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Q9HB75 (PIDD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
p53-induced protein with a death domain
Alternative name(s):
Leucine-rich repeat and death domain-containing protein
Gene names
Name:PIDD
Synonyms:LRDD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length910 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes apoptosis downstream of the tumor suppressor as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. Associates with NEMO/IKBKG and RIP1 and enhances sumoylation and ubiquitination of NEMO/IKBKG which is important for activation of the transcription factor NF-kappa-B. Associates with CASP2/caspase-2 and CRADD/RAIDD, and induces activation of CASP2 which an important regulator in apoptotic pathways. Ref.2 Ref.9 Ref.10

Subunit structure

Interacts with FADD and MAP-kinase activating death domain/MADD. Forms a complex with IKBKG and with receptor-interacting serine-threonine kinase 1/RIP1. Forms also a complex named PIDDosome with CASP2 and CRADD. Ref.1 Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasm. Nucleus Ref.10.

Tissue specificity

Ubiquitous. Ref.1

Induction

Induced by gamma-irradiation. Ref.2

Sequence similarities

Contains 1 death domain.

Contains 7 LRR (leucine-rich) repeats.

Contains 1 peptidase S68 domain.

Contains 2 ZU5 domains.

Sequence caution

The sequence BAD92069.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD92186.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD92766.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAD38708.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainLeucine-rich repeat
Repeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Inferred from mutant phenotype PubMed 21726810. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 21726810. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 21726810. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Traceable author statement PubMed 18309324. Source: UniProtKB

positive regulation of apoptotic process

Traceable author statement PubMed 18309324. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from mutant phenotype PubMed 21726810. Source: UniProtKB

nucleus

Inferred from mutant phenotype PubMed 21726810. Source: UniProtKB

   Molecular_functiondeath receptor binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HB75-1)

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: Q9HB75-2)

The sequence of this isoform differs from the canonical sequence as follows:
     704-720: Missing.
Isoform 3 (identifier: Q9HB75-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: Missing.
     579-589: Missing.
Isoform 4 (identifier: Q9HB75-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-313: Missing.
Isoform 5 (identifier: Q9HB75-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-313: Missing.
     589-589: W → WSVPPSFLSPPPPVCTALLTPSSPR
     759-815: RLRGSEGPRR...VALHLGVSYR → VGLRDSRGAG...GGGLASPWHP
     816-910: Missing.
Isoform 6 (identifier: Q9HB75-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-492: Missing.
     589-589: W → WSVPPSFLSPPPPVCTALLTPSSPR
     704-720: Missing.
     759-815: RLRGSEGPRR...VALHLGVSYR → VGLRDSRGAG...GGGLASPWHP
     816-910: Missing.
Isoform 7 (identifier: Q9HB75-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-313: Missing.
     585-621: THFSWYWLWYTTKNCVGGLARKAWERLRLHRVNLIAL → LALVHHQELCGRPGSEGLGAAAAAPCEPHRSAAAPGP
     622-910: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 910909p53-induced protein with a death domain
PRO_0000245243

Regions

Repeat126 – 14722LRR 1
Repeat149 – 17123LRR 2
Repeat172 – 19423LRR 3
Repeat195 – 21622LRR 4
Repeat218 – 24023LRR 5
Repeat241 – 26323LRR 6
Repeat264 – 28522LRR 7
Domain315 – 422108ZU5 1
Domain423 – 45230Peptidase S68
Domain453 – 565113ZU5 2
Domain788 – 87386Death
Region580 – 716137UPA domain By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue2991Phosphoserine Ref.8
Modified residue3051Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 492492Missing in isoform 6.
VSP_019664
Alternative sequence1 – 313313Missing in isoform 4, isoform 5 and isoform 7.
VSP_019665
Alternative sequence1 – 146146Missing in isoform 3.
VSP_019666
Alternative sequence579 – 58911Missing in isoform 3.
VSP_019667
Alternative sequence585 – 62137THFSW…NLIAL → LALVHHQELCGRPGSEGLGA AAAAPCEPHRSAAAPGP in isoform 7.
VSP_019668
Alternative sequence5891W → WSVPPSFLSPPPPVCTALLT PSSPR in isoform 5 and isoform 6.
VSP_019669
Alternative sequence622 – 910289Missing in isoform 7.
VSP_019670
Alternative sequence704 – 72017Missing in isoform 2 and isoform 6.
VSP_019671
Alternative sequence759 – 81557RLRGS…GVSYR → VGLRDSRGAGQDRGPGVTRV TWWSWGWSPGLNALFPSNRD FEGPRGHGGGLASPWHP in isoform 5 and isoform 6.
VSP_019672
Alternative sequence816 – 91095Missing in isoform 5 and isoform 6.
VSP_019673
Natural variant3311Q → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Corresponds to variant rs10902221 [ dbSNP | Ensembl ].
VAR_028031

Experimental info

Sequence conflict3351V → A in BAC11272. Ref.4
Sequence conflict4211W → L in AAP97716. Ref.3
Sequence conflict4921S → F in BAC11272. Ref.4
Sequence conflict5121A → V in CAD38708. Ref.6
Sequence conflict6011G → E in CAD38708. Ref.6
Sequence conflict8951A → V in AAF69491. Ref.1

Secondary structure

................ 910
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: 8C98FC64230B57F8

FASTA91099,712
        10         20         30         40         50         60 
MAATVEGPEL EAAAAAGDAS EDSDAGSRAL PFLGGNRLSL DLYPGGCQQL LHLCVQQPLQ 

        70         80         90        100        110        120 
LLQVEFLRLS THEDPQLLEA TLAQLPQSLS CLRSLVLKGG QRRDTLGACL RGALTNLPAG 

       130        140        150        160        170        180 
LSGLAHLAHL DLSFNSLETL PACVLQMRGL GALLLSHNCL SELPEALGAL PALTFLTVTH 

       190        200        210        220        230        240 
NRLQTLPPAL GALSTLQRLD LSQNLLDTLP PEIGGLGSLL ELNLASNRLQ SLPASLAGLR 

       250        260        270        280        290        300 
SLRLLVLHSN LLASVPADLA RLPLLTRLDL RDNQLRDLPP ELLDAPFVRL QGNPLGEASP 

       310        320        330        340        350        360 
DAPSSPVAAL IPEMPRLFLT SDLDSFPVTP QGCSVTLACG VRLQFPAGAT ATPITIRYRL 

       370        380        390        400        410        420 
LLPEPGLVPL GPHDALLSHV LELQPHGVAF QQDVGLWLLF TPPQARRCRE VVVRTRNDNS 

       430        440        450        460        470        480 
WGDLETYLEE EAPQRLWAHC QVPHFSWFLV VSRPVSNACL VPPEGTLLCS SGHPGVKVIF 

       490        500        510        520        530        540 
PPGATEEPRR VSMQVVRMAG RELQALLGEP EAAVSPLLCL SQSGPPSFLQ PVTVQLPLPS 

       550        560        570        580        590        600 
GITGLSLDRS RLHLLYWAPP AATWDDITAQ VVLELTHLYA RFQVTHFSWY WLWYTTKNCV 

       610        620        630        640        650        660 
GGLARKAWER LRLHRVNLIA LQRRRDPEQV LLQCLPRNKV DATLRRLLER YRGPEPSDTV 

       670        680        690        700        710        720 
EMFEGEEFFA AFERGIDVDA DRPDCVEGRI CFVFYSHLKN VKEVYVTTTL DREAQAVRGQ 

       730        740        750        760        770        780 
VSFYRGAVPV RVPEEAEAAR QRKGADALWM ATLPIKLPRL RGSEGPRRGA GLSLAPLNLG 

       790        800        810        820        830        840 
DAETGFLTQS NLLSVAGRLG LDWPAVALHL GVSYREVQRI RHEFRDDLDE QIRHMLFSWA 

       850        860        870        880        890        900 
ERQAGQPGAV GLLVQALEQS DRQDVAEEVR AVLELGRRKY QDSIRRMGLA PKDPALPGSS 

       910 
APQPPEPAQA 

« Hide

Isoform 2 [UniParc].

Checksum: 426694FB8EC10235
Show »

FASTA89397,823
Isoform 3 [UniParc].

Checksum: 6BD2B00A12B574DC
Show »

FASTA75382,971
Isoform 4 [UniParc].

Checksum: 2572BA6345C426AA
Show »

FASTA59766,720
Isoform 5 [UniParc].

Checksum: ACB01B6B05784BF1
Show »

FASTA52658,652
Isoform 6 [UniParc].

Checksum: 1A8F34F669B0F38A
Show »

FASTA33037,019
Isoform 7 [UniParc].

Checksum: 5E814E02D2E0E4CB
Show »

FASTA30833,375

References

« Hide 'large scale' references
[1]"LRDD, a novel leucine rich repeat and death domain containing protein."
Telliez J.-B., Bean K.M., Lin L.-L.
Biochim. Biophys. Acta 1478:280-288(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH FADD AND MADD, VARIANT ARG-331.
[2]"Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis."
Lin Y., Ma W., Benchimol S.
Nat. Genet. 26:122-127(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, VARIANT ARG-331.
[3]Zan Q., Guo J.H., Yu L.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT ARG-331.
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), VARIANT ARG-331.
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6), VARIANT ARG-331.
Tissue: Brain and Spleen.
[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] (ISOFORM 5), VARIANT ARG-331.
Tissue: Testis.
[7]"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 ARG-331.
Tissue: Uterus.
[8]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-37; 69-93; 103-111; 183-316; 343-357; 415-435; 454-497; 552-581; 598-605; 613-623; 626-637; 651-740; 743-759; 768-798 AND 826-870, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-299 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[9]"The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress."
Tinel A., Tschopp J.
Science 304:843-846(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, INTERACTION WITH CASP2 AND CRADD.
[10]"PIDD mediates NF-kappaB activation in response to DNA damage."
Janssens S., Tinel A., Lippens S., Tschopp J.
Cell 123:1079-1092(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IKBKG AND RIP1, SUBCELLULAR LOCATION.
[11]"Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage."
Vakifahmetoglu H., Olsson M., Orrenius S., Zhivotovsky B.
Oncogene 25:5683-5692(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASP2 AND CRADD.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF229178 mRNA. Translation: AAF69491.1.
AF274972 mRNA. Translation: AAG13461.1.
AF465246 mRNA. Translation: AAP97716.1.
AK074893 mRNA. Translation: BAC11272.1.
AB208832 mRNA. Translation: BAD92069.1. Different initiation.
AB208949 mRNA. Translation: BAD92186.1. Different initiation.
AB209529 mRNA. Translation: BAD92766.1. Different initiation.
AL833849 mRNA. Translation: CAD38708.1. Different initiation.
BC014904 mRNA. Translation: AAH14904.1.
RefSeqNP_665893.2. NM_145886.3.
NP_665894.2. NM_145887.3.
UniGeneHs.592290.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OF5X-ray3.20H/I/J/K/L778-883[»]
ProteinModelPortalQ9HB75.
SMRQ9HB75. Positions 36-876.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120645. 35 interactions.
IntActQ9HB75. 12 interactions.
MINTMINT-1474528.

Protein family/group databases

MEROPSS68.001.

PTM databases

PhosphoSiteQ9HB75.

Polymorphism databases

DMDM116242715.

Proteomic databases

PaxDbQ9HB75.
PRIDEQ9HB75.

Protocols and materials databases

DNASU55367.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347755; ENSP00000337797; ENSG00000177595. [Q9HB75-1]
ENST00000411829; ENSP00000416801; ENSG00000177595. [Q9HB75-2]
GeneID55367.
KEGGhsa:55367.
UCSCuc001lrk.2. human. [Q9HB75-2]
uc001lrl.1. human. [Q9HB75-3]
uc001lrm.1. human. [Q9HB75-1]
uc001lrp.2. human. [Q9HB75-5]

Organism-specific databases

CTD55367.
GeneCardsGC11M000799.
H-InvDBHIX0021767.
HGNCHGNC:16491. PIDD.
HPACAB012647.
HPA055473.
MIM605247. gene.
neXtProtNX_Q9HB75.
PharmGKBPA30445.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310879.
HOVERGENHBG066762.
InParanoidQ9HB75.
KOK10130.
OMAVPHFSWF.
OrthoDBEOG7BP81T.
PhylomeDBQ9HB75.
TreeFamTF331183.

Enzyme and pathway databases

SignaLinkQ9HB75.

Gene expression databases

ArrayExpressQ9HB75.
BgeeQ9HB75.
GenevestigatorQ9HB75.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR019502. Peptidase_S68_pidd.
IPR000906. ZU5.
[Graphical view]
PfamPF00531. Death. 1 hit.
PF00560. LRR_1. 1 hit.
PF10461. Peptidase_S68. 1 hit.
PF00791. ZU5. 2 hits.
[Graphical view]
SMARTSM00005. DEATH. 1 hit.
SM00369. LRR_TYP. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS51450. LRR. 7 hits.
PS51145. ZU5. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIDD. human.
EvolutionaryTraceQ9HB75.
GeneWikiLRDD.
GenomeRNAi55367.
NextBio59757.
PROQ9HB75.
SOURCESearch...

Entry information

Entry namePIDD_HUMAN
AccessionPrimary (citable) accession number: Q9HB75
Secondary accession number(s): Q59FD1 expand/collapse secondary AC list , Q59H10, Q59HC7, Q7Z4P8, Q8NC89, Q8NDL2, Q96C25, Q9NRE6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 109 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

Peptidase families

Classification of peptidase families and list of entries

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 11

Human chromosome 11: entries, gene names and cross-references to MIM