3
Checksum:i65D88C4315FA45CE
GO
Isoform 2 (identifier: Q8N465-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-172: ILVCQAGC → GL
     285-313: GCPGFAEVLQTFSTCKGMLGEILSAFEFM → VTCVLPACGPGSPRPARLPHPALRTPGLR
     314-521: Missing.

Note: No experimental confirmation available.

Show »
Length:307
Mass (Da):32,933
Checksum:i2EA2EA997C5E4968
GO
Isoform 3 (identifier: Q8N465-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     285-319: GCPGFAEVLQTFSTCKGMLGEILSAFEFMDAVCMQ → VTCVPPACGPGSPRPARLPHPALRTPGVCPQPLRL
     320-521: Missing.

Note: No experimental confirmation available.

Show »
Length:319
Mass (Da):34,173
Checksum:i6C7BDA672635D743
GO

Sequence cautioni

The sequence AAX82020.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151R → G.1 Publication
Corresponds to variant rs4675887 [ dbSNP | Ensembl ].
VAR_025889
Natural varianti147 – 1471I → S in D2HGA1; severe phenotype; loss of catalytic activity. 1 Publication
VAR_025890
Natural varianti338 – 3381V → I.
Corresponds to variant rs1106639 [ dbSNP | Ensembl ].
VAR_050433
Natural varianti361 – 3611A → V.
Corresponds to variant rs1105273 [ dbSNP | Ensembl ].
VAR_050434
Natural varianti375 – 3751D → Y in D2HGA1. 1 Publication
VAR_025891
Natural varianti436 – 4361G → V.1 Publication
VAR_025892
Natural varianti439 – 4391N → D in D2HGA1; mild phenotype; altered catalytic activity. 1 Publication
VAR_025893
Natural varianti444 – 4441V → A in D2HGA1; severe phenotype; altered catalytic activity. 1 Publication
VAR_025894

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei165 – 1728ILVCQAGC → GL in isoform 2. VSP_017876
Alternative sequencei285 – 31935GCPGF…AVCMQ → VTCVPPACGPGSPRPARLPH PALRTPGVCPQPLRL in isoform 3. VSP_054389Add
BLAST
Alternative sequencei285 – 31329GCPGF…AFEFM → VTCVLPACGPGSPRPARLPH PALRTPGLR in isoform 2. VSP_017877Add
BLAST
Alternative sequencei314 – 521208Missing in isoform 2. VSP_017878Add
BLAST
Alternative sequencei320 – 521202Missing in isoform 3. VSP_054390Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551R → Q in AAH36604. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK304773 mRNA. Translation: BAG65528.1.
AC114730 Genomic DNA. Translation: AAX82020.1. Sequence problems.
BC036604 mRNA. Translation: AAH36604.2.
BC071598 mRNA. Translation: AAH71598.1.
CCDSiCCDS33426.1. [Q8N465-1]
RefSeqiNP_001274178.1. NM_001287249.1.
NP_689996.4. NM_152783.4. [Q8N465-1]
UniGeneiHs.516813.

Genome annotation databases

EnsembliENST00000321264; ENSP00000315351; ENSG00000180902. [Q8N465-1]
ENST00000342518; ENSP00000339536; ENSG00000180902.
GeneIDi728294.
KEGGihsa:728294.
UCSCiuc002wce.1. human. [Q8N465-1]

Polymorphism databases

DMDMi91208273.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK304773 mRNA. Translation: BAG65528.1 .
AC114730 Genomic DNA. Translation: AAX82020.1 . Sequence problems.
BC036604 mRNA. Translation: AAH36604.2 .
BC071598 mRNA. Translation: AAH71598.1 .
CCDSi CCDS33426.1. [Q8N465-1 ]
RefSeqi NP_001274178.1. NM_001287249.1.
NP_689996.4. NM_152783.4. [Q8N465-1 ]
UniGenei Hs.516813.

3D structure databases

ProteinModelPortali Q8N465.
SMRi Q8N465. Positions 61-517.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 608722. 3 interactions.
STRINGi 9606.ENSP00000315351.

PTM databases

PhosphoSitei Q8N465.

Polymorphism databases

DMDMi 91208273.

Proteomic databases

MaxQBi Q8N465.
PaxDbi Q8N465.
PeptideAtlasi Q8N465.
PRIDEi Q8N465.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321264 ; ENSP00000315351 ; ENSG00000180902 . [Q8N465-1 ]
ENST00000342518 ; ENSP00000339536 ; ENSG00000180902 .
GeneIDi 728294.
KEGGi hsa:728294.
UCSCi uc002wce.1. human. [Q8N465-1 ]

Organism-specific databases

CTDi 728294.
GeneCardsi GC02P242673.
H-InvDB HIX0023187.
HGNCi HGNC:28358. D2HGDH.
HPAi HPA056216.
MIMi 600721. phenotype.
609186. gene.
neXtProti NX_Q8N465.
Orphaneti 79315. D-2-hydroxyglutaric aciduria.
PharmGKBi PA143485446.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0277.
HOGENOMi HOG000230997.
HOVERGENi HBG079809.
InParanoidi Q8N465.
OMAi VYEWTAR.
OrthoDBi EOG7BS49D.
PhylomeDBi Q8N465.
TreeFami TF323342.

Enzyme and pathway databases

Reactomei REACT_25367. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

Miscellaneous databases

GeneWikii D2HGDH.
GenomeRNAii 728294.
NextBioi 126719.
PROi Q8N465.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8N465.
Bgeei Q8N465.
CleanExi HS_D2HGDH.
Genevestigatori Q8N465.

Family and domain databases

Gene3Di 1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProi IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view ]
Pfami PF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view ]
SUPFAMi SSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEi PS51387. FAD_PCMH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Uterus.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Hippocampus and Placenta.
  4. "Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
    Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
    Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION.
  5. "Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria."
    Struys E.A., Salomons G.S., Achouri Y., van Schaftingen E., Grosso S., Craigen W.J., Verhoeven N.M., Jakobs C.
    Am. J. Hum. Genet. 76:358-360(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS D2HGA1 SER-147 AND ALA-444, CHARACTERIZATION OF VARIANTS D2HGA1 SER-147 AND ALA-444.
  6. Cited for: VARIANT D2HGA1 ASP-439, CHARACTERIZATION OF VARIANT D2HGA1 ASP-439.
  7. "Phenotypic heterogeneity in the presentation of D-2-hydroxyglutaric aciduria in monozygotic twins."
    Misra V.K., Struys E.A., O'brien W., Salomons G.S., Glover T., Jakobs C., Innis J.W.
    Mol. Genet. Metab. 86:200-205(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT D2HGA1 TYR-375.
  8. "D-2-Hydroxyglutaric aciduria in three patients with proven SSADH deficiency: genetic coincidence or a related biochemical epiphenomenon?"
    Struys E.A., Verhoeven N.M., Salomons G.S., Berthelot J., Vianay-Saban C., Chabrier S., Thomas J.A., Tsai A.C.-H., Gibson K.M., Jakobs C.
    Mol. Genet. Metab. 88:53-57(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLY-15 AND VAL-436.

Entry informationi

Entry nameiD2HDH_HUMAN
AccessioniPrimary (citable) accession number: Q8N465
Secondary accession number(s): B4E3L6
, E7ENP2, Q6IQ24, Q8N5Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: September 3, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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