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P08319

- ADH4_HUMAN

UniProt

P08319 - ADH4_HUMAN

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Protein
Alcohol dehydrogenase 4
Gene
ADH4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Zinc 1; catalytic
Metal bindingi69 – 691Zinc 1; catalytic
Metal bindingi99 – 991Zinc 2
Metal bindingi102 – 1021Zinc 2
Metal bindingi105 – 1051Zinc 2
Metal bindingi113 – 1131Zinc 2
Metal bindingi180 – 1801Zinc 1; catalytic
Binding sitei229 – 2291NAD
Binding sitei234 – 2341NAD
Binding sitei375 – 3751NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 492NAD
Nucleotide bindingi205 – 2106NAD
Nucleotide bindingi298 – 3003NAD
Nucleotide bindingi323 – 3253NAD

GO - Molecular functioni

  1. NAD binding Source: UniProtKB
  2. NADPH:quinone reductase activity Source: UniProtKB
  3. alcohol dehydrogenase (NAD) activity Source: UniProtKB
  4. alcohol dehydrogenase activity, zinc-dependent Source: UniProtKB
  5. alditol:NADP+ 1-oxidoreductase activity Source: Ensembl
  6. all-trans retinal binding Source: UniProtKB
  7. benzaldehyde dehydrogenase activity Source: UniProtKB
  8. ethanol binding Source: InterPro
  9. oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: UniProtKB
  10. retinol binding Source: UniProtKB
  11. retinol dehydrogenase activity Source: UniProtKB
  12. zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. alcohol catabolic process Source: UniProtKB
  2. alcohol metabolic process Source: UniProtKB
  3. cellular aldehyde metabolic process Source: UniProtKB
  4. ethanol oxidation Source: UniProtKB
  5. quinone metabolic process Source: UniProtKB
  6. retinoid metabolic process Source: UniProtKB
  7. retinol metabolic process Source: UniProtKB
  8. small molecule metabolic process Source: Reactome
  9. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS06569-MONOMER.
ReactomeiREACT_34. Ethanol oxidation.
SABIO-RKP08319.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase 4 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase class II pi chain
Gene namesi
Name:ADH4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:252. ADH4.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24573.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Alcohol dehydrogenase 4
PRO_0000160681Add
BLAST

Proteomic databases

MaxQBiP08319.
PaxDbiP08319.
PRIDEiP08319.

PTM databases

PhosphoSiteiP08319.

Expressioni

Gene expression databases

ArrayExpressiP08319.
BgeeiP08319.
CleanExiHS_ADH4.
GenevestigatoriP08319.

Organism-specific databases

HPAiHPA020525.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi106639. 4 interactions.
IntActiP08319. 1 interaction.
STRINGi9606.ENSP00000265512.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158
Beta strandi23 – 297
Beta strandi36 – 4510
Helixi48 – 525
Beta strandi63 – 653
Beta strandi70 – 789
Beta strandi90 – 934
Beta strandi100 – 1023
Turni103 – 1064
Helixi122 – 1243
Beta strandi135 – 1384
Beta strandi141 – 1444
Turni147 – 1493
Beta strandi152 – 1598
Beta strandi162 – 1654
Helixi172 – 1754
Helixi176 – 1794
Helixi181 – 19010
Turni191 – 1933
Beta strandi200 – 2045
Helixi208 – 21912
Beta strandi223 – 2286
Helixi232 – 2343
Helixi235 – 2406
Beta strandi244 – 2474
Helixi249 – 2513
Helixi256 – 2638
Beta strandi268 – 2736
Helixi278 – 2869
Turni290 – 2923
Beta strandi293 – 2975
Beta strandi307 – 3093
Helixi311 – 3155
Beta strandi318 – 3225
Helixi325 – 3273
Helixi330 – 34213
Helixi349 – 3513
Beta strandi352 – 3576
Helixi358 – 3603
Helixi361 – 3699
Beta strandi374 – 3796

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3COSX-ray2.10A/B/C/D1-380[»]
ProteinModelPortaliP08319.
SMRiP08319. Positions 1-380.

Miscellaneous databases

EvolutionaryTraceiP08319.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1062.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP08319.
KOiK13980.
OMAiPLTNLCG.
OrthoDBiEOG72NRQ6.
PhylomeDBiP08319.
TreeFamiTF300429.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR028632. Zinc_ADH_II.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PTHR11695:SF308. PTHR11695:SF308. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P08319-1) [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

MGTKGKVIKC KAAIAWEAGK PLCIEEVEVA PPKAHEVRIQ IIATSLCHTD    50
ATVIDSKFEG LAFPVIVGHE AAGIVESIGP GVTNVKPGDK VIPLYAPLCR 100
KCKFCLSPLT NLCGKISNLK SPASDQQLME DKTSRFTCKG KPVYHFFGTS 150
TFSQYTVVSD INLAKIDDDA NLERVCLLGC GFSTGYGAAI NNAKVTPGST 200
CAVFGLGGVG LSAVMGCKAA GASRIIGIDI NSEKFVKAKA LGATDCLNPR 250
DLHKPIQEVI IELTKGGVDF ALDCAGGSET MKAALDCTTA GWGSCTFIGV 300
AAGSKGLTIF PEELIIGRTI NGTFFGGWKS VDSIPKLVTD YKNKKFNLDA 350
LVTHTLPFDK ISEAFDLMNQ GKSVRTILIF 380
Length:380
Mass (Da):40,222
Last modified:October 5, 2010 - v5
Checksum:i45721A08197629F1
GO
Isoform 2 (identifier: P08319-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MGTKGK → MLVRGPHFELQRCKTHLFSSNYLTQ

Show »
Length:399
Mass (Da):42,607
Checksum:iC4ABEC85C04B6C2D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti309 – 3091I → V.2 Publications
Corresponds to variant rs1126671 [ dbSNP | Ensembl ].
VAR_023461
Natural varianti318 – 3181R → H.1 Publication
Corresponds to variant rs29001219 [ dbSNP | Ensembl ].
VAR_023462
Natural varianti374 – 3741V → I.2 Publications
Corresponds to variant rs1126673 [ dbSNP | Ensembl ].
VAR_023463

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MGTKGK → MLVRGPHFELQRCKTHLFSS NYLTQ in isoform 2.
VSP_036788

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521T → S in AAA51595. 1 Publication
Sequence conflicti52 – 521T → S in CAA39813. 1 Publication
Sequence conflicti380 – 3801F → FGRCQEQFRILSD in AAA51595. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15943 mRNA. Translation: AAA51595.1.
X56411
, X56412, X56413, X56414, X56415, X56416, X56417, X56418, X56419 Genomic DNA. Translation: CAA39813.1.
AK290835 mRNA. Translation: BAF83524.1.
AK295556 mRNA. Translation: BAG58459.1.
AY974245 Genomic DNA. Translation: AAX59034.1.
AC019131 Genomic DNA. No translation available.
AP002026 Genomic DNA. No translation available.
BC022319 mRNA. Translation: AAH22319.1.
CCDSiCCDS34032.1. [P08319-1]
PIRiA27109. DEHUAP.
RefSeqiNP_000661.2. NM_000670.3. [P08319-1]
UniGeneiHs.1219.

Genome annotation databases

EnsembliENST00000265512; ENSP00000265512; ENSG00000198099. [P08319-1]
ENST00000423445; ENSP00000397939; ENSG00000198099. [P08319-2]
ENST00000505590; ENSP00000425416; ENSG00000198099. [P08319-2]
ENST00000508393; ENSP00000424630; ENSG00000198099. [P08319-2]
GeneIDi127.
KEGGihsa:127.
UCSCiuc003hun.3. human. [P08319-1]
uc011ced.2. human. [P08319-2]

Polymorphism databases

DMDMi308153684.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15943 mRNA. Translation: AAA51595.1 .
X56411
, X56412 , X56413 , X56414 , X56415 , X56416 , X56417 , X56418 , X56419 Genomic DNA. Translation: CAA39813.1 .
AK290835 mRNA. Translation: BAF83524.1 .
AK295556 mRNA. Translation: BAG58459.1 .
AY974245 Genomic DNA. Translation: AAX59034.1 .
AC019131 Genomic DNA. No translation available.
AP002026 Genomic DNA. No translation available.
BC022319 mRNA. Translation: AAH22319.1 .
CCDSi CCDS34032.1. [P08319-1 ]
PIRi A27109. DEHUAP.
RefSeqi NP_000661.2. NM_000670.3. [P08319-1 ]
UniGenei Hs.1219.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3COS X-ray 2.10 A/B/C/D 1-380 [» ]
ProteinModelPortali P08319.
SMRi P08319. Positions 1-380.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106639. 4 interactions.
IntActi P08319. 1 interaction.
STRINGi 9606.ENSP00000265512.

Chemistry

BindingDBi P08319.
ChEMBLi CHEMBL2096668.
DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei P08319.

Polymorphism databases

DMDMi 308153684.

Proteomic databases

MaxQBi P08319.
PaxDbi P08319.
PRIDEi P08319.

Protocols and materials databases

DNASUi 127.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265512 ; ENSP00000265512 ; ENSG00000198099 . [P08319-1 ]
ENST00000423445 ; ENSP00000397939 ; ENSG00000198099 . [P08319-2 ]
ENST00000505590 ; ENSP00000425416 ; ENSG00000198099 . [P08319-2 ]
ENST00000508393 ; ENSP00000424630 ; ENSG00000198099 . [P08319-2 ]
GeneIDi 127.
KEGGi hsa:127.
UCSCi uc003hun.3. human. [P08319-1 ]
uc011ced.2. human. [P08319-2 ]

Organism-specific databases

CTDi 127.
GeneCardsi GC04M100044.
H-InvDB HIX0200651.
HGNCi HGNC:252. ADH4.
HPAi HPA020525.
MIMi 103740. gene.
neXtProti NX_P08319.
PharmGKBi PA24573.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1062.
HOGENOMi HOG000294674.
HOVERGENi HBG000195.
InParanoidi P08319.
KOi K13980.
OMAi PLTNLCG.
OrthoDBi EOG72NRQ6.
PhylomeDBi P08319.
TreeFami TF300429.

Enzyme and pathway databases

BioCyci MetaCyc:HS06569-MONOMER.
Reactomei REACT_34. Ethanol oxidation.
SABIO-RK P08319.

Miscellaneous databases

EvolutionaryTracei P08319.
GeneWikii ADH4.
GenomeRNAii 127.
NextBioi 507.
PROi P08319.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08319.
Bgeei P08319.
CleanExi HS_ADH4.
Genevestigatori P08319.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR028632. Zinc_ADH_II.
[Graphical view ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
PTHR11695:SF308. PTHR11695:SF308. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 2 hits.
PROSITEi PS00059. ADH_ZINC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit."
    Hoeoeg J.-O., von Bahr-Lindstroem H., Heden L.-O., Holmquist B., Larsson K., Hempel J., Vallee B.L., Joernvall H.
    Biochemistry 26:1926-1932(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. "Cloning and characterization of the human ADH4 gene."
    von Bahr-Lindstroem H., Joernvall H., Hoeoeg J.-O.
    Gene 103:269-274(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Fetal liver.
  3. "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] (ISOFORMS 1 AND 2), VARIANTS VAL-309 AND ILE-374.
    Tissue: Hippocampus and Liver.
  4. NIEHS SNPs program
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-318.
  5. "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].
  6. "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] (ISOFORM 1), VARIANTS VAL-309 AND ILE-374.
    Tissue: Liver.
  7. "Crystal structure of human class II alcohol dehydrogenase (ADH4) in complex with NAD and Zn."
    Structural genomics consortium (SGC)
    Submitted (APR-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.

Entry informationi

Entry nameiADH4_HUMAN
AccessioniPrimary (citable) accession number: P08319
Secondary accession number(s): A8K470
, B4DIE7, C9J4A9, Q8TCD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 156 of the entry and version 5 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

Miscellaneous

There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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