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P56645 (PER3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Period circadian protein homolog 3

Short name=hPER3
Alternative name(s):
Cell growth-inhibiting gene 13 protein
Circadian clock protein PERIOD 3
Gene names
Name:PER3
ORF Names:GIG13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1201 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Originally described as a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. Has a redundant role with the other PER proteins PER1 and PER2 and is not essential for the circadian rhythms maintenance. In contrast, plays an important role in sleep-wake timing and sleep homeostasis probably through the transcriptional regulation of sleep homeostasis-related genes, without influencing circadian parameters. Can bind heme. Ref.6 Ref.7 Ref.9 Ref.10

Subunit structure

Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly with PER1, PER2, CRY1, CRY2, and TIMELESS; interaction with CRY1 and CRY2 is weak and not rhythmic. Interacts with FBXW11 and BTRC. Ref.5

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Mainly cytoplasmic. Translocates to the nucleus through binding PER1, PER2, CRY1 or CRY2, but not TIMELESS By similarity.

Post-translational modification

Phosphorylation by CSNK1E is weak and appears to require association with PER1 and translocation to the nucleus By similarity.

Ubiquitinated By similarity.

Polymorphism

The number of repeats of 18 amino acids in positions 966 to 1055 is polymorphic and varies among at least 2 different alleles. Alleles corresponding in size to a 4 (PER3.4) and 5 (PER3.5) repeats have been described. The sequence shown is that of allele PER3.5. In most populations around 10% of individuals are homozygous for the 5-repeat (PER3.5), whereas approximately 50% are homozygous for the 4-repeat (PER3.4). In some populations in Papua New Guinea the prevalence of the various genotypes appears to be reversed. These repeats and polymorphism are not present in non-primate mammals. Homozygosity for PER3.5 is more likely to show morning preference, whereas homozygosity for the PER3.4 associates with evening preferences. PER3.5 homozygous show vulnerability to sleep loss with a greater cognitive decline in response to total sleep deprivation (Ref.1, Ref.6, Ref.7, Ref.9, Ref.10).

Sequence similarities

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Sequence caution

The sequence BAB32925.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CHEK2O960172EBI-2827813,EBI-1180783

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P56645-1)

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: P56645-2)

The sequence of this isoform differs from the canonical sequence as follows:
     197-197: R → RA
     499-499: G → GGESANGG
     954-954: Y → YQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12011201Period circadian protein homolog 3
PRO_0000162633

Regions

Domain121 – 18868PAS 1
Domain262 – 32867PAS 2
Domain337 – 38044PAC
Region555 – 760206CSNK1E binding domain By similarity
Region1123 – 120179CRY binding domain By similarity
Motif55 – 6410Nuclear export signal 1 By similarity
Motif403 – 41210Nuclear export signal 3 By similarity
Motif729 – 74517Nuclear localization signal By similarity
Motif925 – 9328Nuclear export signal 2 By similarity
Compositional bias567 – 5704Poly-Ser
Compositional bias750 – 7534Poly-Ser
Compositional bias769 – 895127Pro-rich
Compositional bias962 – 1081120Ser-rich

Natural variations

Alternative sequence1971R → RA in isoform 2.
VSP_040326
Alternative sequence4991G → GGESANGG in isoform 2.
VSP_040327
Alternative sequence9541Y → YQ in isoform 2.
VSP_040328
Natural variant6391V → G Associated with delayed sleep phase syndrome (DSPS). Ref.1 Ref.12
Corresponds to variant rs10462020 [ dbSNP | Ensembl ].
VAR_025532
Natural variant8271L → P. Ref.1
Corresponds to variant rs228696 [ dbSNP | Ensembl ].
VAR_022428
Natural variant8561P → A. Ref.1
Corresponds to variant rs228697 [ dbSNP | Ensembl ].
VAR_015514
Natural variant1002 – 101918Missing.
VAR_071049
Natural variant10071A → T.
Corresponds to variant rs1776342 [ dbSNP | Ensembl ].
VAR_028728
Natural variant10101T → I.
Corresponds to variant rs12033719 [ dbSNP | Ensembl ].
VAR_028729
Natural variant10281M → T Only found in PER3.4 allele. Ref.1
Corresponds to variant rs2640909 [ dbSNP | Ensembl ].
VAR_025533
Natural variant10811S → C.
Corresponds to variant rs2640905 [ dbSNP | Ensembl ].
VAR_028730
Natural variant11491H → R. Ref.1
Corresponds to variant rs10462021 [ dbSNP | Ensembl ].
VAR_025534

Experimental info

Sequence conflict9431Q → R in BAB32925. Ref.1

Sequences

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

Last modified January 11, 2011. Version 4.
Checksum: 8129C4246EDD1816

FASTA1,201131,888
        10         20         30         40         50         60 
MPRGEAPGPG RRGAKDEALG EESGERWSPE FHLQRKLADS SHSEQQDRNR VSEELIMVVQ 

        70         80         90        100        110        120 
EMKKYFPSER RNKPSTLDAL NYALRCVHSV QANSEFFQIL SQNGAPQADV SMYSLEELAT 

       130        140        150        160        170        180 
IASEHTSKNT DTFVAVFSFL SGRLVHISEQ AALILNRKKD VLASSHFVDL LAPQDMRVFY 

       190        200        210        220        230        240 
AHTARAQLPF WNNWTQRAAR YECAPVKPFF CRIRGGEDRK QEKCHSPFRI IPYLIHVHHP 

       250        260        270        280        290        300 
AQPELESEPC CLTVVEKIHS GYEAPRIPVN KRIFTTTHTP GCVFLEVDEK AVPLLGYLPQ 

       310        320        330        340        350        360 
DLIGTSILSY LHPEDRSLMV AIHQKVLKYA GHPPFEHSPI RFCTQNGDYI ILDSSWSSFV 

       370        380        390        400        410        420 
NPWSRKISFI IGRHKVRTSP LNEDVFATKI KKMNDNDKDI TELQEQIYKL LLQPVHVSVS 

       430        440        450        460        470        480 
SGYGSLGSSG SQEQLVSIAS SSEASGHRVE ETKAEQMTLQ QVYASVNKIK NLGQQLYIES 

       490        500        510        520        530        540 
MTKSSFKPVT GTRTEPNGGG ECKTFTSFHQ TLKNNSVYTE PCEDLRNDEH SPSYQQINCI 

       550        560        570        580        590        600 
DSVIRYLKSY NIPALKRKCI SCTNTTSSSS EEDKQNHKAD DVQALQAGLQ IPAIPKSEMP 

       610        620        630        640        650        660 
TNGRSIDTGG GAPQILSTAM LSLGSGISQC GYSSTIVHVP PPETARDATL FCEPWTLNMQ 

       670        680        690        700        710        720 
PAPLTSEEFK HVGLTAAVLS AHTQKEEQNY VDKFREKILS SPYSSYLQQE SRSKAKYSYF 

       730        740        750        760        770        780 
QGDSTSKQTR SAGCRKGKHK RKKLPEPPDS SSSNTGSGPR RGAHQNAQPC CPSAASSPHT 

       790        800        810        820        830        840 
SSPTFPPAAM VPSQAPYLVP AFPLPAATSP GREYAAPGTA PEGLHGLPLS EGLQPYPAFP 

       850        860        870        880        890        900 
FPYLDTFMTV FLPDPPVCPL LSPSFLPCPF LGATASSAIS PSMSSAMSPT LDPPPSVTSQ 

       910        920        930        940        950        960 
RREEEKWEAQ SEGHPFITSR SSSPLQLNLL QEEMPRPSES PDQMRRNTCP QTEYCVTGNN 

       970        980        990       1000       1010       1020 
GSESSPATTG ALSTGSPPRE NPSHPTASAL STGSPPMKNP SHPTASALST GSPPMKNPSH 

      1030       1040       1050       1060       1070       1080 
PTASTLSMGL PPSRTPSHPT ATVLSTGSPP SESPSRTGSA ASGSSDSSIY LTSSVYSSKI 

      1090       1100       1110       1120       1130       1140 
SQNGQQSQDV QKKETFPNVA EEPIWRMIRQ TPERILMTYQ VPERVKEVVL KEDLEKLESM 

      1150       1160       1170       1180       1190       1200 
RQQQPQFSHG QKEELAKVYN WIQSQTVTQE IDIQACVTCE NEDSADGAAT SCGQVLVEDS 


C 

« Hide

Isoform 2 [UniParc].

Checksum: D63BD326292813F6
Show »

FASTA1,210132,660

References

« Hide 'large scale' references
[1]"Association of structural polymorphisms in the human period3 gene with delayed sleep phase syndrome."
Ebisawa T., Uchiyama M., Kajimura N., Mishima K., Kamei Y., Katoh M., Watanabe T., Sekimoto M., Shibui K., Kim K., Kudo Y., Ozeki Y., Sugishita M., Toyoshima R., Inoue Y., Yamada N., Nagase T., Ozaki N. expand/collapse author list , Ohara O., Ishida N., Okawa M., Takahashi K., Yamauchi T.
EMBO Rep. 2:342-346(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-91 AND 724-882 (ISOFORMS 1/2), POLYMORPHISM, VARIANTS GLY-639; PRO-827; ALA-856; 1002-HIS--SER-1019 DEL; THR-1028 AND ARG-1149.
[2]Rhodes S., Huckle E.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Identification of a growth inhibition gene."
Kim J.W.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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]"SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein."
Shirogane T., Jin J., Ang X.L., Harper J.W.
J. Biol. Chem. 280:26863-26872(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBXW11 AND BTRC.
[6]"PER3 polymorphism predicts sleep structure and waking performance."
Viola A.U., Archer S.N., James L.M., Groeger J.A., Lo J.C., Skene D.J., von Schantz M., Dijk D.J.
Curr. Biol. 17:613-618(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SLEEP HOMEOSTASIS, CHARACTERIZATION OF POLYMORPHISM.
[7]"PERIOD3, circadian phenotypes, and sleep homeostasis."
Dijk D.J., Archer S.N.
Sleep Med. Rev. 14:151-160(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SLEEP HOMEOSTASIS, CHARACTERIZATION OF POLYMORPHISM, REVIEW.
[8]"Metabolism and the circadian clock converge."
Eckel-Mahan K., Sassone-Corsi P.
Physiol. Rev. 93:107-135(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[9]"Sleep ability mediates individual differences in the vulnerability to sleep loss: evidence from a PER3 polymorphism."
Maire M., Reichert C.F., Gabel V., Viola A.U., Strobel W., Krebs J., Landolt H.P., Bachmann V., Cajochen C., Schmidt C.
Cortex 52:47-59(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SLEEP HOMEOSTASIS, CHARACTERIZATION OF POLYMORPHISM.
[10]"A human sleep homeostasis phenotype in mice expressing a primate-specific PER3 variable-number tandem-repeat coding-region polymorphism."
Hasan S., van der Veen D.R., Winsky-Sommerer R., Hogben A., Laing E.E., Koentgen F., Dijk D.J., Archer S.N.
FASEB J. 28:1-14(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SLEEP HOMEOSTASIS, CHARACTERIZATION OF POLYMORPHISM.
[11]"Molecular architecture of the mammalian circadian clock."
Partch C.L., Green C.B., Takahashi J.S.
Trends Cell Biol. 24:90-99(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Circadian clock-related polymorphisms in seasonal affective disorder and their relevance to diurnal preference."
Johansson C., Willeit M., Smedh C., Ekholm J., Paunio T., Kieseppa T., Lichtermann D., Praschak-Rieder N., Neumeister A., Nilsson L.G., Kasper S., Peltonen L., Adolfsson R., Schalling M., Partonen T.
Neuropsychopharmacology 28:734-739(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLY-639.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB047521 Genomic DNA. Translation: BAB63250.1.
AB047530 Genomic DNA. Translation: BAB63251.1.
AB047531 Genomic DNA. Translation: BAB63252.1.
AB047532 Genomic DNA. Translation: BAB63253.1.
AB047533 Genomic DNA. Translation: BAB63254.1.
AB047534 Genomic DNA. Translation: BAB63255.1.
AB047686 mRNA. Translation: BAB32925.2. Different initiation.
AL157954 mRNA. Translation: CAB76084.1.
AY493418 mRNA. Translation: AAS72879.1.
Z98884 Genomic DNA. Translation: CAI21435.1.
Z98884 Genomic DNA. Translation: CAI21436.1.
CCDSCCDS89.1. [P56645-1]
RefSeqNP_001276790.1. NM_001289861.1.
NP_001276791.1. NM_001289862.1. [P56645-2]
NP_001276792.1. NM_001289863.1.
NP_001276793.1. NM_001289864.1.
NP_058515.1. NM_016831.2. [P56645-1]
UniGeneHs.162200.

3D structure databases

ProteinModelPortalP56645.
SMRP56645. Positions 36-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114386. 7 interactions.
IntActP56645. 4 interactions.
MINTMINT-8052823.
STRING9606.ENSP00000355031.

PTM databases

PhosphoSiteP56645.

Polymorphism databases

DMDM317373535.

Proteomic databases

MaxQBP56645.
PaxDbP56645.
PRIDEP56645.

Protocols and materials databases

DNASU8863.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361923; ENSP00000355031; ENSG00000049246. [P56645-1]
ENST00000377532; ENSP00000366755; ENSG00000049246. [P56645-2]
GeneID8863.
KEGGhsa:8863.
UCSCuc001aoo.3. human. [P56645-1]
uc001aop.3. human. [P56645-2]

Organism-specific databases

CTD8863.
GeneCardsGC01P007844.
HGNCHGNC:8847. PER3.
HPAHPA019530.
MIM603427. gene.
neXtProtNX_P56645.
PharmGKBPA33186.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269786.
HOVERGENHBG008167.
KOK02633.
OMAFKHVGLT.
OrthoDBEOG7S7SD0.
PhylomeDBP56645.
TreeFamTF318445.

Gene expression databases

ArrayExpressP56645.
BgeeP56645.
CleanExHS_PER3.
GenevestigatorP56645.

Family and domain databases

InterProIPR001610. PAC.
IPR000014. PAS.
IPR015524. Per_circ_prot_3.
IPR022728. Period_circadian-like_C.
[Graphical view]
PANTHERPTHR11269:SF13. PTHR11269:SF13. 1 hit.
PfamPF12114. Period_C. 1 hit.
[Graphical view]
SMARTSM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF55785. SSF55785. 1 hit.
PROSITEPS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPER3. human.
GeneWikiPER3.
GenomeRNAi8863.
NextBio33281.
PROP56645.
SOURCESearch...

Entry information

Entry namePER3_HUMAN
AccessionPrimary (citable) accession number: P56645
Secondary accession number(s): Q5H8X4 expand/collapse secondary AC list , Q5H8X5, Q969K6, Q96S77, Q96S78, Q9C0J3, Q9NSP9, Q9UGU8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 130 of the entry and version 4 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 1

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