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O60216 (RAD21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Double-strand-break repair protein rad21 homolog

Short name=hHR21
Alternative name(s):
Nuclear matrix protein 1
Short name=NXP-1
SCC1 homolog
Gene names
Name:RAD21
Synonyms:HR21, KIAA0078, NXP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length631 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Also plays a role in apoptosis, via its cleavage by caspase-3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C-terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway. Ref.9 Ref.12

Subunit structure

Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. Found in a complex with SMC1A, SMC3, CDCA5, PDS5A/APRIN and PDS5B/SCC-112. Interacts with PDS5B and WAPAL; the interaction is direct. Ref.8 Ref.13 Ref.16

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, it is cleaved by separase/ESPL1, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. Once cleaved by caspase-3, the C-terminal 64 kDa cleavage product translocates to the cytoplasm, where it may trigger apoptosis. Ref.2 Ref.10

Domain

The C-terminal part associates with the head of SMC1A, while the N-terminal part binds to the head of SMC3 By similarity.

Post-translational modification

Cleaved by separase/ESPL1 at the onset of anaphase. Cleaved by caspase-3 and caspase-7 at the beginning of apoptosis. The cleavage by ESPL1 and caspase-3 take place at different sites.

Phosphorylated; becomes hyperphosphorylated in M phase of cell cycle. The large dissociation of cohesin from chromosome arms during prophase may be partly due to its phosphorylation by PLK. Ref.10

Polymorphism

Some radiosensitive cancer patients seem to have Arg-481 instead of the conserved Gly-481. It may be that this mutation could contribute to radiosensitivity.

Involvement in disease

Cornelia de Lange syndrome 4 (CDLS4) [MIM:614701]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. It is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Sequence similarities

Belongs to the rad21 family.

Sequence caution

The sequence BAA07554.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Cell division
Chromosome partition
DNA damage
DNA repair
Mitosis
   Cellular componentCentromere
Chromosome
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Mental retardation
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Traceable author statement Ref.1. Source: ProtInc

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

double-strand break repair

Traceable author statement Ref.1. Source: ProtInc

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

protein localization to chromatin

Inferred from mutant phenotype PubMed 21111234. Source: UniProtKB

reciprocal meiotic recombination

Traceable author statement Ref.1. Source: ProtInc

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19468298. Source: BHF-UCL

   Cellular_componentchromosome

Traceable author statement. Source: Reactome

chromosome, centromeric region

Traceable author statement. Source: Reactome

cohesin complex

Traceable author statement PubMed 19468298. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

nuclear meiotic cohesin complex

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 631631Double-strand-break repair protein rad21 homolog
PRO_0000097872

Regions

Region287 – 403117Interaction with WAPAL and PDS5B
Region362 – 40342Interaction with STAG1
Compositional bias469 – 51042Pro-rich

Sites

Site172 – 1732Cleavage; by ESPL1
Site279 – 2802Cleavage; by caspase-3 or caspase-7
Site450 – 4512Cleavage; by ESPL1

Amino acid modifications

Modified residue461Phosphoserine Ref.15 Ref.18
Modified residue1531Phosphoserine Ref.17 Ref.18
Modified residue1751Phosphoserine Ref.15 Ref.17

Natural variations

Natural variant3761P → R in CDLS4. Ref.21
VAR_068691
Natural variant4811G → R. Ref.20
VAR_014281
Natural variant5851C → R in CDLS4. Ref.21
VAR_068692

Experimental info

Mutagenesis1721R → A: Abolishes first cleavage by ESPL1. Ref.11
Mutagenesis2791D → A: Abolishes cleavage by caspase-3. Ref.9 Ref.12
Mutagenesis4501R → A: Abolishes second cleavage by ESPL1. Ref.11
Sequence conflict1361N → I in CAA66940. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O60216 [UniParc].

Last modified November 15, 2002. Version 2.
Checksum: 7D4A6EA6392BE73D

FASTA63171,690
        10         20         30         40         50         60 
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK MALRTSGHLL 

        70         80         90        100        110        120 
LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEEN REAAYNAITL PEEFHDFDQP 

       130        140        150        160        170        180 
LPDLDDIDVA QQFSLNQSRV EEITMREEVG NISILQENDF GDFGMDDREI MREGSAFEDD 

       190        200        210        220        230        240 
DMLVSTTTSN LLLESEQSTS NLNEKINHLE YEDQYKDDNF GEGNDGGILD DKLISNNDGG 

       250        260        270        280        290        300 
IFDDPPALSE AGVMLPEQPA HDDMDEDDNV SMGGPDSPDS VDPVEPMPTM TDQTTLVPNE 

       310        320        330        340        350        360 
EEAFALEPID ITVKETKAKR KRKLIVDSVK ELDSKTIRAQ LSDYSDIVTT LDLAPPTKKL 

       370        380        390        400        410        420 
MMWKETGGVE KLFSLPAQPL WNNRLLKLFT RCLTPLVPED LRKRRKGGEA DNLDEFLKEF 

       430        440        450        460        470        480 
ENPEVPREDQ QQQHQQRDVI DEPIIEEPSR LQESVMEASR TNIDESAMPP PPPQGVKRKA 

       490        500        510        520        530        540 
GQIDPEPVMP PQQVEQMEIP PVELPPEEPP NICQLIPELE LLPEKEKEKE KEKEDDEEEE 

       550        560        570        580        590        600 
DEDASGGDQD QEERRWNKRT QQMLHGLQRA LAKTGAESIS LLELCRNTNR KQAAAKFYSF 

       610        620        630 
LVLKKQQAIE LTQEEPYSDI IATPGPRFHI I 

« Hide

References

« Hide 'large scale' references
[1]"Sequence conservation of the rad21 Schizosaccharomyces pombe DNA double-strand break repair gene in human and mouse."
McKay M.J., Troelstra C., van der Spek P., Kanaar R., Smit B., Hagemeijer A., Bootsma D., Hoeijmakers J.H.J.
Genomics 36:305-315(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"NXP-1, a human protein related to Rad21/Scc1/Mcd1, is a component of the nuclear matrix."
Sadano H., Sugimoto H., Sakai F., Nomura N., Osumi T.
Biochem. Biophys. Res. Commun. 267:418-422(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[3]"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[4]NIEHS SNPs program
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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].
Tissue: Cerebellum.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Testis.
[8]"A potential role for human cohesin in mitotic spindle aster assembly."
Gregson H.C., Schmiesing J.A., Kim J.-S., Kobayashi T., Zhou S., Yokomori K.
J. Biol. Chem. 276:47575-47582(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 406-418, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A; SMC3; STAG1 OR STAG2.
[9]"Linking sister chromatid cohesion and apoptosis: role of rad21."
Pati D., Zhang N., Plon S.E.
Mol. Cell. Biol. 22:8267-8277(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 275-279 (60 KDA PRODUCT), PROTEIN SEQUENCE OF 280-286 (64 KDA C-TERMINAL PRODUCT), CLEAVAGE BY CASPASE-3, FUNCTION, MUTAGENESIS OF ASP-279.
[10]"Human chromatid cohesin component hRad21 is phosphorylated in M phase and associated with metaphase centromeres."
Hoque M.T., Ishikawa F.
J. Biol. Chem. 276:5059-5067(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
[11]"Cohesin cleavage by separase required for anaphase and cytokinesis in human cells."
Hauf S., Waizenegger I.C., Peters J.-M.
Science 293:1320-1323(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY ESPL1, MUTAGENESIS OF ARG-172 AND ARG-450.
[12]"Caspase proteolysis of the cohesin component RAD21 promotes apoptosis."
Chen F., Kamradt M., Mulcahy M., Byun Y., Xu H., McKay M.J., Cryns V.L.
J. Biol. Chem. 277:16775-16781(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CLEAVAGE BY CASPASE-3, MUTAGENESIS OF ASP-279.
[13]"Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates."
Rankin S., Ayad N.G., Kirschner M.W.
Mol. Cell 18:185-200(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH SMC1A; SMC3; CDCA5; PDS5A AND PDS5B.
[14]Erratum
Rankin S., Ayad N.G., Kirschner M.W.
Mol. Cell 18:609-609(2005)
[15]"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-46 AND SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Releasing cohesin from chromosome arms in early mitosis: opposing actions of Wapl-Pds5 and Sgo1."
Shintomi K., Hirano T.
Genes Dev. 23:2224-2236(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDS5B; STAG1 AND WAPAL.
[17]"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-153 AND SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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-46 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"Novel DNA sequence variants in the hHR21 DNA repair gene in radiosensitive cancer patients."
Severin D.M., Leong T., Cassidy B., Elsaleh H., Peters L., Venter D., Southey M., McKay M.
Int. J. Radiat. Oncol. Biol. Phys. 50:1323-1331(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-481.
[21]"RAD21 mutations cause a human cohesinopathy."
Deardorff M.A., Wilde J.J., Albrecht M., Dickinson E., Tennstedt S., Braunholz D., Monnich M., Yan Y., Xu W., Gil-Rodriguez M.C., Clark D., Hakonarson H., Halbach S., Michelis L.D., Rampuria A., Rossier E., Spranger S., Van Maldergem L. expand/collapse author list , Lynch S.A., Gillessen-Kaesbach G., Ludecke H.J., Ramsay R.G., McKay M.J., Krantz I.D., Xu H., Horsfield J.A., Kaiser F.J.
Am. J. Hum. Genet. 90:1014-1027(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDLS4 ARG-376 AND ARG-585.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98294 mRNA. Translation: CAA66940.1.
D38551 mRNA. Translation: BAA07554.2. Different initiation.
AY675320 Genomic DNA. Translation: AAT70725.1.
AK289505 mRNA. Translation: BAF82194.1.
CH471060 Genomic DNA. Translation: EAW91963.1.
BC050381 mRNA. Translation: AAH50381.1.
RefSeqNP_006256.1. NM_006265.2.
UniGeneHs.81848.

3D structure databases

ProteinModelPortalO60216.
SMRO60216. Positions 557-624.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111822. 237 interactions.
DIPDIP-29201N.
IntActO60216. 24 interactions.
MINTMINT-2999858.
STRING9606.ENSP00000297338.

PTM databases

PhosphoSiteO60216.

Proteomic databases

PaxDbO60216.
PeptideAtlasO60216.
PRIDEO60216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297338; ENSP00000297338; ENSG00000164754.
GeneID5885.
KEGGhsa:5885.
UCSCuc003yod.3. human.

Organism-specific databases

CTD5885.
GeneCardsGC08M117858.
HGNCHGNC:9811. RAD21.
HPACAB022065.
HPA020044.
MIM606462. gene.
614701. phenotype.
neXtProtNX_O60216.
Orphanet199. Cornelia de Lange syndrome.
PharmGKBPA34170.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249424.
HOGENOMHOG000233800.
HOVERGENHBG059956.
InParanoidO60216.
KOK06670.
OMAVPREEQQ.
OrthoDBEOG7B31N3.
PhylomeDBO60216.
TreeFamTF101215.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000164754-MONOMER.
ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressO60216.
BgeeO60216.
CleanExHS_RAD21.
GenevestigatorO60216.

Family and domain databases

Gene3D1.10.10.580. 1 hit.
InterProIPR023093. Rad21/Rec8_C.
IPR006909. Rad21/Rec8_C_eu.
IPR006910. Rad21_Rec8_N.
[Graphical view]
PfamPF04824. Rad21_Rec8. 1 hit.
PF04825. Rad21_Rec8_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAD21. human.
GeneWikiRAD21.
GenomeRNAi5885.
NextBio22884.
PMAP-CutDBO60216.
PROO60216.
SOURCESearch...

Entry information

Entry nameRAD21_HUMAN
AccessionPrimary (citable) accession number: O60216
Secondary accession number(s): A8K0E0, Q15001, Q99568
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: April 16, 2014
This is version 129 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

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 8

Human chromosome 8: entries, gene names and cross-references to MIM