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O75976 (CBPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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:
Carboxypeptidase D

EC=3.4.17.22
Alternative name(s):
Metallocarboxypeptidase D
gp180
Gene names
Name:CPD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Releases C-terminal Arg and Lys from polypeptides.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Highly expressed in placenta, pancreas and hepatoma cells. Lower levels found in skeletal muscle, heart and colon carcinoma and melanoma cell lines.

Domain

There are 3 carboxypeptidase-like domains. Only the first two domains seem to have kept a catalytic activity.

Sequence similarities

Belongs to the peptidase M14 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0-6.5.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75976-1)

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: O75976-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MA → MR
     3-249: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 13801349Carboxypeptidase D
PRO_0000004401

Regions

Topological domain32 – 12991268Extracellular Potential
Transmembrane1300 – 132021Helical; Potential
Topological domain1321 – 138060Cytoplasmic Potential
Region32 – 493462Carboxypeptidase-like 1
Region494 – 897404Carboxypeptidase-like 2
Region898 – 1299402Carboxypeptidase-like 3
Motif162 – 1643Cell attachment site Potential

Sites

Active site3501Nucleophile 1 By similarity
Active site7621Nucleophile 2 By similarity
Metal binding1391Zinc 1 By similarity
Metal binding1421Zinc 1 By similarity
Metal binding2571Zinc 1 By similarity
Metal binding5641Zinc 2 By similarity
Metal binding5671Zinc 2 By similarity
Metal binding6711Zinc 2 By similarity

Amino acid modifications

Modified residue13581Phosphoserine Ref.12 Ref.14
Modified residue13611Phosphoserine Ref.12 Ref.14
Modified residue13681Phosphothreonine Ref.10 Ref.12 Ref.14
Modified residue13701Phosphothreonine Ref.10 Ref.12 Ref.14
Lipidation13171S-palmitoyl cysteine Ref.8
Lipidation13211S-palmitoyl cysteine Ref.8
Lipidation13231S-palmitoyl cysteine Ref.8
Glycosylation1721N-linked (GlcNAc...) Ref.9
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation3991N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation6261N-linked (GlcNAc...) Potential
Glycosylation8111N-linked (GlcNAc...) Ref.9 Ref.11
Glycosylation8551N-linked (GlcNAc...) Potential
Glycosylation8671N-linked (GlcNAc...) Potential
Glycosylation8791N-linked (GlcNAc...) Potential
Glycosylation9551N-linked (GlcNAc...) Ref.9 Ref.11
Glycosylation9781N-linked (GlcNAc...) Potential
Glycosylation10701N-linked (GlcNAc...) Ref.11
Glycosylation11421N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 22MA → MR in isoform 2.
VSP_045833
Alternative sequence3 – 249247Missing in isoform 2.
VSP_045834
Natural variant361K → E. Ref.6
Corresponds to variant rs17857300 [ dbSNP | Ensembl ].
VAR_027771
Natural variant4541E → G. Ref.6
Corresponds to variant rs17857301 [ dbSNP | Ensembl ].
VAR_027772
Natural variant5051H → N. Ref.6
Corresponds to variant rs17854355 [ dbSNP | Ensembl ].
VAR_027773
Natural variant8991T → I.
Corresponds to variant rs1860543 [ dbSNP | Ensembl ].
VAR_027774

Experimental info

Sequence conflict8631A → V in BAH14780. Ref.3
Sequence conflict8961D → V Ref.1
Sequence conflict8961D → V Ref.2
Sequence conflict9481M → I in BAH14780. Ref.3
Sequence conflict13361R → W in BAH13725. Ref.3

Sequences

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

Last modified October 3, 2006. Version 2.
Checksum: 567EC1F0B4B7A0C8

FASTA1,380152,931
        10         20         30         40         50         60 
MASGRDERPP WRLGRLLLLM CLLLLGSSAR AAHIKKAEAT TTTTSAGAEA AEGQFDRYYH 

        70         80         90        100        110        120 
EEELESALRE AAAAGLPGLA RLFSIGRSVE GRPLWVLRLT AGLGSLIPEG DAGPDAAGPD 

       130        140        150        160        170        180 
AAGPLLPGRP QVKLVGNMHG DETVSRQVLI YLARELAAGY RRGDPRLVRL LNTTDVYLLP 

       190        200        210        220        230        240 
SLNPDGFERA REGDCGFGDG GPSGASGRDN SRGRDLNRSF PDQFSTGEPP ALDEVPEVRA 

       250        260        270        280        290        300 
LIEWIRRNKF VLSGNLHGGS VVASYPFDDS PEHKATGIYS KTSDDEVFKY LAKAYASNHP 

       310        320        330        340        350        360 
IMKTGEPHCP GDEDETFKDG ITNGAHWYDV EGGMQDYNYV WANCFEITLE LSCCKYPPAS 

       370        380        390        400        410        420 
QLRQEWENNR ESLITLIEKV HIGVKGFVKD SITGSGLENA TISVAGINHN ITTGRFGDFY 

       430        440        450        460        470        480 
RLLVPGTYNL TVVLTGYMPL TVTNVVVKEG PATEVDFSLR PTVTSVIPDT TEAVSTASTV 

       490        500        510        520        530        540 
AIPNILSGTS SSYQPIQPKD FHHHHFPDME IFLRRFANEY PNITRLYSLG KSVESRELYV 

       550        560        570        580        590        600 
MEISDNPGVH EPGEPEFKYI GNMHGNEVVG RELLLNLIEY LCKNFGTDPE VTDLVHNTRI 

       610        620        630        640        650        660 
HLMPSMNPDG YEKSQEGDSI SVIGRNNSNN FDLNRNFPDQ FVQITDPTQP ETIAVMSWMK 

       670        680        690        700        710        720 
SYPFVLSANL HGGSLVVNYP FDDDEQGLAT YSKSPDDAVF QQIALSYSKE NSQMFQGRPC 

       730        740        750        760        770        780 
KNMYPNEYFP HGITNGASWY NVPGGMQDWN YLQTNCFEVT IELGCVKYPL EKELPNFWEQ 

       790        800        810        820        830        840 
NRRSLIQFMK QVHQGVRGFV LDATDGRGIL NATISVAEIN HPVTTYKTGD YWRLLVPGTY 

       850        860        870        880        890        900 
KITASARGYN PVTKNVTVKS EGAIQVNFTL VRSSTDSNNE SKKGKGASSS TNDASDPTTK 

       910        920        930        940        950        960 
EFETLIKDLS AENGLESLML RSSSNLALAL YRYHSYKDLS EFLRGLVMNY PHITNLTNLG 

       970        980        990       1000       1010       1020 
QSTEYRHIWS LEISNKPNVS EPEEPKIRFV AGIHGNAPVG TELLLALAEF LCLNYKKNPA 

      1030       1040       1050       1060       1070       1080 
VTQLVDRTRI VIVPSLNPDG RERAQEKDCT SKIGQTNARG KDLDTDFTNN ASQPETKAII 

      1090       1100       1110       1120       1130       1140 
ENLIQKQDFS LSVALDGGSM LVTYPYDKPV QTVENKETLK HLASLYANNH PSMHMGQPSC 

      1150       1160       1170       1180       1190       1200 
PNKSDENIPG GVMRGAEWHS HLGSMKDYSV TYGHCPEITV YTSCCYFPSA ARLPSLWADN 

      1210       1220       1230       1240       1250       1260 
KRSLLSMLVE VHKGVHGFVK DKTGKPISKA VIVLNEGIKV QTKEGGYFHV LLAPGVHNII 

      1270       1280       1290       1300       1310       1320 
AIADGYQQQH SQVFVHHDAA SSVVIVFDTD NRIFGLPREL VVTVSGATMS ALILTACIIW 

      1330       1340       1350       1360       1370       1380 
CICSIKSNRH KDGFHRLRQH HDEYEDEIRM MSTGSKKSLL SHEFQDETDT EEETLYSSKH 

« Hide

Isoform 2 [UniParc].

Checksum: D253BDC1BA9B56B6
Show »

FASTA1,133126,487

References

« Hide 'large scale' references
[1]"Cloning, functional expression, and chromosomal localization of the human and mouse gp180-carboxypeptidase D-like enzyme."
Ishikawa T., Murakami K., Kido Y., Ohnishi S., Yazaki Y., Harada F., Kuroki K.
Gene 215:361-370(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal liver.
[2]"Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains."
Tan F., Rehli M., Krause S.W., Skidgel R.A.
Biochem. J. 327:81-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain and Placenta.
[3]"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 2).
Tissue: Testis.
[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]Tan F., Rehli M., Skidgel R.A.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 11-13; 49-52; 159-162 AND 493.
[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 1), VARIANTS GLU-36; GLY-454 AND ASN-505.
Tissue: Testis.
[7]"Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein."
McGwire G.B., Tan F., Michel B., Rehli M., Skidgel R.A.
Life Sci. 60:715-724(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking."
Kalinina E.V., Fricker L.D.
J. Biol. Chem. 278:9244-9249(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-1317; CYS-1321 AND CYS-1323.
[9]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-172; ASN-811 AND ASN-955.
[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 THR-1368 AND THR-1370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-811; ASN-955 AND ASN-1070.
Tissue: Liver.
[12]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358; SER-1361; THR-1368 AND THR-1370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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-1358; SER-1361; THR-1368 AND THR-1370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85390 mRNA. Translation: BAA33370.1.
U65090 mRNA. Translation: AAC51775.2.
AK302497 mRNA. Translation: BAH13725.1.
AK316409 mRNA. Translation: BAH14780.1.
AC006050 Genomic DNA. No translation available.
AC090685 Genomic DNA. No translation available.
BC045549 mRNA. Translation: AAH45549.1.
BC045624 mRNA. Translation: AAH45624.1.
BC051702 mRNA. Translation: AAH51702.1.
CCDSCCDS11257.1. [O75976-1]
CCDS56025.1. [O75976-2]
RefSeqNP_001186704.1. NM_001199775.1. [O75976-2]
NP_001295.2. NM_001304.4. [O75976-1]
UniGeneHs.446079.

3D structure databases

ProteinModelPortalO75976.
SMRO75976. Positions 47-460, 494-873, 898-1266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107754. 10 interactions.
IntActO75976. 1 interaction.
MINTMINT-5003925.
STRING9606.ENSP00000225719.

Protein family/group databases

MEROPSM14.011.

PTM databases

PhosphoSiteO75976.

Proteomic databases

MaxQBO75976.
PaxDbO75976.
PRIDEO75976.

Protocols and materials databases

DNASU1362.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225719; ENSP00000225719; ENSG00000108582. [O75976-1]
ENST00000543464; ENSP00000444443; ENSG00000108582. [O75976-2]
GeneID1362.
KEGGhsa:1362.
UCSCuc002hfb.2. human. [O75976-1]

Organism-specific databases

CTD1362.
GeneCardsGC17P028705.
HGNCHGNC:2301. CPD.
HPAHPA052796.
MIM603102. gene.
neXtProtNX_O75976.
PharmGKBPA26823.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2866.
HOGENOMHOG000046445.
HOVERGENHBG006932.
InParanoidO75976.
KOK07752.
OMAEKVHIGV.
OrthoDBEOG7B8S32.
PhylomeDBO75976.
TreeFamTF315592.

Enzyme and pathway databases

BRENDA3.4.17.22. 2681.
ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressO75976.
BgeeO75976.
CleanExHS_CPD.
GenevestigatorO75976.

Family and domain databases

Gene3D2.60.40.1120. 3 hits.
InterProIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERPTHR11532:SF40. PTHR11532:SF40. 1 hit.
PfamPF00246. Peptidase_M14. 3 hits.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 3 hits.
[Graphical view]
SUPFAMSSF49464. SSF49464. 3 hits.
PROSITEPS00132. CARBOXYPEPT_ZN_1. 2 hits.
PS00133. CARBOXYPEPT_ZN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCPD. human.
GeneWikiCPD_(gene).
GenomeRNAi1362.
NextBio35480310.
PROO75976.
SOURCESearch...

Entry information

Entry nameCBPD_HUMAN
AccessionPrimary (citable) accession number: O75976
Secondary accession number(s): B7Z7T9 expand/collapse secondary AC list , B7ZAU4, F5GZH6, O15377, Q86SH9, Q86XE6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 128 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

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