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O43189 (PHF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 134. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PHD finger protein 1

Short name=Protein PHF1
Short name=hPHF1
Alternative name(s):
Polycomb-like protein 1
Short name=hPCl1
Gene names
Name:PHF1
Synonyms:PCL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci (Ref.8 and Ref.16). According to another report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2 (Ref.17). Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53. Ref.7 Ref.8 Ref.9 Ref.14 Ref.16 Ref.17

Subunit structure

Interacts with CHMP1 By similarity. Associated component of the PRC2 complex. Interacts with p53/TP53. Ref.7 Ref.8 Ref.14

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Co-localizes with NEK6 in the centrosome. Ref.8 Ref.9 Ref.11 Ref.14 Ref.16 Ref.17

Tissue specificity

Highest levels in heart, skeletal muscle, and pancreas, lower levels in brain, placenta, lung, liver and kidney.

Domain

The Tudor domain recognizes and binds H3K36me3 (Ref.13, Ref.16 and Ref.17).

Involvement in disease

A chromosomal aberration involving PHF1 may be a cause of endometrial stromal tumors. Translocation t(6;7)(p21;p22) with JAZF1. Translocation t(1;6)(p34;p21) with MEAF6. Ref.6 Ref.12

Sequence similarities

Belongs to the Polycomblike family.

Contains 2 PHD-type zinc fingers.

Contains 1 Tudor domain.

Ontologies

Keywords
   Biological processDNA damage
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from direct assay Ref.17. Source: UniProtKB

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of histone H3-K27 methylation

Inferred from mutant phenotype Ref.17. Source: UniProtKB

positive regulation of histone H3-K27 methylation

Inferred from mutant phenotype Ref.16. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

site of double-strand break

Inferred from direct assay Ref.17. Source: UniProtKB

   Molecular_functionmethylated histone residue binding

Inferred from direct assay Ref.17Ref.16. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: O43189-1)

Also known as: PHF2;

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 1 (identifier: O43189-2)

Also known as: PHF1;

The sequence of this isoform differs from the canonical sequence as follows:
     350-457: SFPSGQGPGG...IRMFASFHPS → RAGPWGRGLT...QTSLKVPPTR
     458-567: Missing.
Note: Contains a phosphoserine at position 360.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567PHD finger protein 1
PRO_0000059288

Regions

Domain29 – 8658Tudor
Zinc finger87 – 14256PHD-type 1
Zinc finger186 – 24055PHD-type 2

Natural variations

Alternative sequence350 – 457108SFPSG…SFHPS → RAGPWGRGLTSPGEAPEAGA RAPEEEAEGESGGAGATLSS AQSARAPGAEGAGSSAEGTA AAPSGCLLPSTLLPAPQGPL GTVDPQTGHPWNFTLVSPQT SLKVPPTR in isoform 1.
VSP_004694
Alternative sequence458 – 567110Missing in isoform 1.
VSP_004695
Natural variant421T → S.
Corresponds to variant rs6934613 [ dbSNP | Ensembl ].
VAR_044500
Natural variant3041R → K. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5
Corresponds to variant rs3116713 [ dbSNP | Ensembl ].
VAR_034382

Experimental info

Mutagenesis411W → A: Abolishes histone H3K36me3-binding and localization at double-strand breaks (DSBs). Ref.16 Ref.17
Mutagenesis471Y → A: Abolishes histone H3K36me3-binding. Ref.16 Ref.17
Mutagenesis651F → A: Abolishes histone H3K36me3-binding. Ref.16
Mutagenesis661E → K: Impairs histone H3K36me3-binding. Ref.16
Mutagenesis711F → A: Abolishes histone H3K36me3-binding. Ref.16

Secondary structure

............ 567
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (PHF2) [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: E81BA9475565957C

FASTA56762,106
        10         20         30         40         50         60 
MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV 

        70         80         90        100        110        120 
CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV 

       130        140        150        160        170        180 
PRAPAPGEGE GTSWVCRQCV FAIATKRGGA LKKGPYARAM LGMKLSLPYG LKGLDWDAGH 

       190        200        210        220        230        240 
LSNRQQSYCY CGGPGEWNLK MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG 

       250        260        270        280        290        300 
PEKVRRLQLR WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE 

       310        320        330        340        350        360 
RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTS FPSGQGPGGG 

       370        380        390        400        410        420 
VSRPLGKRRR PEPEPLRRRQ KGKVEELGPP SAVRNQPEPQ EQRERAHLQR ALQASVSPPS 

       430        440        450        460        470        480 
PSPNQSYQGS SGYNFRPTDA RCLPSSPIRM FASFHPSAST AGTSGDSGPP DRSPLELHIG 

       490        500        510        520        530        540 
FPTDIPKSAP HSMTASSSSV SSPSPGLPRR SAPPSPLCRS LSPGTGGGVR GGVGYLSRGD 

       550        560 
PVRVLARRVR PDGSVQYLVE WGGGGIF 

« Hide

Isoform 1 (PHF1) [UniParc].

Checksum: 611EF2B5A416841C
Show »

FASTA45749,643

References

« Hide 'large scale' references
[1]"The identification and localization of a human gene with sequence similarity to Polycomblike of Drosophila melanogaster."
Coulson M., Robert S., Eyre H.J., Saint R.
Genomics 48:381-383(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-304.
Tissue: Placenta.
[2]Wang J.H., Du G.W., Zhou Y., Yuan J.G., Qiang B.Q.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LYS-304.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LYS-304.
[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], VARIANT LYS-304.
[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] (ISOFORM 2), VARIANT LYS-304.
Tissue: Uterus.
[6]"Consistent rearrangement of chromosomal band 6p21 with generation of fusion genes JAZF1/PHF1 and EPC1/PHF1 in endometrial stromal sarcoma."
Micci F., Panagopoulos I., Bjerkehagen B., Heim S.
Cancer Res. 66:107-112(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH JAZF1.
[7]"Role of hPHF1 in H3K27 methylation and Hox gene silencing."
Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.
Mol. Cell. Biol. 28:1862-1872(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE PRC2 COMPLEX.
[8]"Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo."
Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.
Mol. Cell. Biol. 28:2718-2731(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THE PRC2 COMPLEX, SUBCELLULAR LOCATION.
[9]"A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell."
Hong Z., Jiang J., Lan L., Nakajima S., Kanno S., Koseki H., Yasui A.
Nucleic Acids Res. 36:2939-2947(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial stromal sarcoma."
Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M., Bjerkehagen B., Davidson B., Heim S.
PLoS ONE 7:E39354-E39354(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH MEAF6.
[13]"Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3."
Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J.
Biochem. Biophys. Res. Commun. 430:547-553(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: H3K36ME3-BINDING.
[14]"Polycomb group protein PHF1 regulates p53-dependent cell growth arrest and apoptosis."
Yang Y., Wang C., Zhang P., Gao K., Wang D., Yu H., Zhang T., Jiang S., Hexige S., Hong Z., Yasui A., Liu J.O., Huang H., Yu L.
J. Biol. Chem. 288:529-539(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
[15]"Solution structure of the Tudor domain of PHD finger protein 1 (PHF1 protein)."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 29-85.
[16]"An H3K36 methylation-engaging Tudor motif of Polycomb-like proteins mediates PRC2 complex targeting."
Cai L., Rothbart S.B., Lu R., Xu B., Chen W.Y., Tripathy A., Rockowitz S., Zheng D., Patel D.J., Allis C.D., Strahl B.D., Song J., Wang G.G.
Mol. Cell 49:571-582(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 6-83, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-41; TYR-47; PHE-65; GLU-66 AND PHE-71.
[17]"Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1."
Musselman C.A., Avvakumov N., Watanabe R., Abraham C.G., Lalonde M.E., Hong Z., Allen C., Roy S., Nunez J.K., Nickoloff J., Kulesza C.A., Yasui A., Cote J., Kutateladze T.G.
Nat. Struct. Mol. Biol. 19:1266-1272(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-85, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-41 AND TYR-47.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029678 mRNA. Translation: AAC52062.1.
AF052205 mRNA. Translation: AAC13273.1.
AL662799 Genomic DNA. Translation: CAI18271.1.
AL662799 Genomic DNA. Translation: CAI18272.1.
AL021366 Genomic DNA. Translation: CAA16158.1.
AL021366 Genomic DNA. Translation: CAA16159.1.
AL050332 Genomic DNA. Translation: CAC38366.1.
AL050332 Genomic DNA. Translation: CAC38367.1.
BX088650 Genomic DNA. Translation: CAM26298.1.
BX088650 Genomic DNA. Translation: CAM26299.1.
CH471081 Genomic DNA. Translation: EAX03729.1.
CH471081 Genomic DNA. Translation: EAX03730.1.
BC008834 mRNA. Translation: AAH08834.1.
RefSeqNP_002627.1. NM_002636.4.
NP_077084.1. NM_024165.2.
UniGeneHs.166204.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5PNMR-A29-83[»]
2M0ONMR-A6-83[»]
4HCZX-ray1.85A/B28-85[»]
ProteinModelPortalO43189.
SMRO43189. Positions 6-82, 85-147, 185-265.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111271. 27 interactions.
DIPDIP-34001N.
IntActO43189. 10 interactions.
MINTMINT-1437706.

PTM databases

PhosphoSiteO43189.

Proteomic databases

PaxDbO43189.
PRIDEO43189.

Protocols and materials databases

DNASU5252.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374512; ENSP00000363636; ENSG00000112511. [O43189-2]
ENST00000374516; ENSP00000363640; ENSG00000112511. [O43189-1]
ENST00000427869; ENSP00000391901; ENSG00000225553.
ENST00000454914; ENSP00000407295; ENSG00000225553.
GeneID5252.
KEGGhsa:5252.
UCSCuc003oeh.3. human. [O43189-1]
uc003oei.3. human. [O43189-2]

Organism-specific databases

CTD5252.
GeneCardsGC06P033379.
GC06Po33517.
HGNCHGNC:8919. PHF1.
HPAHPA031038.
MIM602881. gene.
neXtProtNX_O43189.
PharmGKBPA33259.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG244542.
HOVERGENHBG004755.
InParanoidO43189.
KOK11467.
OMAFINGMSS.
PhylomeDBO43189.
TreeFamTF106420.

Gene expression databases

ArrayExpressO43189.
BgeeO43189.
CleanExHS_PHF1.
GenevestigatorO43189.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
InterProIPR025894. Mtf2_C_dom.
IPR002999. Tudor.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF14061. Mtf2_C. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 2 hits.
SM00333. TUDOR. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 2 hits.
PROSITEPS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO43189.
GeneWikiPHF1.
GenomeRNAi5252.
NextBio20290.
PROO43189.
SOURCESearch...

Entry information

Entry namePHF1_HUMAN
AccessionPrimary (citable) accession number: O43189
Secondary accession number(s): B1AZX2 expand/collapse secondary AC list , B1AZX3, O60929, Q5SU07, Q5SU08, Q96KM7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: March 19, 2014
This is version 134 of the entry and version 3 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 6

Human chromosome 6: entries, gene names and cross-references to MIM