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Q504Q3

- PAN2_HUMAN

UniProt

Q504Q3 - PAN2_HUMAN

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Protein

PAB-dependent poly(A)-specific ribonuclease subunit PAN2

Gene

PAN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by poly(A)-binding protein (PABP), which is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1.2 PublicationsUniRule annotation

Catalytic activityi

Exonucleolytic cleavage of poly(A) to 5'-AMP.1 PublicationUniRule annotation

Enzyme regulationi

Positively regulated by the regulatory subunit PAN3.UniRule annotation

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: UniProtKB
  2. nucleic acid binding Source: InterPro
  3. poly(A)-specific ribonuclease activity Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA metabolic process Source: Reactome
  3. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  4. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

mRNA processing

Enzyme and pathway databases

ReactomeiREACT_20514. Deadenylation of mRNA.

Protein family/group databases

MEROPSiC19.978.

Names & Taxonomyi

Protein namesi
Recommended name:
PAB-dependent poly(A)-specific ribonuclease subunit PAN2UniRule annotation (EC:3.1.13.4UniRule annotation)
Short name:
hPan2
Alternative name(s):
Inactive ubiquitin carboxyl-terminal hydrolase 52UniRule annotation
PAB1P-dependent poly(A)-nucleaseUniRule annotation
PAN deadenylation complex catalytic subunit 2UniRule annotation
Gene namesi
Name:PAN2UniRule annotation
Synonyms:KIAA0710, USP52
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:20074. PAN2.

Subcellular locationi

CytoplasmP-body. Nucleus
Note: Shuttles between nucleus and cytoplasm.

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: Ensembl
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB-KW
  4. PAN complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1087 – 10871D → A: Loss of exonuclease activity. 1 Publication

Organism-specific databases

PharmGKBiPA162398664.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12021202PAB-dependent poly(A)-specific ribonuclease subunit PAN2PRO_0000280521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei791 – 7911Phosphoserine1 Publication
Modified residuei1189 – 11891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ504Q3.
PaxDbiQ504Q3.
PRIDEiQ504Q3.

PTM databases

PhosphoSiteiQ504Q3.

Expressioni

Gene expression databases

BgeeiQ504Q3.
CleanExiHS_PAN2.
ExpressionAtlasiQ504Q3. baseline and differential.
GenevestigatoriQ504Q3.

Interactioni

Subunit structurei

Interacts with the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex.2 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
PAN3Q58A456EBI-1058976,EBI-2513054

Protein-protein interaction databases

BioGridi115252. 341 interactions.
DIPiDIP-50708N.
IntActiQ504Q3. 16 interactions.
STRINGi9606.ENSP00000368809.

Structurei

3D structure databases

ProteinModelPortaliQ504Q3.
SMRiQ504Q3. Positions 75-736, 847-1183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati153 – 19341WD 1Add
BLAST
Repeati195 – 23137WD 2Add
BLAST
Repeati244 – 28037WD 3Add
BLAST
Repeati328 – 36740WD 4Add
BLAST
Domaini517 – 924408USPUniRule annotationAdd
BLAST
Domaini975 – 1147173ExonucleaseUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family. PAN2 subfamily.UniRule annotation
Contains 1 exonuclease domain.UniRule annotation
Contains 1 USP domain.UniRule annotation
Contains 4 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG0847.
GeneTreeiENSGT00390000013978.
HOGENOMiHOG000230585.
HOVERGENiHBG089847.
InParanoidiQ504Q3.
KOiK12571.
OMAiMEADWDE.
OrthoDBiEOG7JHM4K.
PhylomeDBiQ504Q3.
TreeFamiTF105657.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.420.10. 1 hit.
HAMAPiMF_03182. PAN2.
InterProiIPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR028881. PAN2.
IPR012337. RNaseH-like_dom.
IPR028889. UCH/PAN2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
PF13423. UCH_1. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEiPS50235. USP_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q504Q3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNFEGLDPGL AEYAPAMHSA LDPVLDAHLN PSLLQNVELD PEGVALEALP
60 70 80 90 100
VQESVHIMEG VYSELHSVVA EVGVPVSVSH FDLHEEMLWV GSHGGHATSF
110 120 130 140 150
FGPALERYSS FQVNGSDDIR QIQSLENGIL FLTKNNLKYM ARGGLIIFDY
160 170 180 190 200
LLDENEDMHS LLLTDSSTLL VGGLQNHIIE IDLNTVQETQ KYAVETPGVT
210 220 230 240 250
IMRQTNRFFF CGHTSGKVSL RDLRTFKVEH EFDAFSGSLS DFDVHGNLLA
260 270 280 290 300
ACGFSSRLTG LACDRFLKVY DLRMMRAITP LQVHVDPAFL RFIPTYTSRL
310 320 330 340 350
AIISQSGQCQ FCEPTGLANP ADIFHVNPVG PLLMTFDVSA SKQALAFGDS
360 370 380 390 400
EGCVHLWTDS PEPSFNPYSR ETEFALPCLV DSLPPLDWSQ DLLPLSLIPV
410 420 430 440 450
PLTTDTLLSD WPAANSAPAP RRAPPVDAEI LRTMKKVGFI GYAPNPRTRL
460 470 480 490 500
RNQIPYRLKE SDSEFDSFSQ VTESPVGREE EPHLHMVSKK YRKVTIKYSK
510 520 530 540 550
LGLEDFDFKH YNKTLFAGLE PHIPNAYCNC MIQVLYFLEP VRCLIQNHLC
560 570 580 590 600
QKEFCLACEL GFLFHMLDLS RGDPCQGNNF LRAFRTIPEA SALGLILADS
610 620 630 640 650
DEASGKGNLA RLIQRWNRFI LTQLHQDMQE LEIPQAYRGA GGSSFCSSGD
660 670 680 690 700
SVIGQLFSCE MENCSLCRCG SETVRASSTL LFTLSYPDGS KSDKTGKNYD
710 720 730 740 750
FAQVLKRSIC LDQNTQAWCD TCEKYQPTIQ TRNIRHLPDI LVINCEVNSS
760 770 780 790 800
KEADFWRMQA EVAFKMAVKK HGGEISKNKE FALADWKELG SPEGVLVCPS
810 820 830 840 850
IEELKNVWLP FSIRMKMTKN KGLDVCNWTD GDEMQWGPAR AEEEHGVYVY
860 870 880 890 900
DLMATVVHIL DSRTGGSLVA HIKVGETYHQ RKEGVTHQQW YLFNDFLIEP
910 920 930 940 950
IDKHEAVQFD MNWKVPAILY YVKRNLNSRY NLNIKNPIEA SVLLAEASLA
960 970 980 990 1000
RKQRKTHTTF IPLMLNEMPQ IGDLVGLDAE FVTLNEEEAE LRSDGTKSTI
1010 1020 1030 1040 1050
KPSQMSVARI TCVRGQGPNE GIPFIDDYIS TQEQVVDYLT QYSGIKPGDL
1060 1070 1080 1090 1100
DAKISSKHLT TLKSTYLKLR FLIDIGVKFV GHGLQKDFRV INLMVPKDQV
1110 1120 1130 1140 1150
LDTVYLFHMP RKRMISLRFL AWYFLDLKIQ GETHDSIEDA RTALQLYRKY
1160 1170 1180 1190 1200
LELSKNGTEP ESFHKVLKGL YEKGRKMDWK VPEPEGQTSP KNAAVFSSVL

AL
Length:1,202
Mass (Da):135,368
Last modified:May 18, 2010 - v3
Checksum:i579194C102FCA019
GO
Isoform 2 (identifier: Q504Q3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     689-692: Missing.

Show »
Length:1,198
Mass (Da):135,008
Checksum:i9F0D327BE78EC7D7
GO
Isoform 3 (identifier: Q504Q3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     643-643: Missing.

Note: No experimental confirmation available.

Show »
Length:1,201
Mass (Da):135,281
Checksum:iE185DC887D382DC1
GO

Sequence cautioni

The sequence BAA31685.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91G → E in AAH94885. (PubMed:15489334)Curated
Sequence conflicti1091 – 10911I → V in AAH94885. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321S → N.1 Publication
Corresponds to variant rs11558139 [ dbSNP | Ensembl ].
VAR_031162
Natural varianti179 – 1791I → L.3 Publications
Corresponds to variant rs1918496 [ dbSNP | Ensembl ].
VAR_031163
Natural varianti1201 – 12011A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036359

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei643 – 6431Missing in isoform 3. 1 PublicationVSP_023748
Alternative sequencei689 – 6924Missing in isoform 2. 2 PublicationsVSP_023749

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB107585 mRNA. Translation: BAD02263.1.
AB014610 mRNA. Translation: BAA31685.2. Different initiation.
BC024043 mRNA. Translation: AAH24043.1.
BC094885 mRNA. Translation: AAH94885.1.
CCDSiCCDS44922.1. [Q504Q3-1]
CCDS53802.1. [Q504Q3-3]
CCDS8915.1. [Q504Q3-2]
RefSeqiNP_001120932.1. NM_001127460.2.
NP_001159751.1. NM_001166279.1.
NP_055686.3. NM_014871.4.
UniGeneiHs.273397.

Genome annotation databases

EnsembliENST00000257931; ENSP00000257931; ENSG00000135473. [Q504Q3-3]
ENST00000425394; ENSP00000401721; ENSG00000135473. [Q504Q3-1]
ENST00000440411; ENSP00000388231; ENSG00000135473. [Q504Q3-2]
ENST00000548043; ENSP00000449861; ENSG00000135473. [Q504Q3-1]
ENST00000610546; ENSP00000481859; ENSG00000135473. [Q504Q3-1]
GeneIDi9924.
KEGGihsa:9924.
UCSCiuc001skx.3. human. [Q504Q3-1]
uc001sky.3. human. [Q504Q3-2]
uc001skz.3. human. [Q504Q3-3]

Polymorphism databases

DMDMi296439280.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB107585 mRNA. Translation: BAD02263.1 .
AB014610 mRNA. Translation: BAA31685.2 . Different initiation.
BC024043 mRNA. Translation: AAH24043.1 .
BC094885 mRNA. Translation: AAH94885.1 .
CCDSi CCDS44922.1. [Q504Q3-1 ]
CCDS53802.1. [Q504Q3-3 ]
CCDS8915.1. [Q504Q3-2 ]
RefSeqi NP_001120932.1. NM_001127460.2.
NP_001159751.1. NM_001166279.1.
NP_055686.3. NM_014871.4.
UniGenei Hs.273397.

3D structure databases

ProteinModelPortali Q504Q3.
SMRi Q504Q3. Positions 75-736, 847-1183.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115252. 341 interactions.
DIPi DIP-50708N.
IntActi Q504Q3. 16 interactions.
STRINGi 9606.ENSP00000368809.

Protein family/group databases

MEROPSi C19.978.

PTM databases

PhosphoSitei Q504Q3.

Polymorphism databases

DMDMi 296439280.

Proteomic databases

MaxQBi Q504Q3.
PaxDbi Q504Q3.
PRIDEi Q504Q3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257931 ; ENSP00000257931 ; ENSG00000135473 . [Q504Q3-3 ]
ENST00000425394 ; ENSP00000401721 ; ENSG00000135473 . [Q504Q3-1 ]
ENST00000440411 ; ENSP00000388231 ; ENSG00000135473 . [Q504Q3-2 ]
ENST00000548043 ; ENSP00000449861 ; ENSG00000135473 . [Q504Q3-1 ]
ENST00000610546 ; ENSP00000481859 ; ENSG00000135473 . [Q504Q3-1 ]
GeneIDi 9924.
KEGGi hsa:9924.
UCSCi uc001skx.3. human. [Q504Q3-1 ]
uc001sky.3. human. [Q504Q3-2 ]
uc001skz.3. human. [Q504Q3-3 ]

Organism-specific databases

CTDi 9924.
GeneCardsi GC12M056710.
HGNCi HGNC:20074. PAN2.
neXtProti NX_Q504Q3.
PharmGKBi PA162398664.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0847.
GeneTreei ENSGT00390000013978.
HOGENOMi HOG000230585.
HOVERGENi HBG089847.
InParanoidi Q504Q3.
KOi K12571.
OMAi MEADWDE.
OrthoDBi EOG7JHM4K.
PhylomeDBi Q504Q3.
TreeFami TF105657.

Enzyme and pathway databases

Reactomei REACT_20514. Deadenylation of mRNA.

Miscellaneous databases

GeneWikii USP52.
GenomeRNAii 9924.
NextBioi 37442.
PROi Q504Q3.

Gene expression databases

Bgeei Q504Q3.
CleanExi HS_PAN2.
ExpressionAtlasi Q504Q3. baseline and differential.
Genevestigatori Q504Q3.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
3.30.420.10. 1 hit.
HAMAPi MF_03182. PAN2.
InterProi IPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR028881. PAN2.
IPR012337. RNaseH-like_dom.
IPR028889. UCH/PAN2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00929. RNase_T. 1 hit.
PF13423. UCH_1. 1 hit.
[Graphical view ]
SMARTi SM00479. EXOIII. 1 hit.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEi PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein."
    Uchida N., Hoshino S., Katada T.
    J. Biol. Chem. 279:1383-1391(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH PAN3 AND POLYADENYLATE-BINDING PROTEIN, MUTAGENESIS OF ASP-1087, VARIANT LEU-179.
    Tissue: Cervix carcinoma.
  2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT LEU-179.
    Tissue: Brain.
  3. Ohara O., Suyama M., Nagase T., Ishikawa K.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  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] (ISOFORMS 1 AND 2), VARIANTS ASN-32 AND LEU-179.
    Tissue: Eye and Testis.
  5. "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases."
    Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S., Lopez-Otin C.
    Biochem. Biophys. Res. Commun. 314:54-62(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF UBIQUITIN CARBOXYL TERMINAL HYDROLASE ACTIVITY.
  6. "Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover."
    Yamashita A., Chang T.-C., Yamashita Y., Zhu W., Zhong Z., Chen C.-Y.A., Shyu A.-B.
    Nat. Struct. Mol. Biol. 12:1054-1063(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "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-1189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells."
    Zheng D., Ezzeddine N., Chen C.Y., Zhu W., He X., Shyu A.B.
    J. Cell Biol. 182:89-101(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structure of the PAN3 pseudokinase reveals the basis for interactions with the PAN2 deadenylase and the GW182 proteins."
    Christie M., Boland A., Huntzinger E., Weichenrieder O., Izaurralde E.
    Mol. Cell 51:360-373(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAN3.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-1201.

Entry informationi

Entry nameiPAN2_HUMAN
AccessioniPrimary (citable) accession number: Q504Q3
Secondary accession number(s): O75189, Q76E12, Q8IVE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3