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Q00796

- DHSO_HUMAN

UniProt

Q00796 - DHSO_HUMAN

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

Functioni

Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm By similarity.1 Publication

Catalytic activityi

L-iditol + NAD+ = L-sorbose + NADH.

Cofactori

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Zinc; catalytic
Binding sitei51 – 511Substrate By similarity
Metal bindingi70 – 701Zinc; catalytic
Metal bindingi71 – 711Zinc; catalytic
Binding sitei156 – 1561Substrate By similarity
Binding sitei299 – 2991Substrate By similarity
Binding sitei300 – 3001Substrate By similarity

GO - Molecular functioni

  1. L-iditol 2-dehydrogenase activity Source: UniProtKB
  2. NAD binding Source: UniProtKB
  3. carbohydrate binding Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. L-xylitol catabolic process Source: UniProtKB
  2. L-xylitol metabolic process Source: UniProtKB
  3. fructose biosynthetic process Source: UniProtKB
  4. glucose metabolic process Source: UniProtKB
  5. sorbitol catabolic process Source: UniProtKB
  6. sperm motility Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

SABIO-RKQ00796.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorbitol dehydrogenase (EC:1.1.1.14)
Alternative name(s):
L-iditol 2-dehydrogenase
Gene namesi
Name:SORD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11184. SORD.

Subcellular locationi

Mitochondrion membrane; Peripheral membrane protein. Cell projectionciliumflagellum
Note: Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface By similarity.

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. membrane Source: UniProtKB
  4. mitochondrial membrane Source: UniProtKB-SubCell
  5. motile cilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Flagellum, Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 357356Sorbitol dehydrogenase
PRO_0000160817Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ00796.
PaxDbiQ00796.
PRIDEiQ00796.

2D gel databases

REPRODUCTION-2DPAGEIPI00216057.

PTM databases

PhosphoSiteiQ00796.

Expressioni

Tissue specificityi

Expressed in kidney and epithelial cells of both benign and malignant prostate tissue. Expressed in epididymis (at protein level).3 Publications

Inductioni

Up-regulated by androgens and down-regulated by castration.1 Publication

Gene expression databases

ArrayExpressiQ00796.
BgeeiQ00796.
CleanExiHS_SORD.
GenevestigatoriQ00796.

Organism-specific databases

HPAiHPA040260.
HPA040621.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi112535. 33 interactions.
IntActiQ00796. 1 interaction.
MINTiMINT-5004436.
STRINGi9606.ENSP00000267814.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 167
Beta strandi19 – 246
Beta strandi34 – 4411
Helixi46 – 549
Beta strandi55 – 573
Beta strandi71 – 799
Beta strandi91 – 944
Beta strandi96 – 983
Helixi104 – 1074
Helixi111 – 1133
Beta strandi130 – 1367
Helixi137 – 1393
Beta strandi140 – 1423
Helixi149 – 16820
Beta strandi175 – 1795
Helixi183 – 19412
Beta strandi198 – 2058
Helixi207 – 2159
Beta strandi219 – 2235
Helixi229 – 24012
Beta strandi245 – 2495
Helixi254 – 26310
Beta strandi269 – 2724
Helixi284 – 2896
Beta strandi293 – 2964
Helixi304 – 3129
Helixi319 – 3213
Beta strandi322 – 3276
Helixi328 – 3303
Helixi331 – 3399
Beta strandi344 – 3496

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PL6X-ray2.00A/B/C/D2-357[»]
1PL7X-ray2.20A/B/C/D2-357[»]
1PL8X-ray1.90A/B/C/D2-357[»]
ProteinModelPortaliQ00796.
SMRiQ00796. Positions 2-357.

Miscellaneous databases

EvolutionaryTraceiQ00796.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1063.
HOGENOMiHOG000294670.
HOVERGENiHBG005484.
InParanoidiQ00796.
KOiK00008.
OMAiGPMIVEG.
OrthoDBiEOG7DRJ36.
PhylomeDBiQ00796.
TreeFamiTF313060.

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.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q00796-1 [UniParc]FASTAAdd to Basket

« Hide

MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH    50
YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR 100
ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE 150
EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV 200
VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC 250
TGAEASIQAG IYATRSGGNL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY 300
CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC 350
DPSDQNP 357
Length:357
Mass (Da):38,325
Last modified:March 23, 2010 - v4
Checksum:iFF13DDD5EBE47754
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti239 – 2391Q → L.1 Publication
Corresponds to variant rs55739437 [ dbSNP | Ensembl ].
VAR_000430
Natural varianti269 – 2691N → T.5 Publications
Corresponds to variant rs2229659 [ dbSNP | Ensembl ].
VAR_060351

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51Missing AA sequence 1 Publication
Sequence conflicti59 – 591N → D AA sequence 1 Publication
Sequence conflicti186 – 1861M → E AA sequence 1 Publication
Sequence conflicti281 – 2811T → S AA sequence 1 Publication
Sequence conflicti289 – 2891I → T AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07361 mRNA. Translation: AAA66064.1.
L29008 mRNA. Translation: AAA80565.1.
L29254
, L29249, L29250, L29251, L29252, L29253 Genomic DNA. Translation: AAA80566.1.
U67243
, U67236, U67237, U67238, U67239, U67240, U67241, U67242 Genomic DNA. Translation: AAB61898.1.
AK312444 mRNA. Translation: BAG35352.1.
AC090888 Genomic DNA. No translation available.
AC091117 Genomic DNA. No translation available.
BC021085 mRNA. Translation: AAH21085.1.
BC025295 mRNA. Translation: AAH25295.1.
CCDSiCCDS10116.1.
PIRiA54674.
RefSeqiNP_003095.2. NM_003104.5.
UniGeneiHs.878.

Genome annotation databases

EnsembliENST00000267814; ENSP00000267814; ENSG00000140263.
GeneIDi6652.
KEGGihsa:6652.
UCSCiuc001zul.4. human.

Polymorphism databases

DMDMi292495088.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07361 mRNA. Translation: AAA66064.1 .
L29008 mRNA. Translation: AAA80565.1 .
L29254
, L29249 , L29250 , L29251 , L29252 , L29253 Genomic DNA. Translation: AAA80566.1 .
U67243
, U67236 , U67237 , U67238 , U67239 , U67240 , U67241 , U67242 Genomic DNA. Translation: AAB61898.1 .
AK312444 mRNA. Translation: BAG35352.1 .
AC090888 Genomic DNA. No translation available.
AC091117 Genomic DNA. No translation available.
BC021085 mRNA. Translation: AAH21085.1 .
BC025295 mRNA. Translation: AAH25295.1 .
CCDSi CCDS10116.1.
PIRi A54674.
RefSeqi NP_003095.2. NM_003104.5.
UniGenei Hs.878.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PL6 X-ray 2.00 A/B/C/D 2-357 [» ]
1PL7 X-ray 2.20 A/B/C/D 2-357 [» ]
1PL8 X-ray 1.90 A/B/C/D 2-357 [» ]
ProteinModelPortali Q00796.
SMRi Q00796. Positions 2-357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112535. 33 interactions.
IntActi Q00796. 1 interaction.
MINTi MINT-5004436.
STRINGi 9606.ENSP00000267814.

Chemistry

ChEMBLi CHEMBL2275.
DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei Q00796.

Polymorphism databases

DMDMi 292495088.

2D gel databases

REPRODUCTION-2DPAGE IPI00216057.

Proteomic databases

MaxQBi Q00796.
PaxDbi Q00796.
PRIDEi Q00796.

Protocols and materials databases

DNASUi 6652.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000267814 ; ENSP00000267814 ; ENSG00000140263 .
GeneIDi 6652.
KEGGi hsa:6652.
UCSCi uc001zul.4. human.

Organism-specific databases

CTDi 6652.
GeneCardsi GC15P045315.
HGNCi HGNC:11184. SORD.
HPAi HPA040260.
HPA040621.
MIMi 182500. gene.
neXtProti NX_Q00796.
PharmGKBi PA36021.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1063.
HOGENOMi HOG000294670.
HOVERGENi HBG005484.
InParanoidi Q00796.
KOi K00008.
OMAi GPMIVEG.
OrthoDBi EOG7DRJ36.
PhylomeDBi Q00796.
TreeFami TF313060.

Enzyme and pathway databases

SABIO-RK Q00796.

Miscellaneous databases

EvolutionaryTracei Q00796.
GeneWikii SORD.
GenomeRNAii 6652.
NextBioi 25929.
PROi Q00796.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q00796.
Bgeei Q00796.
CleanExi HS_SORD.
Genevestigatori Q00796.

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.
[Graphical view ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 1 hit.
PROSITEi PS00059. ADH_ZINC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization."
    Lee F.K., Cheung M.C., Chung S.
    Genomics 21:354-358(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-269.
    Tissue: Liver.
  2. "Structural organization of the human sorbitol dehydrogenase gene (SORD)."
    Iwata T., Popescu N.C., Zimonjic D.B., Karlsson C., Hoeoeg J.-O., Vaca G., Rodriguez I.R., Carper D.
    Genomics 26:55-62(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS LEU-239 AND THR-269.
  3. "Identification and characterisation of a sequence related to human sorbitol dehydrogenase."
    Carr I.M., Markham A.F., Coletta P.L.
    Eur. J. Biochem. 245:760-767(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-269.
  4. "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], VARIANT THR-269.
    Tissue: Brain.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [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], VARIANT THR-269.
    Tissue: Brain and Lymph.
  7. "Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme."
    Karlsson C., Maret W., Auld D.S., Hoeoeg J.-O., Joernvall H.
    Eur. J. Biochem. 186:543-550(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-357.
    Tissue: Liver.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
    Tissue: Platelet.
  9. "Polyol pathway in human epididymis and semen."
    Frenette G., Thabet M., Sullivan R.
    J. Androl. 27:233-239(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Sorbitol dehydrogenase expression is regulated by androgens in the human prostate."
    Szabo Z., Hamalainen J., Loikkanen I., Moilanen A.M., Hirvikoski P., Vaisanen T., Paavonen T.K., Vaarala M.H.
    Oncol. Rep. 23:1233-1239(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  12. "ZAC1 is up-regulated by hypertonicity and decreases sorbitol dehydrogenase expression, allowing accumulation of sorbitol in kidney cells."
    Lanaspa M.A., Andres-Hernando A., Rivard C.J., Dai Y., Li N., Berl T.
    J. Biol. Chem. 284:19974-19981(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiDHSO_HUMAN
AccessioniPrimary (citable) accession number: Q00796
Secondary accession number(s): B2R655
, J3JZZ5, Q16682, Q9UMD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 23, 2010
Last modified: July 9, 2014
This is version 160 of the entry and version 4 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

The polyol pathway is proposed to be involved the cellular toxicity of diabetic hyperglycemia.

Keywords - Technical termi

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

Documents

  1. Human chromosome 15
    Human chromosome 15: 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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