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Q9HCC0

- MCCB_HUMAN

UniProt

Q9HCC0 - MCCB_HUMAN

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Protein

Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial

Gene

MCCC2

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

Functioni

Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism.1 Publication

Catalytic activityi

ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA.1 Publication

Kineticsi

kcat is 4.0 sec(-1).

  1. KM=45 µM for ATP1 Publication
  2. KM=74 µM for 3-methylcrotonyl-CoA1 Publication

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. methylcrotonoyl-CoA carboxylase activity Source: UniProtKB

GO - Biological processi

  1. biotin metabolic process Source: Reactome
  2. branched-chain amino acid catabolic process Source: Reactome
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. coenzyme A metabolic process Source: Ensembl
  5. leucine catabolic process Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
  7. vitamin metabolic process Source: Reactome
  8. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000131844-MONOMER.
ReactomeiREACT_11153. Biotin transport and metabolism.
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
REACT_197. Branched-chain amino acid catabolism.
UniPathwayiUPA00363; UER00861.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.4)
Short name:
MCCase subunit beta
Alternative name(s):
3-methylcrotonyl-CoA carboxylase 2
3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit
3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
Gene namesi
Name:MCCC2
Synonyms:MCCB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6937. MCCC2.

Subcellular locationi

Mitochondrion matrix 2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Methylcrotonoyl-CoA carboxylase 2 deficiency (MCC2D) [MIM:210210]: An autosomal recessive disorder of leucine catabolism. The phenotype is variable, ranging from neonatal onset with severe neurological involvement to asymptomatic adults. There is a characteristic organic aciduria with massive excretion of 3-hydroxyisovaleric acid and 3-methylcrotonylglycine, usually in combination with a severe secondary carnitine deficiency.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991E → Q in MCC2D; severe and mild form. 1 Publication
Corresponds to variant rs28934883 [ dbSNP | Ensembl ].
VAR_012792
Natural varianti155 – 1551R → Q in MCC2D; mild form. 1 Publication
VAR_012793
Natural varianti167 – 1671C → R in MCC2D. 1 Publication
Corresponds to variant rs28934884 [ dbSNP | Ensembl ].
VAR_012794
Natural varianti173 – 1731S → L in MCC2D; severe form. 1 Publication
VAR_012795
Natural varianti193 – 1931R → C in MCC2D; mild form. 1 Publication
VAR_012796
Natural varianti218 – 2181A → T in MCC2D. 1 Publication
VAR_012797
Natural varianti268 – 2681R → T in MCC2D; asymptomatic form. 1 Publication
VAR_012798
Natural varianti280 – 2801D → Y in MCC2D. 1 Publication
Corresponds to variant rs119103226 [ dbSNP | Ensembl ].
VAR_067199
Natural varianti310 – 3101P → R in MCC2D; mild form. 1 Publication
VAR_012799
Natural varianti339 – 3391V → M in MCC2D; severe form. 1 Publication
VAR_012800
Natural varianti437 – 4371I → V in MCC2D; mild form.
VAR_012801
Natural varianti459 – 4591P → S in MCC2D. 1 Publication
VAR_067200

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi210210. phenotype.
Orphaneti6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKBiPA30681.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222Mitochondrion1 PublicationAdd
BLAST
Chaini23 – 563541Methylcrotonoyl-CoA carboxylase beta chain, mitochondrialPRO_0000000291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; alternateBy similarity
Modified residuei70 – 701N6-succinyllysine; alternateBy similarity
Modified residuei141 – 1411N6-succinyllysineBy similarity
Modified residuei495 – 4951N6-acetyllysine; alternateBy similarity
Modified residuei495 – 4951N6-succinyllysine; alternateBy similarity
Modified residuei511 – 5111N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9HCC0.
PaxDbiQ9HCC0.
PRIDEiQ9HCC0.

2D gel databases

REPRODUCTION-2DPAGEIPI00784044.

PTM databases

PhosphoSiteiQ9HCC0.

Expressioni

Gene expression databases

BgeeiQ9HCC0.
CleanExiHS_MCCC2.
ExpressionAtlasiQ9HCC0. baseline and differential.
GenevestigatoriQ9HCC0.

Organism-specific databases

HPAiHPA038300.
HPA038301.

Interactioni

Subunit structurei

Probably a dodecamer composed of six biotin-containing alpha subunits (MCCC1) and six beta (MCCC2) subunits.

Protein-protein interaction databases

BioGridi122050. 19 interactions.
IntActiQ9HCC0. 12 interactions.
MINTiMINT-8051924.
STRINGi9606.ENSP00000343657.

Structurei

3D structure databases

ProteinModelPortaliQ9HCC0.
SMRiQ9HCC0. Positions 28-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 557503CarboxyltransferaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 37230Acyl-CoA bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the AccD/PCCB family.Curated
Contains 1 carboxyltransferase domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG4799.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218692.
HOVERGENiHBG052424.
InParanoidiQ9HCC0.
KOiK01969.
OMAiYSSARCW.
PhylomeDBiQ9HCC0.
TreeFamiTF300446.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

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: Q9HCC0-1) [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
MWAVLRLALR PCARASPAGP RAYHGDSVAS LGTQPDLGSA LYQENYKQMK
60 70 80 90 100
ALVNQLHERV EHIKLGGGEK ARALHISRGK LLPRERIDNL IDPGSPFLEL
110 120 130 140 150
SQFAGYQLYD NEEVPGGGII TGIGRVSGVE CMIIANDATV KGGAYYPVTV
160 170 180 190 200
KKQLRAQEIA MQNRLPCIYL VDSGGAYLPR QADVFPDRDH FGRTFYNQAI
210 220 230 240 250
MSSKNIAQIA VVMGSCTAGG AYVPAMADEN IIVRKQGTIF LAGPPLVKAA
260 270 280 290 300
TGEEVSAEDL GGADLHCRKS GVSDHWALDD HHALHLTRKV VRNLNYQKKL
310 320 330 340 350
DVTIEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFTEFKAF
360 370 380 390 400
YGDTLVTGFA RIFGYPVGIV GNNGVLFSES AKKGTHFVQL CCQRNIPLLF
410 420 430 440 450
LQNITGFMVG REYEAEGIAK DGAKMVAAVA CAQVPKITLI IGGSYGAGNY
460 470 480 490 500
GMCGRAYSPR FLYIWPNARI SVMGGEQAAN VLATITKDQR AREGKQFSSA
510 520 530 540 550
DEAALKEPII KKFEEEGNPY YSSARVWDDG IIDPADTRLV LGLSFSAALN
560
APIEKTDFGI FRM
Length:563
Mass (Da):61,333
Last modified:March 1, 2001 - v1
Checksum:i8E3D401AF52DC7D2
GO
Isoform 2 (identifier: Q9HCC0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-246: Missing.

Note: No experimental confirmation available.

Show »
Length:525
Mass (Da):57,519
Checksum:i344050ABB7A9DE8A
GO

Sequence cautioni

The sequence AAH14897.1 differs from that shown. Reason: Frameshift at position 359. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991E → Q in MCC2D; severe and mild form. 1 Publication
Corresponds to variant rs28934883 [ dbSNP | Ensembl ].
VAR_012792
Natural varianti155 – 1551R → Q in MCC2D; mild form. 1 Publication
VAR_012793
Natural varianti167 – 1671C → R in MCC2D. 1 Publication
Corresponds to variant rs28934884 [ dbSNP | Ensembl ].
VAR_012794
Natural varianti173 – 1731S → L in MCC2D; severe form. 1 Publication
VAR_012795
Natural varianti193 – 1931R → C in MCC2D; mild form. 1 Publication
VAR_012796
Natural varianti218 – 2181A → T in MCC2D. 1 Publication
VAR_012797
Natural varianti268 – 2681R → T in MCC2D; asymptomatic form. 1 Publication
VAR_012798
Natural varianti280 – 2801D → Y in MCC2D. 1 Publication
Corresponds to variant rs119103226 [ dbSNP | Ensembl ].
VAR_067199
Natural varianti310 – 3101P → R in MCC2D; mild form. 1 Publication
VAR_012799
Natural varianti339 – 3391V → M in MCC2D; severe form. 1 Publication
VAR_012800
Natural varianti437 – 4371I → V in MCC2D; mild form.
VAR_012801
Natural varianti459 – 4591P → S in MCC2D. 1 Publication
VAR_067200
Natural varianti478 – 4781A → G.
Corresponds to variant rs35068278 [ dbSNP | Ensembl ].
VAR_038630

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei209 – 24638Missing in isoform 2. 1 PublicationVSP_000069Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050049 mRNA. Translation: BAB16880.1.
AB050050 Genomic DNA. Translation: BAB41121.1.
AF310971 mRNA. Translation: AAG53094.1.
AF301000 mRNA. Translation: AAK16404.1.
AF261884 mRNA. Translation: AAK49409.1.
AC138832 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95693.1.
BC014897 mRNA. Translation: AAH14897.1. Frameshift.
BC065027 mRNA. Translation: AAH65027.1.
AL079298 mRNA. Translation: CAB45194.1.
CCDSiCCDS34184.1. [Q9HCC0-1]
RefSeqiNP_071415.1. NM_022132.4. [Q9HCC0-1]
XP_005248624.1. XM_005248567.1. [Q9HCC0-2]
UniGeneiHs.604789.

Genome annotation databases

EnsembliENST00000340941; ENSP00000343657; ENSG00000131844. [Q9HCC0-1]
GeneIDi64087.
KEGGihsa:64087.
UCSCiuc003kbs.4. human. [Q9HCC0-1]

Polymorphism databases

DMDMi20138731.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050049 mRNA. Translation: BAB16880.1 .
AB050050 Genomic DNA. Translation: BAB41121.1 .
AF310971 mRNA. Translation: AAG53094.1 .
AF301000 mRNA. Translation: AAK16404.1 .
AF261884 mRNA. Translation: AAK49409.1 .
AC138832 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95693.1 .
BC014897 mRNA. Translation: AAH14897.1 . Frameshift.
BC065027 mRNA. Translation: AAH65027.1 .
AL079298 mRNA. Translation: CAB45194.1 .
CCDSi CCDS34184.1. [Q9HCC0-1 ]
RefSeqi NP_071415.1. NM_022132.4. [Q9HCC0-1 ]
XP_005248624.1. XM_005248567.1. [Q9HCC0-2 ]
UniGenei Hs.604789.

3D structure databases

ProteinModelPortali Q9HCC0.
SMRi Q9HCC0. Positions 28-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122050. 19 interactions.
IntActi Q9HCC0. 12 interactions.
MINTi MINT-8051924.
STRINGi 9606.ENSP00000343657.

Chemistry

DrugBanki DB00121. Biotin.

PTM databases

PhosphoSitei Q9HCC0.

Polymorphism databases

DMDMi 20138731.

2D gel databases

REPRODUCTION-2DPAGE IPI00784044.

Proteomic databases

MaxQBi Q9HCC0.
PaxDbi Q9HCC0.
PRIDEi Q9HCC0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340941 ; ENSP00000343657 ; ENSG00000131844 . [Q9HCC0-1 ]
GeneIDi 64087.
KEGGi hsa:64087.
UCSCi uc003kbs.4. human. [Q9HCC0-1 ]

Organism-specific databases

CTDi 64087.
GeneCardsi GC05P070883.
HGNCi HGNC:6937. MCCC2.
HPAi HPA038300.
HPA038301.
MIMi 210210. phenotype.
609014. gene.
neXtProti NX_Q9HCC0.
Orphaneti 6. Isolated 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKBi PA30681.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4799.
GeneTreei ENSGT00530000063337.
HOGENOMi HOG000218692.
HOVERGENi HBG052424.
InParanoidi Q9HCC0.
KOi K01969.
OMAi YSSARCW.
PhylomeDBi Q9HCC0.
TreeFami TF300446.

Enzyme and pathway databases

UniPathwayi UPA00363 ; UER00861 .
BioCyci MetaCyc:ENSG00000131844-MONOMER.
Reactomei REACT_11153. Biotin transport and metabolism.
REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
REACT_197. Branched-chain amino acid catabolism.

Miscellaneous databases

GenomeRNAii 64087.
NextBioi 65884.
PROi Q9HCC0.
SOURCEi Search...

Gene expression databases

Bgeei Q9HCC0.
CleanExi HS_MCCC2.
ExpressionAtlasi Q9HCC0. baseline and differential.
Genevestigatori Q9HCC0.

Family and domain databases

Gene3Di 3.90.226.10. 2 hits.
InterProi IPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view ]
Pfami PF01039. Carboxyl_trans. 1 hit.
[Graphical view ]
SUPFAMi SSF52096. SSF52096. 2 hits.
PROSITEi PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human non-biotin containing subunit gene of 3-methylcrotonyl-CoA carboxylase (MCCB)."
    Fukuda T., Otsuka H., Morishita R., Takemoto Y., Sone M., Nakao M., Abe S., Kondo I.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANTS MCC2D ARG-167 AND THR-218.
  3. "The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency."
    Baumgartner M.R., Almashanu S., Suormala T., Obie C., Cole R.N., Packman S., Baumgartner E.R., Valle D.
    J. Clin. Invest. 107:495-504(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MCC2D GLN-99; GLN-155; LEU-173; CYS-193; ARG-310 AND MET-339.
  4. "Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency."
    Holzinger A., Roeschinger W., Lagler F., Mayerhofer P.U., Lichtner P., Kattenfeld T., Thuy L.P., Nyhan W.L., Koch H.G., Muntau A.C., Roscher A.A.
    Hum. Mol. Genet. 10:1299-1306(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MCC2D THR-268.
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Testis and Uterus.
  8. Cited for: PROTEIN SEQUENCE OF 23-28, SUBCELLULAR LOCATION.
    Tissue: Kidney.
  9. "Expression, purification, characterization of human 3-methylcrotonyl-CoA carboxylase (MCCC)."
    Chu C.H., Cheng D.
    Protein Expr. Purif. 53:421-427(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  10. The European IMAGE consortium
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 469-563.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Mutational spectrum in eight Korean patients with 3-methylcrotonyl-CoA carboxylase deficiency."
    Cho S.Y., Park H.D., Lee Y.W., Ki C.S., Lee S.Y., Sohn Y.B., Park S.W., Kim S.H., Ji S., Kim S.J., Choi E.W., Kim C.H., Ko A.R., Paik K.H., Lee D.H., Jin D.K.
    Clin. Genet. 81:96-98(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MCC2D TYR-280 AND SER-459.

Entry informationi

Entry nameiMCCB_HUMAN
AccessioniPrimary (citable) accession number: Q9HCC0
Secondary accession number(s): A6NIY9, Q96C27, Q9Y4L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 137 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3