Peroxisomal multifunctional enzyme type 2

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P51659 (DHB4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (7) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Peroxisomal multifunctional enzyme type 2
Short name=MFE-2

Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 4
Short name=17-beta-HSD 4
D-bifunctional protein
Short name=DBP
Multifunctional protein 2
Short name=MPF-2

Cleaved into the following 2 chains:

(3R)-hydroxyacyl-CoA dehydrogenase
EC=1.1.1.n12
Enoyl-CoA hydratase 2
EC=4.2.1.107
EC=4.2.1.119
Alternative name(s):
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase

Gene names

Name:	HSD17B4
Synonyms:	EDH17B4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	736 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids. Ref.2 Ref.5
Catalytic activity	(R)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH. Ref.2 (24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestanoyl-CoA = (24E)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA + H₂O. Ref.2 (3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H₂O. Ref.2
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Homodimer. Ref.5
Subcellular location	Peroxisome.
Tissue specificity	Present in many tissues with highest concentrations in liver, heart, prostate and testis.
Involvement in disease	Defects in HSD17B4 are a cause of D-bifunctional protein deficiency (DBPD) [MIM:261515]. DBPD is a disorder of peroxisomal fatty acid beta-oxidation. Ref.13 Ref.14 Ref.15 Defects in HSD17B4 are the cause of Perrault syndrome (PRS) [MIM:233400]. PRS is a sex-influenced disorder characterized by sensorineural deafness in both males and females and ovarian dysgenesis in females. Some patients also have neurologic manifestations, including mild mental retardation and cerebellar and peripheral nervous system involvement. Ref.16
Miscellaneous	The protein is found both as a full length peptide and in a cleaved version.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. Contains 1 MaoC-like domain. Contains 1 SCP2 domain.
Biophysicochemical properties	Kinetic parameters: K_M=10 µM for D-3-hydroxy-octanoyl-CoA Ref.2 K_M=13 µM for NAD K_M=2.7 µM for 3-ketooctanoyl-CoA K_M=5.4 µM for NADH V_max=8.8 µmol/min/mg enzyme

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Coding sequence diversity	Polymorphism
Disease	Deafness Disease mutation
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	bile acid biosynthetic process Traceable author statement. Source: Reactome fatty acid beta-oxidation using acyl-CoA oxidase Traceable author statement. Source: Reactome
Cellular component	peroxisomal matrix Traceable author statement. Source: Reactome
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Traceable author statement. Source: Reactome 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity Traceable author statement. Source: Reactome estradiol 17-beta-dehydrogenase activity Traceable author statement. Source: ProtInc isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW long-chain-enoyl-CoA hydratase activity Traceable author statement. Source: Reactome nucleotide binding Inferred from electronic annotation. Source: InterPro sterol binding Traceable author statement. Source: ProtInc sterol transporter activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 736

735

Peroxisomal multifunctional enzyme type 2

PRO_0000054583

Chain

2 – 311

310

(3R)-hydroxyacyl-CoA dehydrogenase

PRO_0000400082

Chain

312 – 736

425

Enoyl-CoA hydratase 2

PRO_0000400083

Regions

Domain

484 – 600

117

MaoC-like

Domain

624 – 736

113

SCP2

Nucleotide binding

13 – 37

NAD By similarity

Nucleotide binding

75 – 76

NAD

Nucleotide binding

164 – 168

NAD

Nucleotide binding

196 – 199

NAD

Region

2 – 305

304

(3R)-hydroxyacyl-CoA dehydrogenase

Region

322 – 622

301

Enoyl-CoA hydratase 2

Region

406 – 407

(3R)-3-hydroxydecanoyl-CoA binding By similarity

Region

510 – 515

(3R)-3-hydroxydecanoyl-CoA binding By similarity

Motif

734 – 736

Microbody targeting signal Potential

Sites

Active site

164

Proton acceptor By similarity

Binding site

NAD; via amide nitrogen

Binding site

NAD

Binding site

NAD; via carbonyl oxygen

Binding site

151

Substrate By similarity

Binding site

435

(3R)-3-hydroxydecanoyl-CoA By similarity

Binding site

533

(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen By similarity

Binding site

563

(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen By similarity

Binding site

706

Substrate

Binding site

724

Substrate

Amino acid modifications

Modified residue

Phosphoserine Ref.8

Modified residue

265

Phosphothreonine Ref.7 Ref.8

Modified residue

292

Phosphothreonine Ref.8

Modified residue

294

Phosphoserine Ref.8

Modified residue

304

Phosphoserine Ref.8

Modified residue

309

Phosphoserine Ref.8

Modified residue

317

Phosphothreonine Ref.8

Modified residue

318

Phosphoserine Ref.8

Modified residue

565

N6-acetyllysine Ref.9

Modified residue

608

Phosphothreonine Ref.8

Modified residue

663

N6-acetyllysine By similarity

Modified residue

669

N6-acetyllysine Ref.9

Modified residue

707

N6-acetyllysine Ref.9

Natural variations

Natural variant

G → S in DBPD. Ref.13

VAR_037576

Natural variant

F → L.
Corresponds to variant rs28943588 [ dbSNP | Ensembl ].

VAR_052309

Natural variant

106

R → H.
Corresponds to variant rs25640 [ dbSNP | Ensembl ].

VAR_014872

Natural variant

106

R → P in DBPD. Ref.15

VAR_065906

Natural variant

140

K → N.
Corresponds to variant rs28943589 [ dbSNP | Ensembl ].

VAR_052310

Natural variant

217

Y → C in PRS. Ref.16

VAR_065907

Natural variant

292

T → S.
Corresponds to variant rs1143650 [ dbSNP | Ensembl ].

VAR_024625

Natural variant

427

A → V.
Corresponds to variant rs28943590 [ dbSNP | Ensembl ].

VAR_052311

Natural variant

457

N → Y in DBPD; the mutation leads to an unstable protein. Ref.14

VAR_065908

Natural variant

491

A → T.
Corresponds to variant rs28943591 [ dbSNP | Ensembl ].

VAR_052312

Natural variant

511

W → R. Ref.14
Corresponds to variant rs11539471 [ dbSNP | Ensembl ].

VAR_014873

Natural variant

559

I → V.
Corresponds to variant rs11205 [ dbSNP | Ensembl ].

VAR_014874

Natural variant

606

A → S.
Corresponds to variant rs15228 [ dbSNP | Ensembl ].

VAR_052313

Natural variant

687

T → I.
Corresponds to variant rs28943592 [ dbSNP | Ensembl ].

VAR_052314

Natural variant

728

M → V.
Corresponds to variant rs28943594 [ dbSNP | Ensembl ].

VAR_052315

Experimental info

Mutagenesis

G → S: No dehydrogenase activity. Ref.6

Mutagenesis

347

Y → A: No hydratase activity. Ref.6

Mutagenesis

366

E → A: No hydratase activity. Ref.6

Mutagenesis

370

D → A: No effect. Ref.6

Mutagenesis

406

H → A: No effect. Ref.6

Mutagenesis

408

E → A: No effect. Ref.6

Mutagenesis

410

Y → A: No effect. Ref.6

Mutagenesis

490

D → A: No effect. Ref.6

Mutagenesis

505

Y → A: Completely inactive. Ref.6

Mutagenesis

510

D → A: No hydratase activity. Ref.6

Mutagenesis

515

H → A: Completely inactive. Ref.6

Mutagenesis

517

D → A: No effect. Ref.6

Mutagenesis

532

H → A: No effect. Ref.6

Secondary structure

736

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P51659 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7B11E02483328BCE
Show »

FASTA

736

79,686

        10         20         30         40         50         60 
MGSPLRFDGR VVLVTGAGAG LGRAYALAFA ERGALVVVND LGGDFKGVGK GSLAADKVVE 

        70         80         90        100        110        120 
EIRRRGGKAV ANYDSVEEGE KVVKTALDAF GRIDVVVNNA GILRDRSFAR ISDEDWDIIH 

       130        140        150        160        170        180 
RVHLRGSFQV TRAAWEHMKK QKYGRIIMTS SASGIYGNFG QANYSAAKLG LLGLANSLAI 

       190        200        210        220        230        240 
EGRKSNIHCN TIAPNAGSRM TQTVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG 

       250        260        270        280        290        300 
AGWIGKLRWE RTLGAIVRQK NHPMTPEAVK ANWKKICDFE NASKPQSIQE STGSIIEVLS 

       310        320        330        340        350        360 
KIDSEGGVSA NHTSRATSTA TSGFAGAIGQ KLPPFSYAYT ELEAIMYALG VGASIKDPKD 

       370        380        390        400        410        420 
LKFIYEGSSD FSCLPTFGVI IGQKSMMGGG LAEIPGLSIN FAKVLHGEQY LELYKPLPRA 

       430        440        450        460        470        480 
GKLKCEAVVA DVLDKGSGVV IIMDVYSYSE KELICHNQFS LFLVGSGGFG GKRTSDKVKV 

       490        500        510        520        530        540 
AVAIPNRPPD AVLTDTTSLN QAALYRLSGD WNPLHIDPNF ASLAGFDKPI LHGLCTFGFS 

       550        560        570        580        590        600 
ARRVLQQFAD NDVSRFKAIK ARFAKPVYPG QTLQTEMWKE GNRIHFQTKV QETGDIVISN 

       610        620        630        640        650        660 
AYVDLAPTSG TSAKTPSEGG KLQSTFVFEE IGRRLKDIGP EVVKKVNAVF EWHITKGGNI 

       670        680        690        700        710        720 
GAKWTIDLKS GSGKVYQGPA KGAADTTIIL SDEDFMEVVL GKLDPQKAFF SGRLKARGNI 

       730 
MLSQKLQMIL KDYAKL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV." Adamski J., Normand T., Leenders F., Monte D., Begue A., Stehelin D., Jungblut P.W., de Launoit Y. Biochem. J. 311:437-443(1995) [PubMed: 7487879] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein." Jiang L.L., Miyazawa S., Souri M., Hashimoto T. J. Biochem. 121:364-369(1997) [PubMed: 9089413] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 69-77; 81-90; 261-270; 291-310; 312-339; 413-426; 451-459; 478-488 AND 590-631, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV." Leenders F., Dolez V., Begue A., Moller G., Gloeckner J.C., de Launoit Y., Adamski J. Mamm. Genome 9:1036-1041(1998) [PubMed: 9880674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase." Jiang L.L., Kobayashi A., Matsuura H., Fukushima H., Hashimoto T. J. Biochem. 120:624-632(1996) [PubMed: 8902629] [Abstract] Cited for: FUNCTION, SUBUNIT.
[6]	"Human peroxisomal multifunctional enzyme type 2. Site-directed mutagenesis studies show the importance of two protic residues for 2-enoyl-CoA hydratase 2 activity." Qin Y.M., Haapalainen A.M., Kilpelainen S.H., Marttila M.S., Koski M.K., Glumoff T., Novikov D.K., Hiltunen J.K. J. Biol. Chem. 275:4965-4972(2000) [PubMed: 10671535] [Abstract] Cited for: MUTAGENESIS OF GLY-16; TYR-347; GLU-366; ASP-370; HIS-406; GLU-408; TYR-410; ASP-490; TYR-505; ASP-510; HIS-515; ASP-517 AND HIS-532.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-265; THR-292; SER-294; SER-304; SER-309; THR-317; SER-318 AND THR-608, MASS SPECTROMETRY.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-565; LYS-669 AND LYS-707, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution." Haapalainen A.M., van Aalten D.M., Merilaeinen G., Jalonen J.E., Pirilae P., Wierenga R.K., Hiltunen J.K., Glumoff T. J. Mol. Biol. 313:1127-1138(2001) [PubMed: 11700068] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 618-736 IN COMPLEX WITH LIGAND.
[12]	"Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2." Koski K.M., Haapalainen A.M., Hiltunen J.K., Glumoff T. J. Mol. Biol. 345:1157-1169(2005) [PubMed: 15644212] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 320-614.
[13]	"Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency." van Grunsven E.G., van Berkel E., Ijlst L., Vreken P., de Klerk J.B.C., Adamski J., Lemonde H., Clayton P.T., Cuebas D.A., Wanders R.J.A. Proc. Natl. Acad. Sci. U.S.A. 95:2128-2133(1998) [PubMed: 9482850] [Abstract] Cited for: VARIANT DBPD SER-16.
[14]	"Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency." van Grunsven E.G., Mooijer P.A., Aubourg P., Wanders R.J. Hum. Mol. Genet. 8:1509-1516(1999) [PubMed: 10400999] [Abstract] Cited for: VARIANT DBPD TYR-457, VARIANT ARG-511.
[15]	"D-bifunctional protein deficiency with fetal ascites, polyhydramnios, and contractures of hands and toes." Nakano K., Zhang Z., Shimozawa N., Kondo N., Ishii N., Funatsuka M., Shirakawa S., Itoh M., Takashima S., Une M., Kana-aki R.R., Mukai K., Osawa M., Suzuki Y. J. Pediatr. 139:865-867(2001) [PubMed: 11743515] [Abstract] Cited for: VARIANT DBPD PRO-106.
[16]	"Mutations in the DBP-deficiency protein HSD17B4 cause ovarian dysgenesis, hearing loss, and ataxia of Perrault Syndrome." Pierce S.B., Walsh T., Chisholm K.M., Lee M.K., Thornton A.M., Fiumara A., Opitz J.M., Levy-Lahad E., Klevit R.E., King M.C. Am. J. Hum. Genet. 87:282-288(2010) [PubMed: 20673864] [Abstract] Cited for: VARIANT PRS CYS-217.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X87176 mRNA. Translation: CAA60643.1.
AF057740

AF057739 Genomic DNA. Translation: AAD08652.1.
BC003098 mRNA. Translation: AAH03098.1.

IPI

IPI00019912.

PIR

S59136.

RefSeq

NP_000405.1. NM_000414.3.
NP_001186220.1. NM_001199291.1.
NP_001186221.1. NM_001199292.1.

UniGene

Hs.406861.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IKT	X-ray	1.75	A	618-736	[»]
1S9C	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L	320-614	[»]
1ZBQ	X-ray	2.71	A/B/C/D/E/F	1-304	[»]

ProteinModelPortal

P51659.

SMR

P51659. Positions 3-304, 323-606, 622-736.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51659. 13 interactions.

MINT

MINT-1135639.

STRING

P51659.

PTM databases

PhosphoSite

P51659.

Polymorphism databases

DMDM

1706396.

Proteomic databases

PeptideAtlas

P51659.

PRIDE

P51659.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256216; ENSP00000256216; ENSG00000133835.

GeneID

3295.

KEGG

hsa:3295.

UCSC

uc003ksj.2. human.

Organism-specific databases

CTD

3295.

GeneCards

GC05P118816.

H-InvDB

HIX0005116.

HGNC

HGNC:5213. HSD17B4.

HPA

HPA021302.
HPA021311.
HPA021479.

MIM

233400. phenotype.
261515. phenotype.
601860. gene.

neXtProt

NX_P51659.

Orphanet

300. Bifunctional enzyme deficiency.
2855. Perrault syndrome.
2981. Pseudo-Zellweger syndrome.
912. Zellweger syndrome.

PharmGKB

PA29481.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17870.

HOVERGEN

HBG002174.

InParanoid

P51659.

OrthoDB

EOG4255S8.

PhylomeDB

P51659.

Enzyme and pathway databases

Reactome

REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P51659.

Bgee

P51659.

CleanEx

HS_HSD17B4.

Genevestigator

P51659.

GermOnline

ENSG00000133835. Homo sapiens.

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR002539. MaoC_deHydtase.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR003033. SCP2_sterol-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

K12405.

Pfam

PF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

SUPFAM

SSF55718. SCP2. 1 hit.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00157. NADH.

NextBio

13071.

SOURCE

Search...

Entry information

Entry name

DHB4_HUMAN

Accession

Primary (citable) accession number: P51659

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents