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Q9P2R6 (RERE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Arginine-glutamic acid dipeptide repeats protein
Alternative name(s):
Atrophin-1-like protein
Atrophin-1-related protein
Gene names
Name:RERE
Synonyms:ARG, ARP, ATN1L, KIAA0458
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role as a transcriptional repressor during development. May play a role in the control of cell survival. Overexpression of RERE recruits BAX to the nucleus particularly to POD and triggers caspase-3 activation, leading to cell death. Ref.2

Subunit structure

Interacts with HDAC1 By similarity. Interacts with ATN1. Interaction with ATN1 is improved when the poly-Gln region of ATN1 is extended. Interacts with FAT1. Ref.1 Ref.9

Subcellular location

Nucleus. Note: Localized in nuclear bodies of variables size. Colocalized with PML and BAX in nuclear PODs. Ref.1 Ref.2

Tissue specificity

Widely expressed. Expressed in tumor cell lines. Ref.1 Ref.2 Ref.6

Domain

The interaction with ATN1 is mediated by the coiled coil domain.

Involvement in disease

A chromosomal aberration involving RERE is found in the neuroblastoma cell line NGP. Translocation t(1;15)(p36.2;q24).

Sequence similarities

Contains 1 BAH domain.

Contains 1 ELM2 domain.

Contains 1 GATA-type zinc finger.

Contains 1 SANT domain.

Sequence caution

The sequence AAC31120.1 differs from that shown. Reason: Frameshift at positions 588 and 596.

The sequence AAD27584.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATN1P542593EBI-948076,EBI-945980
EHMT2Q96KQ73EBI-948076,EBI-744366

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9P2R6-1)

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: Q9P2R6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-554: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15661566Arginine-glutamic acid dipeptide repeats protein
PRO_0000083504

Regions

Domain103 – 283181BAH
Domain284 – 387104ELM2
Domain391 – 44353SANT
Zinc finger507 – 53226GATA-type
Coiled coil1156 – 121156 Potential
Compositional bias738 – 1118381Pro-rich
Compositional bias1179 – 120426Arg/Glu-rich (mixed charge)
Compositional bias1300 – 132223Arg/Glu-rich (mixed charge)
Compositional bias1425 – 144521His-rich
Compositional bias1451 – 151060Pro-rich

Amino acid modifications

Modified residue531Phosphoserine Ref.8 Ref.12
Modified residue561Phosphoserine Ref.8 Ref.12
Modified residue3041Phosphoserine Ref.7
Modified residue6421Phosphoserine Ref.8 Ref.11 Ref.12
Modified residue6561Phosphoserine Ref.12
Modified residue6751Phosphoserine Ref.10 Ref.12
Modified residue6791Phosphoserine Ref.10 Ref.12
Modified residue11061Phosphoserine Ref.7 Ref.12
Modified residue11581N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 554554Missing in isoform 2.
VSP_016878

Experimental info

Sequence conflict651S → G in BAA95898. Ref.1
Sequence conflict681A → T in BAA95898. Ref.1
Sequence conflict114 – 1152ES → VC in BAA95898. Ref.1
Sequence conflict6431P → L in AAC31120. Ref.3
Sequence conflict9211A → G in BAA95898. Ref.1
Sequence conflict9401P → A in BAA95898. Ref.1
Sequence conflict9571F → L in AAD27584. Ref.6
Sequence conflict9771T → K no nucleotide entry Ref.2
Sequence conflict9841H → N no nucleotide entry Ref.2
Sequence conflict1009 – 10113QSQ → RTR in AAD27584. Ref.6
Sequence conflict11171E → D in AAD27584. Ref.6
Sequence conflict12721H → Q in AAD27584. Ref.6
Sequence conflict1489 – 14902ML → IV in BAA95898. Ref.1
Sequence conflict15291R → K in AAD27584. Ref.6
Sequence conflict15361W → C in AAD27584. Ref.6
Sequence conflict15431M → R in AAD27584. Ref.6

Secondary structure

....... 1566
Helix Strand Turn

Details...

Sequences

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

Last modified January 10, 2006. Version 2.
Checksum: ECA4A22026E3E96F

FASTA1,566172,424
        10         20         30         40         50         60 
MTADKDKDKD KEKDRDRDRD REREKRDKAR ESENSRPRRS CTLEGGAKNY AESDHSEDED 

        70         80         90        100        110        120 
NDNNSATAEE STKKNKKKPP KKKSRYERTD TGEITSYITE DDVVYRPGDC VYIESRRPNT 

       130        140        150        160        170        180 
PYFICSIQDF KLVHNSQACC RSPTPALCDP PACSLPVASQ PPQHLSEAGR GPVGSKRDHL 

       190        200        210        220        230        240 
LMNVKWYYRQ SEVPDSVYQH LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA 

       250        260        270        280        290        300 
LRGKCNISHF SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ 

       310        320        330        340        350        360 
PFPSPDGDTV TQHEELVWMP GVNDCDLLMY LRAARSMAAF AGMCDGGSTE DGCVAASRDD 

       370        380        390        400        410        420 
TTLNALNTLH ESGYDAGKAL QRLVKKPVPK LIEKCWTEDE VKRFVKGLRQ YGKNFFRIRK 

       430        440        450        460        470        480 
ELLPNKETGE LITFYYYWKK TPEAASSRAH RRHRRQAVFR RIKTRTASTP VNTPSRPPSS 

       490        500        510        520        530        540 
EFLDLSSASE DDFDSEDSEQ ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG 

       550        560        570        580        590        600 
ELPPIEKPVD PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPASPDGRTS 

       610        620        630        640        650        660 
PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA SSPLKSNKRQ REKVASDTEE 

       670        680        690        700        710        720 
ADRTSSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD PKDIDQDNRS TSPSIPSPQD 

       730        740        750        760        770        780 
NESDSDSSAQ QQMLQAQPPA LQAPTGVTPA PSSAPPGTPQ LPTPGPTPSA TAVPPQGSPT 

       790        800        810        820        830        840 
ASQAPNQPQA PTAPVPHTHI QQAPALHPQR PPSPHPPPHP SPHPPLQPLT GSAGQPSAPS 

       850        860        870        880        890        900 
HAQPPLHGQG PPGPHSLQAG PLLQHPGPPQ PFGLPPQASQ GQAPLGTSPA AAYPHTSLQL 

       910        920        930        940        950        960 
PASQSALQSQ QPPREQPLPP APLAMPHIKP PPTTPIPQLP APQAHKHPPH LSGPSPFSMN 

       970        980        990       1000       1010       1020 
ANLPPPPALK PLSSLSTHHP PSAHPPPLQL MPQSQPLPSS PAQPPGLTQS QNLPPPPASH 

      1030       1040       1050       1060       1070       1080 
PPTGLHQVAP QPPFAQHPFV PGGPPPITPP TCPSTSTPPA GPGTSAQPPC SGAAASGGSI 

      1090       1100       1110       1120       1130       1140 
AGGSSCPLPT VQIKEEALDD AEEPESPPPP PRSPSPEPTV VDTPSHASQS ARFYKHLDRG 

      1150       1160       1170       1180       1190       1200 
YNSCARTDLY FMPLAGSKLA KKREEAIEKA KREAEQKARE EREREKEKEK ERERERERER 

      1210       1220       1230       1240       1250       1260 
EAERAAKASS SAHEGRLSDP QLSGPGHMRP SFEPPPTTIA AVPPYIGPDT PALRTLSEYA 

      1270       1280       1290       1300       1310       1320 
RPHVMSPTNR NHPFYMPLNP TDPLLAYHMP GLYNVDPTIR ERELREREIR EREIRERELR 

      1330       1340       1350       1360       1370       1380 
ERMKPGFEVK PPELDPLHPA ANPMEHFARH SALTIPPTAG PHPFASFHPG LNPLERERLA 

      1390       1400       1410       1420       1430       1440 
LAGPQLRPEM SYPDRLAAER IHAERMASLT SDPLARLQMF NVTPHHHQHS HIHSHLHLHQ 

      1450       1460       1470       1480       1490       1500 
QDPLHQGSAG PVHPLVDPLT AGPHLARFPY PPGTLPNPLL GQPPHEHEML RHPVFGTPYP 

      1510       1520       1530       1540       1550       1560 
RDLPGAIPPP MSAAHQLQAM HAQSAELQRL AMEQQWLHGH PHMHGGHLPS QEDYYSRLKK 


EGDKQL 

« Hide

Isoform 2 [UniParc].

Checksum: 54B60DCBF0FB85FE
Show »

FASTA1,012109,048

References

« Hide 'large scale' references
[1]"Protein binding of a DRPLA family through arginine-glutamic acid dipeptide repeats is enhanced by extended polyglutamine."
Yanagisawa H., Bundo M., Miyashita T., Okamura-Oho Y., Tadokoro K., Tokunaga K., Yamada M.
Hum. Mol. Genet. 9:1433-1442(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ATN1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Human RERE is localized to nuclear promyelocytic leukemia oncogenic domains and enhances apoptosis."
Waerner T., Gardellin P., Pfizenmaier K., Weith A., Kraut N.
Cell Growth Differ. 12:201-210(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[3]"Cloning and localization of human atrophin-1 (DRPLA) related gene."
Xia J.-H., Liu C.-Y., Ruan Q.-G., Wang D.-A., Deng H.-X.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1566 (ISOFORM 1).
Tissue: Brain.
[6]"Identification and characterization of novel genes located at the t(1;15)(p36.2;q24) translocation breakpoint in the neuroblastoma cell line NGP."
Amler L.C., Bauer A., Corvi R., Dihlmann S., Praml C., Cavenee W.K., Schwab M., Hampton G.M.
Genomics 64:195-202(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 555-1566, TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION.
[7]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-1106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-53; SER-56 AND SER-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Atrophin proteins interact with the Fat1 cadherin and regulate migration and orientation in vascular smooth muscle cells."
Hou R., Sibinga N.E.
J. Biol. Chem. 284:6955-6965(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FAT1.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND SER-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-53; SER-56; SER-642; SER-656; SER-675; SER-679 AND SER-1106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Solution structure of the SANT domain in arginine-glutamic acid dipeptide (RE) repeats."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 392-446.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB036737 mRNA. Translation: BAA95898.1.
AF016005 mRNA. Translation: AAC31120.1. Frameshift.
AF041104 expand/collapse EMBL AC list , AF041096, AF041097, AF041098, AF041099, AF041100, AF041101, AF041102, AF041103 Genomic DNA. Translation: AAC28264.1.
AL356072, AL096855, AL357713 Genomic DNA. Translation: CAH70516.1.
AL357713, AL096855, AL356072 Genomic DNA. Translation: CAH73433.1.
AL096855, AL356072, AL357713 Genomic DNA. Translation: CAI19208.1.
AB007927 mRNA. Translation: BAA32303.3.
AF118275 mRNA. Translation: AAD27584.1. Different initiation.
RefSeqNP_001036146.1. NM_001042681.1.
NP_001036147.1. NM_001042682.1.
NP_036234.3. NM_012102.3.
XP_005263521.1. XM_005263464.1.
UniGeneHs.463041.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YQKNMR-A392-441[»]
ProteinModelPortalQ9P2R6.
SMRQ9P2R6. Positions 284-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106963. 25 interactions.
IntActQ9P2R6. 22 interactions.
MINTMINT-2820762.
STRING9606.ENSP00000338629.

PTM databases

PhosphoSiteQ9P2R6.

Polymorphism databases

DMDM85540730.

Proteomic databases

PaxDbQ9P2R6.
PRIDEQ9P2R6.

Protocols and materials databases

DNASU473.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337907; ENSP00000338629; ENSG00000142599. [Q9P2R6-1]
ENST00000400908; ENSP00000383700; ENSG00000142599. [Q9P2R6-1]
ENST00000476556; ENSP00000422246; ENSG00000142599. [Q9P2R6-2]
GeneID473.
KEGGhsa:473.
UCSCuc001apd.3. human. [Q9P2R6-1]

Organism-specific databases

CTD473.
GeneCardsGC01M008412.
HGNCHGNC:9965. RERE.
HPAHPA024093.
MIM605226. gene.
neXtProtNX_Q9P2R6.
PharmGKBPA34332.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331121.
HOGENOMHOG000231091.
HOVERGENHBG079774.
InParanoidQ9P2R6.
KOK05628.
OMAHHPPSAH.
OrthoDBEOG7D59MN.
PhylomeDBQ9P2R6.
TreeFamTF328554.

Gene expression databases

ArrayExpressQ9P2R6.
BgeeQ9P2R6.
CleanExHS_RERE.
GenevestigatorQ9P2R6.

Family and domain databases

InterProIPR002951. Atrophin-like.
IPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]
PfamPF03154. Atrophin-1. 1 hit.
PF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view]
SMARTSM00439. BAH. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRERE. human.
EvolutionaryTraceQ9P2R6.
GeneWikiRERE.
GenomeRNAi473.
NextBio1955.
PROQ9P2R6.
SOURCESearch...

Entry information

Entry nameRERE_HUMAN
AccessionPrimary (citable) accession number: Q9P2R6
Secondary accession number(s): O43393 expand/collapse secondary AC list , O75046, O75359, Q5VXL9, Q6P6B9, Q9Y2W4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: April 16, 2014
This is version 126 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM