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Q8IZH2 (XRN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
5'-3' exoribonuclease 1

EC=3.1.13.-
Alternative name(s):
Strand-exchange protein 1 homolog
Gene names
Name:XRN1
Synonyms:SEP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1706 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major 5'-3' exoribonuclease involved in mRNA decay. Required for the 5'-3'-processing of the G4 tetraplex-containing DNA and RNA substrates. The kinetic of hydrolysis is faster for G4 RNA tetraplex than for G4 DNA tetraplex and monomeric RNA tetraplex. Binds to RNA and DNA By similarity. Plays a role in replication-dependent histone mRNA degradation. May act as a tumor suppressor protein in osteogenic sarcoma (OGS). Ref.8 Ref.9

Subunit structure

Associates with alpha and beta tubulins By similarity. Found in a mRNP complex with UPF1, UPF2, UPF3B and XRN1. Interacts with ZC3HAV1 in an RNA-dependent manner. Interacts with DIS3L2. Ref.6 Ref.12 Ref.13

Subcellular location

Cytoplasm. Note: Discrete foci at the inner surface of the cell membrane. Ref.1 Ref.5 Ref.7

Tissue specificity

Expressed in heart, brain, pancreas, spleen, testis, osteogenic sarcoma (OGS) biopsy and primary cell lines. Ref.8

Induction

By GDNF/glial cell line-derived neurotrophic factor. Ref.1

Miscellaneous

Down-regulated in OGS biopsy.

Sequence similarities

Belongs to the 5'-3' exonuclease family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   LigandDNA-binding
RNA-binding
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

histone mRNA catabolic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear mRNA surveillance

Inferred from mutant phenotype PubMed 17545563. Source: UniProtKB

nuclear-transcribed mRNA catabolic process

Inferred from mutant phenotype PubMed 17545563. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

rRNA catabolic process

Inferred from mutant phenotype PubMed 20368444. Source: UniProtKB

   Cellular_componentcytoplasmic mRNA processing body

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

   Molecular_function5'-3' exonuclease activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IZH2-1)

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: Q8IZH2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1354-1354: M → MK
     1540-1552: Missing.
Isoform 3 (identifier: Q8IZH2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     449-459: DDFLADQAACY → EYVFANAFILK
     460-1706: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 170617065'-3' exoribonuclease 1
PRO_0000071392

Amino acid modifications

Modified residue13481Phosphoserine By similarity

Natural variations

Alternative sequence449 – 45911DDFLADQAACY → EYVFANAFILK in isoform 3.
VSP_016692
Alternative sequence460 – 17061247Missing in isoform 3.
VSP_016693
Alternative sequence13541M → MK in isoform 2.
VSP_016694
Alternative sequence1540 – 155213Missing in isoform 2.
VSP_016695
Natural variant6741S → G.
Corresponds to variant rs35214510 [ dbSNP | Ensembl ].
VAR_053000
Natural variant12591V → A.
Corresponds to variant rs35902661 [ dbSNP | Ensembl ].
VAR_053001

Experimental info

Sequence conflict481D → G in CAE45950. Ref.2
Sequence conflict551I → T in BAC04718. Ref.4
Sequence conflict1131K → E in CAH18332. Ref.2
Sequence conflict1421R → K in AAH48104. Ref.3
Sequence conflict1481K → E in CAH18332. Ref.2
Sequence conflict5721Missing in CAB63749. Ref.2
Sequence conflict7221L → I in CAE45950. Ref.2
Sequence conflict8341K → R in CAH18332. Ref.2
Sequence conflict12501Q → R in CAH18332. Ref.2
Sequence conflict14631L → F in CAE45950. Ref.2
Sequence conflict16861S → P in CAH18332. Ref.2

Sequences

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

Last modified March 1, 2003. Version 1.
Checksum: D06A76208DE78698

FASTA1,706194,107
        10         20         30         40         50         60 
MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD VHFRISDDKI 

        70         80         90        100        110        120 
FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKAIEKGE 

       130        140        150        160        170        180 
TLPTEARFDS NCITPGTEFM ARLHEHLKYF VNMKISTDKS WQGVTIYFSG HETPGEGEHK 

       190        200        210        220        230        240 
IMEFIRSEKA KPDHDPNTRH CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA 

       250        260        270        280        290        300 
PEETTFHLLH LSLMREYIDY EFSVLKEKIT FKYDIERIID DWILMGFLVG NDFIPHLPHL 

       310        320        330        340        350        360 
HINHDALPLL YGTYVTILPE LGGYINESGH LNLPRFEKYL VKLSDFDREH FSEVFVDLKW 

       370        380        390        400        410        420 
FESKVGNKYL NEAAGVAAEE ARNYKEKKKL KGQENSLCWT ALDKNEGEMI TSKDNLEDET 

       430        440        450        460        470        480 
EDDDLFETEF RQYKRTYYMT KMGVDVVSDD FLADQAACYV QAIQWILHYY YHGVQSWSWY 

       490        500        510        520        530        540 
YPYHYAPFLS DIHNISTLKI HFELGKPFKP FEQLLAVLPA ASKNLLPACY QHLMTNEDSP 

       550        560        570        580        590        600 
IIEYYPPDFK TDLNGKQQEW EAVVLIPFID EKRLLEAMET CNHSLKKEER KRNQHSECLM 

       610        620        630        640        650        660 
CWYDRDTEFI YPSPWPEKFP AIERCCTRYK IISLDAWRVD INKNKITRID QKALYFCGFP 

       670        680        690        700        710        720 
TLKHIRHKFF LKKSGVQVFQ QSSRGENMML EILVDAESDE LTVENVASSV LGKSVFVNWP 

       730        740        750        760        770        780 
HLEEARVVAV SDGETKFYLE EPPGTQKLYS GRTAPPSKVV HLGDKEQSNW AKEVQGISEH 

       790        800        810        820        830        840 
YLRRKGIIIN ETSAVVYAQL LTGRKYQINQ NGEVRLEKQW SKQVVPFVYQ TIVKDIRAFD 

       850        860        870        880        890        900 
SRFSNIKTLD DLFPLRSMVF MLGTPYYGCT GEVQDSGDVI TEGRIRVIFS IPCEPNLDAL 

       910        920        930        940        950        960 
IQNQHKYSIK YNPGYVLASR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK ANVGLNLKFN 

       970        980        990       1000       1010       1020 
KKNEEVPGYT KKVGSEWMYS SAAEQLLAEY LERAPELFSY IAKNSQEDVF YEDDIWPGEN 

      1030       1040       1050       1060       1070       1080 
ENGAEKVQEI ITWLKGHPVS TLSRSSCDLQ ILDAAIVEKI EEEVEKCKQR KNNKKVRVTV 

      1090       1100       1110       1120       1130       1140 
KPHLLYRPLE QQHGVIPDRD AEFCLFDRVV NVRENFSVPV GLRGTIIGIK GANREADVLF 

      1150       1160       1170       1180       1190       1200 
EVLFDEEFPG GLTIRCSPGR GYRLPTSALV NLSHGSRSET GNQKLTAIVK PQPAVHQHSS 

      1210       1220       1230       1240       1250       1260 
SSSVSSGHLG ALNHSPQSLF VPTQVPTKDD DEFCNIWQSL QGSGKMQYFQ PTIQEKGAVL 

      1270       1280       1290       1300       1310       1320 
PQEISQVNQH HKSGFNDNSV KYQQRKHDPH RKFKEECKSP KAECWSQKMS NKQPNSGIEN 

      1330       1340       1350       1360       1370       1380 
FLASLNISKE NEVQSSHHGE PPSEEHLSPQ SFAMGTRMLK EILKIDGSNT VDHKNEIKQI 

      1390       1400       1410       1420       1430       1440 
ANEIPVSSNR RDEYGLPSQP KQNKKLASYM NKPHSANEYH NVQSMDNMCW PAPSQIPPVS 

      1450       1460       1470       1480       1490       1500 
TPVTELSRIC SLVGMPQPDF SFLRMPQTMT VCQVKLSNGL LVHGPQCHSE NEAKEKAALF 

      1510       1520       1530       1540       1550       1560 
ALQQLGSLGM NFPLPSQVFA NYPSAVPPGT IPPAFPPPTG WDHYGSNYAL GAANIMPSSS 

      1570       1580       1590       1600       1610       1620 
HLFGSMPWGP SVPVPGKPFH HTLYSGTMPM AGGIPGGVHN QFIPLQVTKK RVANKKNFEN 

      1630       1640       1650       1660       1670       1680 
KEAQSSQATP VQTSQPDSSN IVKVSPRESS SASLKSSPIA QPASSFQVET ASQGHSISHH 

      1690       1700 
KSTPISSSRR KSRKLAVNFG VSKPSE 

« Hide

Isoform 2 [UniParc].

Checksum: 25AD7CD0191A4E05
Show »

FASTA1,694192,843
Isoform 3 [UniParc].

Checksum: 2C546FA5EDB81BC3
Show »

FASTA45953,818

References

« Hide 'large scale' references
[1]"Identification of human SEP1 as a glial cell line-derived neurotrophic factor-inducible protein and its expression in the nervous system."
Shimoyama Y., Morikawa Y., Ichihara M., Kodama Y., Fukuda N., Hayashi H., Morinaga T., Iwashita T., Murakumo Y., Takahashi M.
Neuroscience 121:899-906(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION BY GDNF, SUBCELLULAR LOCATION.
Tissue: Neuroblastoma.
[2]"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] (ISOFORMS 1 AND 2).
Tissue: Fetal kidney, Small intestine and Testis.
[3]"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 3).
Tissue: Brain and Testis.
[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] OF 1-473 (ISOFORMS 1/2).
Tissue: Mesangial cell.
[5]"Cloning and characterization of human Sep1 (hSEP1) gene and cytoplasmic localization of its product."
Sato Y., Shimamoto A., Shobuike T., Sugimoto M., Ikeda H., Kuroda S., Furuichi Y.
DNA Res. 5:241-246(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION.
[6]"Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities."
Lejeune F., Li X., Maquat L.E.
Mol. Cell 12:675-687(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF1; UPF2 AND UPF3B.
[7]"The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci."
Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.
RNA 8:1489-1501(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"The human homolog of yeast SEP1 is a novel candidate tumor suppressor gene in osteogenic sarcoma."
Zhang K., Dion N., Fuchs B., Damron T., Gitelis S., Irwin R., O'Connor M., Schwartz H., Scully S.P., Rock M.G., Bolander M.E., Sarkar G.
Gene 298:121-127(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL TUMOR SUPPRESSION ROLE IN OSTEOGENIC SARCOMA, TISSUE SPECIFICITY.
[9]"Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
Mullen T.E., Marzluff W.F.
Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
[10]"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.
[11]"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].
[12]"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZC3HAV1.
[13]"Exonuclease hDIS3L2 specifies an exosome-independent 3'-5' degradation pathway of human cytoplasmic mRNA."
Lubas M., Damgaard C.K., Tomecki R., Cysewski D., Jensen T.H., Dziembowski A.
EMBO J. 32:1855-1868(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DIS3L2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY137776 mRNA. Translation: AAN11306.1.
AL133623 mRNA. Translation: CAB63749.1.
BX640905 mRNA. Translation: CAE45950.1.
CR627396 mRNA. Translation: CAH10490.1.
CR749518 mRNA. Translation: CAH18332.1.
BC039314 mRNA. Translation: AAH39314.1.
BC048104 mRNA. Translation: AAH48104.1.
AK096177 mRNA. Translation: BAC04718.1.
PIRT43461.
RefSeqNP_001269786.1. NM_001282857.1.
NP_001269788.1. NM_001282859.1.
NP_061874.3. NM_019001.4.
UniGeneHs.435103.

3D structure databases

ProteinModelPortalQ8IZH2.
SMRQ8IZH2. Positions 1-600.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119970. 68 interactions.
DIPDIP-31174N.
IntActQ8IZH2. 25 interactions.
STRING9606.ENSP00000264951.

PTM databases

PhosphoSiteQ8IZH2.

Polymorphism databases

DMDM74714582.

Proteomic databases

PaxDbQ8IZH2.
PRIDEQ8IZH2.

Protocols and materials databases

DNASU54464.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264951; ENSP00000264951; ENSG00000114127. [Q8IZH2-1]
ENST00000392981; ENSP00000376707; ENSG00000114127. [Q8IZH2-2]
ENST00000463916; ENSP00000418404; ENSG00000114127. [Q8IZH2-3]
GeneID54464.
KEGGhsa:54464.
UCSCuc003eus.3. human. [Q8IZH2-1]
uc003euu.3. human. [Q8IZH2-2]
uc003euw.3. human. [Q8IZH2-3]

Organism-specific databases

CTD54464.
GeneCardsGC03M142025.
HGNCHGNC:30654. XRN1.
HPAHPA035005.
HPA035006.
MIM607994. gene.
neXtProtNX_Q8IZH2.
PharmGKBPA134878471.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5049.
HOVERGENHBG094164.
InParanoidQ8IZH2.
KOK12618.
OMACKQRKSN.
OrthoDBEOG7S7SCW.
PhylomeDBQ8IZH2.
TreeFamTF105757.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ8IZH2.
BgeeQ8IZH2.
CleanExHS_XRN1.
GenevestigatorQ8IZH2.

Family and domain databases

InterProIPR027073. 5_3_exoribonuclease.
IPR016494. 5_3_exoribonuclease_1.
IPR004859. Put_53exo.
[Graphical view]
PANTHERPTHR12341. PTHR12341. 1 hit.
PfamPF03159. XRN_N. 1 hit.
[Graphical view]
PIRSFPIRSF006743. Exonuclease_Xnr1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSXRN1. human.
GenomeRNAi54464.
NextBio56731.
PROQ8IZH2.
SOURCESearch...

Entry information

Entry nameXRN1_HUMAN
AccessionPrimary (citable) accession number: Q8IZH2
Secondary accession number(s): Q4G0S3 expand/collapse secondary AC list , Q68D88, Q6AI24, Q6MZS8, Q86WS7, Q8N8U4, Q9UF39
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 98 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

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 3

Human chromosome 3: entries, gene names and cross-references to MIM