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Q6NVY1

- HIBCH_HUMAN

UniProt

Q6NVY1 - HIBCH_HUMAN

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Protein

3-hydroxyisobutyryl-CoA hydrolase, mitochondrial

Gene

HIBCH

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

Functioni

Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA.1 Publication

Catalytic activityi

3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei121 – 1211Substrate
Binding sitei146 – 1461Substrate; via amide nitrogen
Binding sitei169 – 1691Substrate
Binding sitei177 – 1771Substrate

GO - Molecular functioni

  1. 3-hydroxyisobutyryl-CoA hydrolase activity Source: UniProtKB

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. valine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Branched-chain amino acid catabolism

Enzyme and pathway databases

BRENDAi3.1.2.4. 2681.
ReactomeiREACT_197. Branched-chain amino acid catabolism.
SABIO-RKQ6NVY1.
UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC:3.1.2.4)
Alternative name(s):
3-hydroxyisobutyryl-coenzyme A hydrolase
Short name:
HIB-CoA hydrolase
Short name:
HIBYL-CoA-H
Gene namesi
Name:HIBCH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4908. HIBCH.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

HIBCH deficiency (HIBCHD) [MIM:250620]: The enzyme defect results in accumulation of methacrylyl-CoA, a highly reactive compound, which readily undergoes addition reactions with free sulfhydryl groups. Affected individuals showed delayed development of motor skills, hypotonia, initial poor feeding, and a deterioration in neurological function during first stages of life.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221Y → C in HIBCHD. 1 Publication
VAR_031870

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi250620. phenotype.
Orphaneti88639. Neurodegeneration due to 3-hydroxyisobutyryl-CoA hydrolase deficiency.
PharmGKBiPA29281.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionBy similarityAdd
BLAST
Chaini33 – 3863543-hydroxyisobutyryl-CoA hydrolase, mitochondrialPRO_0000284929Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
Modified residuei92 – 921N6-acetyllysine; alternate1 Publication
Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
Modified residuei221 – 2211N6-acetyllysine; alternateBy similarity
Modified residuei221 – 2211N6-succinyllysine; alternateBy similarity
Modified residuei257 – 2571N6-succinyllysineBy similarity
Modified residuei297 – 2971N6-acetyllysine; alternateBy similarity
Modified residuei297 – 2971N6-succinyllysine; alternateBy similarity
Modified residuei301 – 3011N6-succinyllysineBy similarity
Modified residuei353 – 3531N6-acetyllysine; alternateBy similarity
Modified residuei353 – 3531N6-succinyllysine; alternateBy similarity
Modified residuei360 – 3601N6-acetyllysineBy similarity
Modified residuei365 – 3651N6-acetyllysineBy similarity
Modified residuei377 – 3771N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ6NVY1.
PaxDbiQ6NVY1.
PeptideAtlasiQ6NVY1.
PRIDEiQ6NVY1.

2D gel databases

REPRODUCTION-2DPAGEIPI00419802.

PTM databases

PhosphoSiteiQ6NVY1.

Expressioni

Tissue specificityi

Highly expressed in liver and kidney, also detected in heart, muscle and brain (at protein level). Not detected in lung.1 Publication

Gene expression databases

BgeeiQ6NVY1.
CleanExiHS_HIBCH.
ExpressionAtlasiQ6NVY1. baseline and differential.
GenevestigatoriQ6NVY1.

Organism-specific databases

HPAiHPA036540.
HPA036541.

Interactioni

Protein-protein interaction databases

BioGridi117658. 9 interactions.
IntActiQ6NVY1. 2 interactions.
STRINGi9606.ENSP00000352706.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 437Combined sources
Beta strandi46 – 516Combined sources
Helixi54 – 563Combined sources
Helixi62 – 7716Combined sources
Beta strandi83 – 886Combined sources
Beta strandi91 – 955Combined sources
Helixi100 – 1078Combined sources
Helixi114 – 12916Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi141 – 1444Combined sources
Helixi146 – 1494Combined sources
Turni150 – 1534Combined sources
Beta strandi154 – 1596Combined sources
Beta strandi164 – 1663Combined sources
Helixi169 – 1713Combined sources
Helixi180 – 1867Combined sources
Helixi191 – 1988Combined sources
Helixi205 – 2095Combined sources
Beta strandi214 – 2163Combined sources
Helixi219 – 2213Combined sources
Helixi222 – 23110Combined sources
Helixi237 – 25014Combined sources
Turni253 – 2564Combined sources
Helixi262 – 2643Combined sources
Helixi265 – 2717Combined sources
Beta strandi274 – 2763Combined sources
Helixi277 – 28711Combined sources
Helixi290 – 29910Combined sources
Helixi304 – 31714Combined sources
Helixi322 – 33716Combined sources
Helixi341 – 3499Combined sources
Helixi364 – 3663Combined sources
Helixi369 – 3768Combined sources
Helixi380 – 3823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BPTX-ray1.50A32-386[»]
ProteinModelPortaliQ6NVY1.
SMRiQ6NVY1. Positions 32-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6NVY1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00570000079226.
HOVERGENiHBG054809.
InParanoidiQ6NVY1.
KOiK05605.
OMAiVASLCHA.
PhylomeDBiQ6NVY1.
TreeFamiTF314329.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6NVY1-1) [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

        10         20         30         40         50
MGQREMWRLM SRFNAFKRTN TILHHLRMSK HTDAAEEVLL EKKGCTGVIT
60 70 80 90 100
LNRPKFLNAL TLNMIRQIYP QLKKWEQDPE TFLIIIKGAG GKAFCAGGDI
110 120 130 140 150
RVISEAEKAK QKIAPVFFRE EYMLNNAVGS CQKPYVALIH GITMGGGVGL
160 170 180 190 200
SVHGQFRVAT EKCLFAMPET AIGLFPDVGG GYFLPRLQGK LGYFLALTGF
210 220 230 240 250
RLKGRDVYRA GIATHFVDSE KLAMLEEDLL ALKSPSKENI ASVLENYHTE
260 270 280 290 300
SKIDRDKSFI LEEHMDKINS CFSANTVEEI IENLQQDGSS FALEQLKVIN
310 320 330 340 350
KMSPTSLKIT LRQLMEGSSK TLQEVLTMEY RLSQACMRGH DFHEGVRAVL
360 370 380
IDKDQSPKWK PADLKEVTEE DLNNHFKSLG SSDLKF
Length:386
Mass (Da):43,482
Last modified:May 1, 2007 - v2
Checksum:i11B0632ED1DF2FFA
GO
Isoform 2 (identifier: Q6NVY1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     338-385: Missing.

Note: No experimental confirmation available.

Show »
Length:338
Mass (Da):38,012
Checksum:i747FD3FC0745E844
GO

Sequence cautioni

The sequence AAC52114.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH05190.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAY24178.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD96699.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD96743.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411E → G in AAH67822. (PubMed:15489334)Curated
Sequence conflicti83 – 831L → V in AAC52114. (PubMed:8824301)Curated
Sequence conflicti111 – 1111Q → R in BAD96699. 1 PublicationCurated
Sequence conflicti184 – 19815LPRLQ…FLALT → FATTPRKTWLLPCIN in AAC52114. (PubMed:8824301)CuratedAdd
BLAST
Sequence conflicti369 – 3691E → K in BAD96699. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461T → A.3 Publications
Corresponds to variant rs1058180 [ dbSNP | Ensembl ].
VAR_031869
Natural varianti122 – 1221Y → C in HIBCHD. 1 Publication
VAR_031870

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei338 – 38548Missing in isoform 2. CuratedVSP_024780Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66669 mRNA. Translation: AAC52114.1. Different initiation.
AK222979 mRNA. Translation: BAD96699.1. Different initiation.
AK223023 mRNA. Translation: BAD96743.1. Different initiation.
AC092178 Genomic DNA. Translation: AAY24178.1. Different initiation.
AC010679 Genomic DNA. Translation: AAX93234.1.
CH471058 Genomic DNA. Translation: EAX10873.1.
CH471058 Genomic DNA. Translation: EAX10875.1.
BC005190 mRNA. Translation: AAH05190.2. Different initiation.
BC067822 mRNA. Translation: AAH67822.1.
CCDSiCCDS2304.1. [Q6NVY1-1]
CCDS46475.1. [Q6NVY1-2]
RefSeqiNP_055177.2. NM_014362.3. [Q6NVY1-1]
NP_932164.1. NM_198047.2. [Q6NVY1-2]
UniGeneiHs.656685.

Genome annotation databases

EnsembliENST00000359678; ENSP00000352706; ENSG00000198130. [Q6NVY1-1]
ENST00000392332; ENSP00000376144; ENSG00000198130. [Q6NVY1-2]
GeneIDi26275.
KEGGihsa:26275.
UCSCiuc002uru.3. human. [Q6NVY1-1]
uc002urv.3. human. [Q6NVY1-2]

Polymorphism databases

DMDMi146324905.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66669 mRNA. Translation: AAC52114.1 . Different initiation.
AK222979 mRNA. Translation: BAD96699.1 . Different initiation.
AK223023 mRNA. Translation: BAD96743.1 . Different initiation.
AC092178 Genomic DNA. Translation: AAY24178.1 . Different initiation.
AC010679 Genomic DNA. Translation: AAX93234.1 .
CH471058 Genomic DNA. Translation: EAX10873.1 .
CH471058 Genomic DNA. Translation: EAX10875.1 .
BC005190 mRNA. Translation: AAH05190.2 . Different initiation.
BC067822 mRNA. Translation: AAH67822.1 .
CCDSi CCDS2304.1. [Q6NVY1-1 ]
CCDS46475.1. [Q6NVY1-2 ]
RefSeqi NP_055177.2. NM_014362.3. [Q6NVY1-1 ]
NP_932164.1. NM_198047.2. [Q6NVY1-2 ]
UniGenei Hs.656685.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BPT X-ray 1.50 A 32-386 [» ]
ProteinModelPortali Q6NVY1.
SMRi Q6NVY1. Positions 32-386.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117658. 9 interactions.
IntActi Q6NVY1. 2 interactions.
STRINGi 9606.ENSP00000352706.

PTM databases

PhosphoSitei Q6NVY1.

Polymorphism databases

DMDMi 146324905.

2D gel databases

REPRODUCTION-2DPAGE IPI00419802.

Proteomic databases

MaxQBi Q6NVY1.
PaxDbi Q6NVY1.
PeptideAtlasi Q6NVY1.
PRIDEi Q6NVY1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359678 ; ENSP00000352706 ; ENSG00000198130 . [Q6NVY1-1 ]
ENST00000392332 ; ENSP00000376144 ; ENSG00000198130 . [Q6NVY1-2 ]
GeneIDi 26275.
KEGGi hsa:26275.
UCSCi uc002uru.3. human. [Q6NVY1-1 ]
uc002urv.3. human. [Q6NVY1-2 ]

Organism-specific databases

CTDi 26275.
GeneCardsi GC02M191054.
HGNCi HGNC:4908. HIBCH.
HPAi HPA036540.
HPA036541.
MIMi 250620. phenotype.
610690. gene.
neXtProti NX_Q6NVY1.
Orphaneti 88639. Neurodegeneration due to 3-hydroxyisobutyryl-CoA hydrolase deficiency.
PharmGKBi PA29281.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1024.
GeneTreei ENSGT00570000079226.
HOVERGENi HBG054809.
InParanoidi Q6NVY1.
KOi K05605.
OMAi VASLCHA.
PhylomeDBi Q6NVY1.
TreeFami TF314329.

Enzyme and pathway databases

UniPathwayi UPA00362 .
BRENDAi 3.1.2.4. 2681.
Reactomei REACT_197. Branched-chain amino acid catabolism.
SABIO-RK Q6NVY1.

Miscellaneous databases

EvolutionaryTracei Q6NVY1.
GenomeRNAii 26275.
NextBioi 48577.
PROi Q6NVY1.
SOURCEi Search...

Gene expression databases

Bgeei Q6NVY1.
CleanExi HS_HIBCH.
ExpressionAtlasi Q6NVY1. baseline and differential.
Genevestigatori Q6NVY1.

Family and domain databases

Gene3Di 1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProi IPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
[Graphical view ]
SUPFAMi SSF52096. SSF52096. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and tissue-specific expression of human beta-hydroxyisobutyryl-coenzyme A hydrolase."
    Hawes J.W., Jaskiewicz J., Shimomura Y., Huang B., Bunting J., Harper E.T., Harris R.A.
    J. Biol. Chem. 271:26430-26434(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-46.
    Tissue: Small intestine.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-46.
  5. "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 ALA-46.
    Tissue: Testis.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Crystal structure of human beta-hydroxyisobutyryl-COA hydrolase in complex with quercetin."
    Structural genomics consortium (SGC)
    Submitted (JAN-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 32-386 IN COMPLEX WITH 3-HYDROXY-2-METHYLPROPANOIC ACID AND QUERCETIN.
  9. "Mutations in the gene encoding 3-hydroxyisobutyryl-CoA hydrolase results in progressive infantile neurodegeneration."
    Loupatty F.J., Clayton P.T., Ruiter J.P.N., Ofman R., Ijlst L., Brown G.K., Thorburn D.R., Harris R.A., Duran M., Desousa C., Krywawych S., Heales S.J.R., Wanders R.J.A.
    Am. J. Hum. Genet. 80:195-199(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIBCHD CYS-122.

Entry informationi

Entry nameiHIBCH_HUMAN
AccessioniPrimary (citable) accession number: Q6NVY1
Secondary accession number(s): D3DPI4
, Q53GA8, Q53GF2, Q53RF7, Q53TC6, Q92931, Q9BS94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: November 26, 2014
This is version 100 of the entry and version 2 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

3D-structure, 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3