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P49916 (DNLI3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA ligase 3

EC=6.5.1.1
Alternative name(s):
DNA ligase III
Polydeoxyribonucleotide synthase [ATP] 3
Gene names
Name:LIG3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1009 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with DNA-repair protein XRCC1 and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.

Catalytic activity

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).

Cofactor

Magnesium By similarity.

Subcellular location

Nucleus.

Tissue specificity

Testis, thymus, prostate and heart.

Sequence similarities

Belongs to the ATP-dependent DNA ligase family.

Contains 1 BRCT domain.

Contains 1 PARP-type zinc finger.

Sequence caution

The sequence AAA85022.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAL91592.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA59230.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA recombination
DNA repair
DNA replication
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

base-excision repair

Traceable author statement. Source: Reactome

base-excision repair, DNA ligation

Inferred from electronic annotation. Source: Ensembl

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

double-strand break repair via nonhomologous end joining

Inferred from electronic annotation. Source: Ensembl

lagging strand elongation

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrial DNA repair

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA recombination

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Inferred from Biological aspect of Ancestor. Source: RefGenome

reciprocal meiotic recombination

Traceable author statement Ref.2. Source: ProtInc

spermatogenesis

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentchromosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

synaptonemal complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement Ref.2. Source: ProtInc

DNA ligase (ATP) activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA ligase activity

Inferred from direct assay PubMed 9809069. Source: UniProtKB

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 Alpha (identifier: P49916-1)

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 Beta (identifier: P49916-2)

The sequence of this isoform differs from the canonical sequence as follows:
     933-1009: VLLDIFTGVR...IRKRRLVAPC → RRPASEQRGRTVPAGRR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10091009DNA ligase 3
PRO_0000059574

Regions

Domain933 – 100977BRCT
Zinc finger93 – 18593PARP-type

Sites

Active site5081N6-AMP-lysine intermediate By similarity
Metal binding5601Magnesium 1 By similarity
Metal binding6551Magnesium 2 By similarity
Binding site5061ATP By similarity
Binding site5131ATP By similarity
Binding site5281ATP By similarity
Binding site6601ATP By similarity
Binding site6711ATP By similarity
Binding site6751ATP By similarity

Amino acid modifications

Modified residue2101Phosphoserine Ref.8 Ref.12 Ref.14
Modified residue2271Phosphoserine Ref.9

Natural variations

Alternative sequence933 – 100977VLLDI…LVAPC → RRPASEQRGRTVPAGRR in isoform Beta.
VSP_001302
Natural variant2241R → W.
Corresponds to variant rs3744356 [ dbSNP | Ensembl ].
VAR_020196
Natural variant7171D → N in a colorectal cancer sample; somatic mutation. Ref.17
VAR_036513
Natural variant8671R → H. Ref.3
Corresponds to variant rs3136025 [ dbSNP | Ensembl ].
VAR_018807
Natural variant8981K → T.
Corresponds to variant rs4986974 [ dbSNP | Ensembl ].
VAR_021938
Natural variant9861P → S.
Corresponds to variant rs4986973 [ dbSNP | Ensembl ].
VAR_020197

Secondary structure

.................................................................................................................................... 1009
Helix Strand Turn

Details...

Sequences

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

Last modified July 7, 2009. Version 2.
Checksum: 0E4057E33C3F19A6

FASTA1,009112,907
        10         20         30         40         50         60 
MSLAFKIFFP QTLRALSRKE LCLFRKHHWR DVRQFSQWSE TDLLHGHPLF LRRKPVLSFQ 

        70         80         90        100        110        120 
GSHLRSRATY LVFLPGLHVG LCSGPCEMAE QRFCVDYAKR GTAGCKKCKE KIVKGVCRIG 

       130        140        150        160        170        180 
KVVPNPFSES GGDMKEWYHI KCMFEKLERA RATTKKIEDL TELEGWEELE DNEKEQITQH 

       190        200        210        220        230        240 
IADLSSKAAG TPKKKAVVQA KLTTTGQVTS PVKGASFVTS TNPRKFSGFS AKPNNSGEAP 

       250        260        270        280        290        300 
SSPTPKRSLS SSKCDPRHKD CLLREFRKLC AMVADNPSYN TKTQIIQDFL RKGSAGDGFH 

       310        320        330        340        350        360 
GDVYLTVKLL LPGVIKTVYN LNDKQIVKLF SRIFNCNPDD MARDLEQGDV SETIRVFFEQ 

       370        380        390        400        410        420 
SKSFPPAAKS LLTIQEVDEF LLRLSKLTKE DEQQQALQDI ASRCTANDLK CIIRLIKHDL 

       430        440        450        460        470        480 
KMNSGAKHVL DALDPNAYEA FKASRNLQDV VERVLHNAQE VEKEPGQRRA LSVQASLMTP 

       490        500        510        520        530        540 
VQPMLAEACK SVEYAMKKCP NGMFSEIKYD GERVQVHKNG DHFSYFSRSL KPVLPHKVAH 

       550        560        570        580        590        600 
FKDYIPQAFP GGHSMILDSE VLLIDNKTGK PLPFGTLGVH KKAAFQDANV CLFVFDCIYF 

       610        620        630        640        650        660 
NDVSLMDRPL CERRKFLHDN MVEIPNRIMF SEMKRVTKAL DLADMITRVI QEGLEGLVLK 

       670        680        690        700        710        720 
DVKGTYEPGK RHWLKVKKDY LNEGAMADTA DLVVLGAFYG QGSKGGMMSI FLMGCYDPGS 

       730        740        750        760        770        780 
QKWCTVTKCA GGHDDATLAR LQNELDMVKI SKDPSKIPSW LKVNKIYYPD FIVPDPKKAA 

       790        800        810        820        830        840 
VWEITGAEFS KSEAHTADGI SIRFPRCTRI RDDKDWKSAT NLPQLKELYQ LSKEKADFTV 

       850        860        870        880        890        900 
VAGDEGSSTT GGSSEENKGP SGSAVSRKAP SKPSASTKKA EGKLSNSNSK DGNMQTAKPS 

       910        920        930        940        950        960 
AMKVGEKLAT KSSPVKVGEK RKAADETLCQ TKVLLDIFTG VRLYLPPSTP DFSRLRRYFV 

       970        980        990       1000 
AFDGDLVQEF DMTSATHVLG SRDKNPAAQQ VSPEWIWACI RKRRLVAPC 

« Hide

Isoform Beta [UniParc].

Checksum: 0C10E40E0686DB77
Show »

FASTA949106,018

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination."
Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C., Yu G.-L., Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E., Haseltine W.A., Lindahl T.
Mol. Cell. Biol. 15:3206-3216(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Tissue: Prostate.
[2]"Mammalian DNA ligase III: molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination."
Chen J., Tomkinson A.E., Ramos W., Mackey Z.B., Danehower S., Walter C.A., Schultz R.A., Besterman J.M., Husain I.
Mol. Cell. Biol. 15:5412-5422(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
Tissue: Testis.
[3]NIEHS SNPs program
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-867.
[4]"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].
[5]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].
[6]"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 ALPHA).
Tissue: Pancreas.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"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 SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Expression, purification, and biophysical characterization of the BRCT domain of human DNA ligase IIIalpha."
Thornton K.H., Krishnan V.V., West M.G., Popham J., Ramirez M., Thelen M.P., Cosman M.
Protein Expr. Purif. 21:401-411(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 924-1009.
[16]"Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha."
Kulczyk A.W., Yang J.C., Neuhaus D.
J. Mol. Biol. 341:723-738(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-204.
[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-717.
+Additional computationally mapped references.

Web resources

Wikipedia

DNA ligase entry

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84740 mRNA. Translation: CAA59230.1. Different initiation.
U40671 mRNA. Translation: AAA85022.1. Different initiation.
AF491645 Genomic DNA. Translation: AAL91592.1. Different initiation.
AC004223 Genomic DNA. No translation available.
AC022903 Genomic DNA. No translation available.
CH471147 Genomic DNA. Translation: EAW80199.1.
BC068005 mRNA. Translation: AAH68005.1.
PIRI37292.
RefSeqNP_002302.2. NM_002311.4.
NP_039269.2. NM_013975.3.
XP_005258028.1. XM_005257971.2.
UniGeneHs.100299.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IMONMR-A924-1009[»]
1IN1NMR-A924-1009[»]
1UW0NMR-A88-204[»]
3L2PX-ray3.00A257-833[»]
3PC7X-ray1.65A/B924-1008[»]
3PC8X-ray2.31C/D924-1008[»]
3QVGX-ray2.26A/C924-1008[»]
ProteinModelPortalP49916.
SMRP49916. Positions 88-204, 257-833, 928-1008.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110168. 18 interactions.
IntActP49916. 7 interactions.
MINTMINT-4531178.
STRING9606.ENSP00000367787.

Chemistry

DrugBankDB00290. Bleomycin.

PTM databases

PhosphoSiteP49916.

Polymorphism databases

DMDM251757259.

Proteomic databases

PaxDbP49916.
PRIDEP49916.

Protocols and materials databases

DNASU3980.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262327; ENSP00000262327; ENSG00000005156. [P49916-2]
ENST00000378526; ENSP00000367787; ENSG00000005156. [P49916-1]
GeneID3980.
KEGGhsa:3980.
UCSCuc002hik.2. human. [P49916-1]

Organism-specific databases

CTD3980.
GeneCardsGC17P033307.
HGNCHGNC:6600. LIG3.
HPAHPA006723.
MIM600940. gene.
neXtProtNX_P49916.
PharmGKBPA30374.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1793.
HOGENOMHOG000007653.
HOVERGENHBG005515.
InParanoidP49916.
KOK10776.
OMALFSEMKH.
OrthoDBEOG7BKCT2.
PhylomeDBP49916.
TreeFamTF316220.

Enzyme and pathway databases

BRENDA6.5.1.1. 2681.
ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP49916.
BgeeP49916.
CleanExHS_LIG3.
GenevestigatorP49916.

Family and domain databases

Gene3D1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
3.30.1740.10. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR000977. DNA_ligase_ATP-dep.
IPR012309. DNA_ligase_ATP-dep_C.
IPR012310. DNA_ligase_ATP-dep_cent.
IPR016059. DNA_ligase_ATP-dep_CS.
IPR012308. DNA_ligase_ATP-dep_N.
IPR012340. NA-bd_OB-fold.
IPR001510. Znf_PARP.
[Graphical view]
PfamPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
PF00645. zf-PARP. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF52113. SSF52113. 1 hit.
TIGRFAMsTIGR00574. dnl1. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
PS00347. PARP_ZN_FINGER_1. 1 hit.
PS50064. PARP_ZN_FINGER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLIG3. human.
EvolutionaryTraceP49916.
GeneWikiLIG3.
GenomeRNAi3980.
NextBio15598.
PROP49916.
SOURCESearch...

Entry information

Entry nameDNLI3_HUMAN
AccessionPrimary (citable) accession number: P49916
Secondary accession number(s): Q16714, Q6NVK3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: April 16, 2014
This is version 155 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 17

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