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Q9UKF6 (CPSF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cleavage and polyadenylation specificity factor subunit 3

EC=3.1.27.-
Alternative name(s):
Cleavage and polyadenylation specificity factor 73 kDa subunit
Short name=CPSF 73 kDa subunit
mRNA 3'-end-processing endonuclease CPSF-73
Gene names
Name:CPSF3
Synonyms:CPSF73
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. Ref.6 Ref.7 Ref.9 Ref.16

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF2, CSTF2 and SYMPK. Interacts with TUT1; the interaction is direct and mediates the recruitment of the CPSF complex on the 3'UTR of pre-mRNAs. Interacts with WDR33. Ref.6 Ref.9 Ref.11 Ref.12

Subcellular location

Nucleus Ref.7.

Post-translational modification

Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3. Ref.8

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. CPSF3 subfamily.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionEndonuclease
Hydrolase
Nuclease
Ribonucleoprotein
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from sequence or structural similarity. Source: GOC

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

histone mRNA 3'-end processing

Inferred from direct assay Ref.9. Source: UniProtKB

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA cleavage

Traceable author statement PubMed 8929409. Source: ProtInc

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA polyadenylation

Traceable author statement PubMed 8929409. Source: ProtInc

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentmRNA cleavage and polyadenylation specificity factor complex

Inferred from direct assay PubMed 18305108Ref.12. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function5'-3' exonuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

RNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

endoribonuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 18288197Ref.9Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 684683Cleavage and polyadenylation specificity factor subunit 3
PRO_0000074400

Sites

Active site3961Proton donor Potential
Metal binding711Zinc 1
Metal binding731Zinc 1
Metal binding751Zinc 2
Metal binding761Zinc 2
Metal binding1581Zinc 1
Metal binding1791Zinc 1
Metal binding1791Zinc 2
Metal binding4181Zinc 2

Amino acid modifications

Modified residue21N-acetylserine Ref.10 Ref.15
Modified residue6811Phosphothreonine Ref.13
Cross-link462Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8
Cross-link465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8
Cross-link545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8

Natural variations

Natural variant1421E → G. Ref.4
Corresponds to variant rs17850770 [ dbSNP | Ensembl ].
VAR_037646
Natural variant5781D → N in a breast cancer sample; somatic mutation. Ref.17
VAR_035873

Experimental info

Mutagenesis731H → A: Inhibits histone 3'-end processing. Ref.9 Ref.16
Mutagenesis75 – 762DH → KA: Loss of histone 3'-end processing. Ref.9 Ref.16
Mutagenesis751D → A: Inhibits histone 3'-end processing. Ref.9 Ref.16
Mutagenesis761H → A: Inhibits histone 3'-end processing. Ref.9 Ref.16
Mutagenesis3341S → A: Does not inhibit histone 3'-end processing. Ref.9 Ref.16
Mutagenesis3961H → A: Inhibits histone 3'-end processing. Ref.9 Ref.16
Mutagenesis4621K → R: Reduced sumoylation; when associated with R-465 and R-545. Ref.8 Ref.16
Mutagenesis4651K → R: Reduced sumoylation; when associated with R-462 and R-545. Ref.8 Ref.16
Mutagenesis5451K → R: Reduced sumoylation; when associated with R-462 and R-465. Ref.8 Ref.16

Secondary structure

.................................................................................. 684
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UKF6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F8AA24EA6FB78377

FASTA68477,486
        10         20         30         40         50         60 
MSAIPAEESD QLLIRPLGAG QEVGRSCIIL EFKGRKIMLD CGIHPGLEGM DALPYIDLID 

        70         80         90        100        110        120 
PAEIDLLLIS HFHLDHCGAL PWFLQKTSFK GRTFMTHATK AIYRWLLSDY VKVSNISADD 

       130        140        150        160        170        180 
MLYTETDLEE SMDKIETINF HEVKEVAGIK FWCYHAGHVL GAAMFMIEIA GVKLLYTGDF 

       190        200        210        220        230        240 
SRQEDRHLMA AEIPNIKPDI LIIESTYGTH IHEKREEREA RFCNTVHDIV NRGGRGLIPV 

       250        260        270        280        290        300 
FALGRAQELL LILDEYWQNH PELHDIPIYY ASSLAKKCMA VYQTYVNAMN DKIRKQININ 

       310        320        330        340        350        360 
NPFVFKHISN LKSMDHFDDI GPSVVMASPG MMQSGLSREL FESWCTDKRN GVIIAGYCVE 

       370        380        390        400        410        420 
GTLAKHIMSE PEEITTMSGQ KLPLKMSVDY ISFSAHTDYQ QTSEFIRALK PPHVILVHGE 

       430        440        450        460        470        480 
QNEMARLKAA LIREYEDNDE VHIEVHNPRN TEAVTLNFRG EKLAKVMGFL ADKKPEQGQR 

       490        500        510        520        530        540 
VSGILVKRNF NYHILSPCDL SNYTDLAMST VKQTQAIPYT GPFNLLCYQL QKLTGDVEEL 

       550        560        570        580        590        600 
EIQEKPALKV FKNITVIQEP GMVVLEWLAN PSNDMYADTV TTVILEVQSN PKIRKGAVQK 

       610        620        630        640        650        660 
VSKKLEMHVY SKRLEIMLQD IFGEDCVSVK DDSILSVTVD GKTANLNLET RTVECEEGSE 

       670        680 
DDESLREMVE LAAQRLYEAL TPVH 

« Hide

References

« Hide 'large scale' references
[1]"Homo sapiens mRNA for CPSF (cleavage and polyadenylation specificity factor) 73 kDa subunit."
Yu S., Chen W., Pang X., Dong X., Wang H.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatoma.
[2]"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. expand/collapse author list , 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].
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 GLY-142.
Tissue: Brain and Uterus.
[5]"H. sapiens mRNA for the 73 kDa subunit of CPSF (cleavage and polyadenylation specificity factor, partial cds)."
Pusch W.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 120-498.
[6]"Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase."
Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.
EMBO J. 23:616-626(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PRE-MRNA 3'-END PROCESSING, IDENTIFICATION IN THE CPSF COMPLEX.
[7]"Evidence that polyadenylation factor CPSF-73 is the mRNA 3' processing endonuclease."
Ryan K., Calvo O., Manley J.L.
RNA 10:565-573(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex."
Vethantham V., Rao N., Manley J.L.
Mol. Cell. Biol. 27:8848-8858(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-462; LYS-465 AND LYS-545, MUTAGENESIS OF LYS-462; LYS-465 AND LYS-545.
[9]"Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation."
Kolev N.G., Yario T.A., Benson E., Steitz J.A.
EMBO Rep. 9:1013-1018(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CPSF2; CSTF2 AND SYMPK, MUTAGENESIS OF HIS-73; ASP-75; HIS-76; SER-334 AND HIS-396.
[10]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Molecular architecture of the human pre-mRNA 3' processing complex."
Shi Y., Di Giammartino D.C., Taylor D., Sarkeshik A., Rice W.J., Yates J.R. III, Frank J., Manley J.L.
Mol. Cell 33:365-376(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WDR33.
[12]"The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
Laishram R.S., Anderson R.A.
EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CPSF COMPLEX, INTERACTION WITH TUT1.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease."
Mandel C.R., Kaneko S., Zhang H., Gebauer D., Vethantham V., Manley J.L., Tong L.
Nature 444:953-956(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-459 IN COMPLEX WITH ZINC IONS, FUNCTION, MUTAGENESIS OF 75-ASP-HIS-76.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-578.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF171877 mRNA. Translation: AAF00224.1.
AC080162 Genomic DNA. Translation: AAY14858.1.
CH471053 Genomic DNA. Translation: EAX00989.1.
BC011654 mRNA. Translation: AAH11654.1.
BC020211 mRNA. Translation: AAH20211.1.
AF017269 mRNA. Translation: AAB70268.1.
CCDSCCDS1664.1.
RefSeqNP_057291.1. NM_016207.3.
UniGeneHs.515972.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I7TX-ray2.10A1-459[»]
2I7VX-ray2.10A1-459[»]
ProteinModelPortalQ9UKF6.
SMRQ9UKF6. Positions 7-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119680. 22 interactions.
DIPDIP-42501N.
IntActQ9UKF6. 8 interactions.
MINTMINT-1742891.
STRING9606.ENSP00000238112.

PTM databases

PhosphoSiteQ9UKF6.

Polymorphism databases

DMDM18203503.

Proteomic databases

MaxQBQ9UKF6.
PaxDbQ9UKF6.
PeptideAtlasQ9UKF6.
PRIDEQ9UKF6.

Protocols and materials databases

DNASU51692.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238112; ENSP00000238112; ENSG00000119203.
GeneID51692.
KEGGhsa:51692.
UCSCuc002qzo.2. human.

Organism-specific databases

CTD51692.
GeneCardsGC02P009514.
HGNCHGNC:2326. CPSF3.
HPAHPA034657.
MIM606029. gene.
neXtProtNX_Q9UKF6.
PharmGKBPA26843.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1236.
HOGENOMHOG000203394.
HOVERGENHBG051107.
InParanoidQ9UKF6.
KOK14403.
OMAEISFSAH.
OrthoDBEOG7BW0HT.
PhylomeDBQ9UKF6.
TreeFamTF105643.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ9UKF6.
BgeeQ9UKF6.
CleanExHS_CPSF3.
GenevestigatorQ9UKF6.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR022712. Beta_Casp.
IPR021718. CPSF73-100_C.
IPR011108. RMMBL.
[Graphical view]
PfamPF10996. Beta-Casp. 1 hit.
PF11718. CPSF73-100_C. 1 hit.
PF00753. Lactamase_B. 1 hit.
PF07521. RMMBL. 1 hit.
[Graphical view]
SMARTSM01027. Beta-Casp. 1 hit.
SM01098. CPSF73-100_C. 1 hit.
SM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCPSF3. human.
EvolutionaryTraceQ9UKF6.
GeneWikiCPSF3.
GenomeRNAi51692.
NextBio55702.
PROQ9UKF6.
SOURCESearch...

Entry information

Entry nameCPSF3_HUMAN
AccessionPrimary (citable) accession number: Q9UKF6
Secondary accession number(s): O14769, Q53RS2, Q96F36
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 116 of the entry and version 1 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 2

Human chromosome 2: entries, gene names and cross-references to MIM