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Q14526 (HIC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hypermethylated in cancer 1 protein

Short name=Hic-1
Alternative name(s):
Zinc finger and BTB domain-containing protein 29
Gene names
Name:HIC1
Synonyms:ZBTB29
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length733 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor. Recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor suppressor. May be involved in development of head, face, limbs and ventral body wall. Involved in down-regulation of SIRT1 and thereby is involved in regulation of p53/TP53-dependent apoptotic DNA-damage responses. The specific target gene promoter association seems to be depend on corepressors, such as CTBP1 or CTBP2 and MTA1. The regulation of SIRT1 transcription in response to nutrient deprivation seems to involve CTBP1. In cooperation with MTA1 (indicative for an association with the NuRD complex) represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2 specifically in quiescent cells. Involved in regulation of the Wnt signaling pathway probably by association with TCF7L2 and preventing TCF7L2 and CTNNB1 association with promoters of TCF-responsive genes. Seems to repress transcription from E2F1 and ATOH1 which involves ARID1A, indicative for the participation of a distinct SWI/SNF-type chromatin-remodeling complex. Probably represses transcription from ACKR3, FGFBP1 and EFNA1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19

Subunit structure

Self-associates. Interacts with HIC2. Interacts with CTBP1 and CTBP2. Interacts with TCF7L2 and ARID1A. Interacts with MTA1 and MBD3; indicative for an association with the NuRD complex. Ref.5 Ref.6 Ref.10 Ref.11 Ref.13 Ref.16 Ref.18

Subcellular location

Nucleus Ref.5.

Tissue specificity

Ubiquitously expressed with highest levels found in lung, colon, prostate, thymus, testis and ovary. Expression is absent or decreased in many tumor cells.

Domain

The BTB domain inhibits the binding to a single consensus binding site, but mediates cooperative binding to multiple binding sites.

Post-translational modification

Acetylated on several residues, including Lys-333. Lys-333 is deacetylated by SIRT1. Ref.12

Sumoylated on Lys-333 by a PIAS family member, which enhances interaction with MTA1, positively regulates transcriptional repression activity and is enhanced by HDAC4. Ref.12

Miscellaneous

The HIC1 gene is frequently found epigenetically silenced or deleted in different types of solid tumors.

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family. Hic subfamily.

Contains 1 BTB (POZ) domain.

Contains 5 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
Repressor
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay Ref.8. Source: UniProtKB

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of Wnt signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6Ref.7. Source: UniProtKB

positive regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionhistone deacetylase binding

Inferred from direct assay Ref.6. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding

Inferred from direct assay Ref.7. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARID1AO144972EBI-2507362,EBI-637887
CTBP1Q133634EBI-2507362,EBI-908846
Ctbp1O8871210EBI-2507362,EBI-604547From a different organism.
CTBP2P565452EBI-2507362,EBI-741533
Ctbp2P565462EBI-2507362,EBI-1384883From a different organism.
TCF7L2Q9NQB06EBI-2507362,EBI-924724

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q14526-1)

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.
Isoform 2 (identifier: Q14526-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 733733Hypermethylated in cancer 1 protein
PRO_0000046942

Regions

Domain47 – 11064BTB
Zinc finger439 – 45921C2H2-type 1
Zinc finger509 – 52921C2H2-type 2
Zinc finger537 – 55721C2H2-type 3
Zinc finger565 – 58521C2H2-type 4
Zinc finger593 – 61321C2H2-type 5
Region154 – 315162Mediates HDAC-dependent transcriptional repression
Region241 – 2477Interaction with CTBP1
Compositional bias110 – 11910Poly-Ala
Compositional bias160 – 1678Poly-Gly
Compositional bias195 – 1995Poly-Pro

Amino acid modifications

Modified residue3331N6-acetyllysine; alternate Ref.12
Cross-link333Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.12

Natural variations

Alternative sequence1 – 1919Missing in isoform 2.
VSP_006826
Natural variant7251R → G. Ref.1
Corresponds to variant rs1063317 [ dbSNP | Ensembl ].
VAR_063109

Experimental info

Mutagenesis2441L → A: Abolishes interaction with CTBP1 and CTBP2. Impairs transcriptional repression. Ref.11
Mutagenesis3331K → Q: Mimicks acetylation. Impairs interaction with RBBP4 and MTA1 and no effect on interaction with CTBP2. Reduces transcriptional repression. Ref.12 Ref.18
Mutagenesis3331K → R: Abolishes sumoylation; impairs transcriptional repression activity. Ref.12 Ref.18
Mutagenesis3351E → A: Impairs transcriptional repression activity. Decreases interaction with MTA1. Ref.12 Ref.18
Mutagenesis3361P → A: Impairs K-333 acetylation; no effect on sumoylation. Decreases interaction with MTA1. Ref.12 Ref.18
Mutagenesis5401C → S: Abolishes repression activity. Ref.7
Sequence conflict1901P → R in AAD09201. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 5.
Checksum: 6DDD0F49C4E490D3

FASTA73376,508
        10         20         30         40         50         60 
MTFPEADILL KSGECAGQTM LDTMEAPGHS RQLLLQLNNQ RTKGFLCDVI IVVQNALFRA 

        70         80         90        100        110        120 
HKNVLAASSA YLKSLVVHDN LLNLDHDMVS PAVFRLVLDF IYTGRLADGA EAAAAAAVAP 

       130        140        150        160        170        180 
GAEPSLGAVL AAASYLQIPD LVALCKKRLK RHGKYCHLRG GGGGGGGYAP YGRPGRGLRA 

       190        200        210        220        230        240 
ATPVIQACYP SPVGPPPPPA AEPPSGPEAA VNTHCAELYA SGPGPAAALC ASERRCSPLC 

       250        260        270        280        290        300 
GLDLSKKSPP GSAAPERPLA ERELPPRPDS PPSAGPAAYK EPPLALPSLP PLPFQKLEEA 

       310        320        330        340        350        360 
APPSDPFRGG SGSPGPEPPG RPDGPSLLYR WMKHEPGLGS YGDELGRERG SPSERCEERG 

       370        380        390        400        410        420 
GDAAVSPGGP PLGLAPPPRY PGSLDGPGAG GDGDDYKSSS EETGSSEDPS PPGGHLEGYP 

       430        440        450        460        470        480 
CPHLAYGEPE SFGDNLYVCI PCGKGFPSSE QLNAHVEAHV EEEEALYGRA EAAEVAAGAA 

       490        500        510        520        530        540 
GLGPPFGGGG DKVAGAPGGL GELLRPYRCA SCDKSYKDPA TLRQHEKTHW LTRPYPCTIC 

       550        560        570        580        590        600 
GKKFTQRGTM TRHMRSHLGL KPFACDACGM RFTRQYRLTE HMRIHSGEKP YECQVCGGKF 

       610        620        630        640        650        660 
AQQRNLISHM KMHAVGGAAG AAGALAGLGG LPGVPGPDGK GKLDFPEGVF AVARLTAEQL 

       670        680        690        700        710        720 
SLKQQDKAAA AELLAQTTHF LHDPKVALES LYPLAKFTAE LGLSPDKAAE VLSQGAHLAA 

       730 
GPDGRTIDRF SPT 

« Hide

Isoform 2 [UniParc].

Checksum: 3AB8B6CB2C97218D
Show »

FASTA71474,514

References

« Hide 'large scale' references
[1]"p53 activates expression of HIC-1, a new candidate tumour suppressor gene on 17p13.3."
Wales M.M., Biel M.A., el Deiry W., Nelkin B.D., Issa J.-P., Cavenee W.K., Kuerbitz S.J., Baylin S.B.
Nat. Med. 1:570-577(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT GLY-725.
[2]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B."
Deltour S., Guerardel C., Leprince D.
Proc. Natl. Acad. Sci. U.S.A. 96:14831-14836(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-ASSOCIATION.
[5]"Characterization of HRG22, a human homologue of the putative tumor suppressor gene HIC1."
Deltour S., Pinte S., Guerardel C., Leprince D.
Biochem. Biophys. Res. Commun. 287:427-434(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, INTERACTION WITH HIC2, SUBCELLULAR LOCATION.
[6]"The human candidate tumor suppressor gene HIC1 recruits CtBP through a degenerate GLDLSKK motif."
Deltour S., Pinte S., Guerardel C., Wasylyk B., Leprince D.
Mol. Cell. Biol. 22:4890-4901(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH CTBP1.
[7]"The tumor suppressor gene HIC1 (hypermethylated in cancer 1) is a sequence-specific transcriptional repressor: definition of its consensus binding sequence and analysis of its DNA binding and repressive properties."
Pinte S., Stankovic-Valentin N., Deltour S., Rood B.R., Guerardel C., Leprince D.
J. Biol. Chem. 279:38313-38324(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF CYS-540.
[8]"Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses."
Chen W.Y., Wang D.H., Yen R.C., Luo J., Gu W., Baylin S.B.
Cell 123:437-448(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Mechanism of fibroblast growth factor-binding protein 1 repression by TGF-beta."
Briones V.R., Chen S., Riegel A.T., Lechleider R.J.
Biochem. Biophys. Res. Commun. 345:595-601(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"HIC1 attenuates Wnt signaling by recruitment of TCF-4 and beta-catenin to the nuclear bodies."
Valenta T., Lukas J., Doubravska L., Fafilek B., Korinek V.
EMBO J. 25:2326-2337(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN WNT SIGNALING, INTERACTION WITH TCF7L2.
[11]"A L225A substitution in the human tumour suppressor HIC1 abolishes its interaction with the corepressor CtBP."
Stankovic-Valentin N., Verger A., Deltour-Balerdi S., Quinlan K.G., Crossley M., Leprince D.
FEBS J. 273:2879-2890(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF LEU-244.
[12]"An acetylation/deacetylation-SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity."
Stankovic-Valentin N., Deltour S., Seeler J., Pinte S., Vergoten G., Guerardel C., Dejean A., Leprince D.
Mol. Cell. Biol. 27:2661-2675(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-333, ACETYLATION AT LYS-333, MUTAGENESIS OF LYS-333; GLU-335 AND PRO-336.
[13]"Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex."
Zhang Q., Wang S.Y., Fleuriel C., Leprince D., Rocheleau J.V., Piston D.W., Goodman R.H.
Proc. Natl. Acad. Sci. U.S.A. 104:829-833(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTBP1.
[14]"Cooperation between the Hic1 and Ptch1 tumor suppressors in medulloblastoma."
Briggs K.J., Corcoran-Schwartz I.M., Zhang W., Harcke T., Devereux W.L., Baylin S.B., Eberhart C.G., Watkins D.N.
Genes Dev. 22:770-785(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]Erratum
Briggs K.J., Corcoran-Schwartz I.M., Zhang W., Harcke T., Devereux W.L., Baylin S.B., Eberhart C.G., Watkins D.N.
Genes Dev. 22:1410-1410(2008)
[16]"HIC1 interacts with a specific subunit of SWI/SNF complexes, ARID1A/BAF250A."
Van Rechem C., Boulay G., Leprince D.
Biochem. Biophys. Res. Commun. 385:586-590(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARID1A.
[17]"Scavenger chemokine (CXC motif) receptor 7 (CXCR7) is a direct target gene of HIC1 (hypermethylated in cancer 1)."
Van Rechem C., Rood B.R., Touka M., Pinte S., Jenal M., Guerardel C., Ramsey K., Monte D., Begue A., Tschan M.P., Stephan D.A., Leprince D.
J. Biol. Chem. 284:20927-20935(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Differential regulation of HIC1 target genes by CtBP and NuRD, via an acetylation/SUMOylation switch, in quiescent versus proliferating cells."
Van Rechem C., Boulay G., Pinte S., Stankovic-Valentin N., Guerardel C., Leprince D.
Mol. Cell. Biol. 30:4045-4059(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MTA1 AND MBD3, MUTAGENESIS OF LYS-333; GLU-335 AND PRO-336.
[19]"A potential tumor suppressor role for Hic1 in breast cancer through transcriptional repression of ephrin-A1."
Zhang W., Zeng X., Briggs K.J., Beaty R., Simons B., Chiu Yen R.W., Tyler M.A., Tsai H.C., Ye Y., Gesell G.S., Herman J.G., Baylin S.B., Watkins D.N.
Oncogene 29:2467-2476(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41919 Genomic DNA. Translation: AAD09201.1.
AC090617 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90562.1.
CH471108 Genomic DNA. Translation: EAW90563.1.
RefSeqNP_001091672.1. NM_001098202.1.
NP_006488.2. NM_006497.3.
UniGeneHs.695682.
Hs.72956.

3D structure databases

ProteinModelPortalQ14526.
SMRQ14526. Positions 25-145, 437-659.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109337. 24 interactions.
IntActQ14526. 11 interactions.
MINTMINT-2730619.
STRING9606.ENSP00000314080.

PTM databases

PhosphoSiteQ14526.

Polymorphism databases

DMDM296439502.

Proteomic databases

PaxDbQ14526.
PRIDEQ14526.

Protocols and materials databases

DNASU3090.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322941; ENSP00000314080; ENSG00000177374. [Q14526-1]
ENST00000399849; ENSP00000382742; ENSG00000177374. [Q14526-2]
GeneID3090.
KEGGhsa:3090.
UCSCuc002fty.4. human. [Q14526-1]

Organism-specific databases

CTD3090.
GeneCardsGC17P001967.
H-InvDBHIX0039113.
HGNCHGNC:4909. HIC1.
HPAHPA043372.
MIM603825. gene.
neXtProtNX_Q14526.
Orphanet531. Miller-Dieker syndrome.
PharmGKBPA29282.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000026793.
HOVERGENHBG031606.
InParanoidQ14526.
OMAERCEERG.
OrthoDBEOG74J97F.
PhylomeDBQ14526.
TreeFamTF333488.

Enzyme and pathway databases

SignaLinkQ14526.

Gene expression databases

ArrayExpressQ14526.
BgeeQ14526.
CleanExHS_HIC1.
GenevestigatorQ14526.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
3.30.710.10. 1 hit.
InterProIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR028424. HIC1.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERPTHR11389:SF322. PTHR11389:SF322. 1 hit.
PfamPF00651. BTB. 1 hit.
PF00096. zf-C2H2. 2 hits.
[Graphical view]
SMARTSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 5 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHIC1.
GenomeRNAi3090.
NextBio12259.
PROQ14526.
SOURCESearch...

Entry information

Entry nameHIC1_HUMAN
AccessionPrimary (citable) accession number: Q14526
Secondary accession number(s): D3DTI4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 132 of the entry and version 5 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM