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Q9UHD9 (UBQL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquilin-2
Alternative name(s):
Chap1
DSK2 homolog
Protein linking IAP with cytoskeleton 2
Short name=PLIC-2
Short name=hPLIC-2
Ubiquitin-like product Chap1/Dsk2
Gene names
Name:UBQLN2
Synonyms:N4BP4, PLIC2
ORF Names:HRIHFB2157
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length624 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Increases the half-life of proteins destined to be degraded by the proteasome; may modulate proteasome-mediated protein degradation. Ref.2

Subunit structure

Binds UBE3A and BTRC. Interacts with the 19S proteasome subunit. Ref.1 Ref.2

Subcellular location

Cytoplasm. Nucleus. Note: Where it colocalizes with the proteasome. Associated with fibers in mitotic cells. Ref.2 Ref.7

Induction

Highly expressed in mitotic cells from metaphase to telophase. Expression in non-mitotic cells is very low.

Involvement in disease

Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia (ALS15) [MIM:300857]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS15 may develop frontotemporal dementia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Contains 1 UBA domain.

Contains 1 ubiquitin-like domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   DomainRepeat
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADRM1Q161863EBI-947187,EBI-954387
PSMD4P550363EBI-947187,EBI-359318
RAD23AP547253EBI-947187,EBI-746453
RPN13O487264EBI-947187,EBI-7710745From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 624623Ubiquilin-2
PRO_0000211011

Regions

Domain33 – 10775Ubiquitin-like
Repeat491 – 49331
Repeat494 – 49632
Repeat497 – 49933
Repeat500 – 50234
Repeat503 – 50535
Repeat506 – 50836
Repeat509 – 51137
Repeat512 – 51438
Repeat515 – 51739
Repeat518 – 520310
Repeat521 – 523311
Repeat524 – 526312
Domain581 – 62141UBA
Region491 – 5263612 X 3 AA tandem repeats of P-X-X

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.10

Natural variations

Natural variant1551S → N in ALS15; uncertain pathological significance. Ref.15
VAR_068892
Natural variant1891P → T in ALS15; uncertain pathological significance. Ref.15
VAR_068893
Natural variant2351L → H.
Corresponds to variant rs17002693 [ dbSNP | Ensembl ].
VAR_052680
Natural variant2821A → V Probable disease-associated mutation found in a patient with frontotemporal dementia. Ref.13
VAR_068894
Natural variant2831A → T in ALS15. Ref.13
VAR_068895
Natural variant4251Q → R in ALS15. Ref.13
VAR_068896
Natural variant4871T → I in ALS15. Ref.14
VAR_068897
Natural variant4971P → H in ALS15; leads to defective ubiquitin-mediated proteasomal degradation. Ref.12
VAR_066562
Natural variant4971P → S in ALS15. Ref.12
VAR_066563
Natural variant5061P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation. Ref.12
VAR_066564
Natural variant5091P → S in ALS15. Ref.12
VAR_066565
Natural variant5251P → S in ALS15. Ref.12
VAR_066566

Experimental info

Sequence conflict5441S → R Ref.1
Sequence conflict5441S → R Ref.5

Secondary structure

................. 624
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UHD9 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DF7DF8C4D7B71AC3

FASTA62465,696
        10         20         30         40         50         60 
MAENGESSGP PRPSRGPAAA QGSAAAPAEP KIIKVTVKTP KEKEEFAVPE NSSVQQFKEA 

        70         80         90        100        110        120 
ISKRFKSQTD QLVLIFAGKI LKDQDTLIQH GIHDGLTVHL VIKSQNRPQG QSTQPSNAAG 

       130        140        150        160        170        180 
TNTTSASTPR SNSTPISTNS NPFGLGSLGG LAGLSSLGLS STNFSELQSQ MQQQLMASPE 

       190        200        210        220        230        240 
MMIQIMENPF VQSMLSNPDL MRQLIMANPQ MQQLIQRNPE ISHLLNNPDI MRQTLEIARN 

       250        260        270        280        290        300 
PAMMQEMMRN QDLALSNLES IPGGYNALRR MYTDIQEPML NAAQEQFGGN PFASVGSSSS 

       310        320        330        340        350        360 
SGEGTQPSRT ENRDPLPNPW APPPATQSSA TTSTTTSTGS GSGNSSSNAT GNTVAAANYV 

       370        380        390        400        410        420 
ASIFSTPGMQ SLLQQITENP QLIQNMLSAP YMRSMMQSLS QNPDLAAQMM LNSPLFTANP 

       430        440        450        460        470        480 
QLQEQMRPQL PAFLQQMQNP DTLSAMSNPR AMQALMQIQQ GLQTLATEAP GLIPSFTPGV 

       490        500        510        520        530        540 
GVGVLGTAIG PVGPVTPIGP IGPIVPFTPI GPIGPIGPTG PAAPPGSTGS GGPTGPTVSS 

       550        560        570        580        590        600 
AAPSETTSPT SESGPNQQFI QQMVQALAGA NAPQLPNPEV RFQQQLEQLN AMGFLNREAN 

       610        620 
LQALIATGGD INAAIERLLG SQPS 

« Hide

References

« Hide 'large scale' references
[1]"A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch."
Kaye F.J., Modi S., Ivanovska I., Koonin E.V., Thress K., Kubo A., Kornbluth S., Rose M.D.
FEBS Lett. 467:348-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STCH.
Tissue: Lung.
[2]"The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome."
Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L., Gill G., Howley P.M.
Mol. Cell 6:409-419(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE PROTEASOME AND UBE3A.
Tissue: B-cell.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Placenta.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-624.
Tissue: Amygdala.
[7]"Selection system for genes encoding nuclear-targeted proteins."
Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-624, SUBCELLULAR LOCATION.
Tissue: Fetal brain.
[8]"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].
[9]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a."
Walters K.J., Kleijnen M.F., Goh A.M., Wagner G., Howley P.M.
Biochemistry 41:1767-1777(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-103.
[12]"Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia."
Deng H.X., Chen W., Hong S.T., Boycott K.M., Gorrie G.H., Siddique N., Yang Y., Fecto F., Shi Y., Zhai H., Jiang H., Hirano M., Rampersaud E., Jansen G.H., Donkervoort S., Bigio E.H., Brooks B.R., Ajroud K. expand/collapse author list , Sufit R.L., Haines J.L., Mugnaini E., Pericak-Vance M.A., Siddique T.
Nature 477:211-215(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS15 HIS-497; SER-497; THR-506; SER-509 AND SER-525, CHARACTERIZATION OF VARIANTS ALS15 HIS-497 AND THR-506.
[13]"Screening in ALS and FTD patients reveals 3 novel UBQLN2 mutations outside the PXX domain and a pure FTD phenotype."
Synofzik M., Maetzler W., Grehl T., Prudlo J., Vom Hagen J.M., Haack T., Rebassoo P., Munz M., Schols L., Biskup S.
Neurobiol. Aging 33:E13-E17(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS15 THR-283 AND ARG-425, VARIANT VAL-282.
[14]"UBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis."
Williams K.L., Warraich S.T., Yang S., Solski J.A., Fernando R., Rouleau G.A., Nicholson G.A., Blair I.P.
Neurobiol. Aging 33:E3-E10(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS15 ILE-487.
[15]"UBQLN2 mutations are rare in French and French-Canadian amyotrophic lateral sclerosis."
Daoud H., Suhail H., Szuto A., Camu W., Salachas F., Meininger V., Bouchard J.P., Dupre N., Dion P.A., Rouleau G.A.
Neurobiol. Aging 33:E1-E5(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS15 ASN-155 AND THR-189.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF189009 mRNA. Translation: AAF17237.1.
AF293385 mRNA. Translation: AAG02474.1.
AL354793 Genomic DNA. Translation: CAD13519.1.
CH471154 Genomic DNA. Translation: EAW93233.1.
BC069237 mRNA. Translation: AAH69237.1.
AL442081 mRNA. Translation: CAC09446.1.
AB015344 mRNA. Translation: BAA34801.1.
RefSeqNP_038472.2. NM_013444.3.
UniGeneHs.179309.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J8CNMR-A1-103[»]
ProteinModelPortalQ9UHD9.
SMRQ9UHD9. Positions 1-103, 578-624.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119006. 60 interactions.
DIPDIP-42116N.
IntActQ9UHD9. 12 interactions.
MINTMINT-1192483.
STRING9606.ENSP00000345195.

PTM databases

PhosphoSiteQ9UHD9.

Polymorphism databases

DMDM124056593.

Proteomic databases

PaxDbQ9UHD9.
PeptideAtlasQ9UHD9.
PRIDEQ9UHD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338222; ENSP00000345195; ENSG00000188021.
GeneID29978.
KEGGhsa:29978.
UCSCuc004dus.3. human.

Organism-specific databases

CTD29978.
GeneCardsGC0XP056606.
HGNCHGNC:12509. UBQLN2.
HPACAB013481.
HPA006431.
MIM300264. gene.
300857. phenotype.
neXtProtNX_Q9UHD9.
Orphanet803. Amyotrophic lateral sclerosis.
PharmGKBPA37156.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5272.
HOGENOMHOG000234878.
HOVERGENHBG064537.
InParanoidQ9UHD9.
KOK04523.
OMALMASPEM.
OrthoDBEOG7HF1J8.
PhylomeDBQ9UHD9.
TreeFamTF314412.

Gene expression databases

BgeeQ9UHD9.
CleanExHS_UBQLN2.
GenevestigatorQ9UHD9.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR015496. Ubiquilin.
IPR028430. Ubiquilin-2.
IPR000626. Ubiquitin-like.
[Graphical view]
PANTHERPTHR10677. PTHR10677. 1 hit.
PTHR10677:SF5. PTHR10677:SF5. 1 hit.
PfamPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UHD9.
GeneWikiUBQLN2.
GenomeRNAi29978.
NextBio52728.
PROQ9UHD9.
SOURCESearch...

Entry information

Entry nameUBQL2_HUMAN
AccessionPrimary (citable) accession number: Q9UHD9
Secondary accession number(s): O94798 expand/collapse secondary AC list , Q5D027, Q9H3W6, Q9HAZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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