O60216 (RAD21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	631 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Chromosome › centromere. 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 process	Apoptosis Cell cycle Cell division Chromosome partition DNA damage DNA repair Mitosis
Cellular component	Centromere Chromosome Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Mental retardation
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell division 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 mitotic metaphase/anaphase transition Traceable author statement. Source: Reactome mitotic prometaphase 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_component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cohesin complex Traceable author statement PubMed 19468298. Source: BHF-UCL nuclear meiotic cohesin complex Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PDS5A	Q29RF7	3	EBI-80739,EBI-1175454
PDS5B	Q9NTI5	3	EBI-80739,EBI-1175604
SMC3	Q9UQE7	8	EBI-80739,EBI-80718
WAPAL	Q7Z5K2	11	EBI-80739,EBI-1022242

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 631	631	Double-strand-break repair protein rad21 homolog		PRO_0000097872
Regions
	Region	287 – 403	117	Interaction with WAPAL and PDS5B
	Region	362 – 403	42	Interaction with STAG1
	Compositional bias	469 – 510	42	Pro-rich
Sites
	Site	172 – 173	2	Cleavage; by ESPL1
	Site	279 – 280	2	Cleavage; by caspase-3 or caspase-7
	Site	450 – 451	2	Cleavage; by ESPL1
Amino acid modifications
	Modified residue	46	1	Phosphoserine Ref.15 Ref.18
	Modified residue	153	1	Phosphoserine Ref.17 Ref.18
	Modified residue	175	1	Phosphoserine Ref.15 Ref.17
Natural variations
	Natural variant	376	1	P → R in CDLS4. Ref.21		VAR_068691
	Natural variant	481	1	G → R. Ref.20		VAR_014281
	Natural variant	585	1	C → R in CDLS4. Ref.21		VAR_068692
Experimental info
	Mutagenesis	172	1	R → A: Abolishes first cleavage by ESPL1. Ref.11
	Mutagenesis	279	1	D → A: Abolishes cleavage by caspase-3. Ref.9 Ref.12
	Mutagenesis	450	1	R → A: Abolishes second cleavage by ESPL1. Ref.11
	Sequence conflict	136	1	N → I in CAA66940. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O60216 [UniParc]. Last modified November 15, 2002. Version 2. Checksum: 7D4A6EA6392BE73D	FASTA	631	71,690
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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. , 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

NIEHS-SNPs

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.
IPI	IPI00006715.
RefSeq	NP_006256.1. NM_006265.2.
UniGene	Hs.81848.
3D structure databases
ProteinModelPortal	O60216.
SMR	O60216. Positions 558-628.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29201N.
IntAct	O60216. 19 interactions.
MINT	MINT-2999858.
STRING	9606.ENSP00000297338.
PTM databases
PhosphoSite	O60216.
Proteomic databases
PaxDb	O60216.
PeptideAtlas	O60216.
PRIDE	O60216.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297338; ENSP00000297338; ENSG00000164754.
GeneID	5885.
KEGG	hsa:5885.
UCSC	uc003yod.3. human.
Organism-specific databases
CTD	5885.
GeneCards	GC08M117858.
HGNC	HGNC:9811. RAD21.
HPA	CAB022065. HPA020044.
MIM	606462. gene. 614701. phenotype.
neXtProt	NX_O60216.
Orphanet	199. Cornelia de Lange syndrome.
PharmGKB	PA34170.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG249424.
HOGENOM	HOG000233800.
HOVERGEN	HBG059956.
InParanoid	O60216.
KO	K06670.
OMA	VPREEQQ.
OrthoDB	EOG47PX5K.
PhylomeDB	O60216.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000164754-MONOMER.
Reactome	REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	O60216.
Bgee	O60216.
CleanEx	HS_RAD21.
Genevestigator	O60216.
GermOnline	ENSG00000164754. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.580. 1 hit.
InterPro	IPR023093. Rad21/Rec8_C. IPR006909. Rad21/Rec8_C_eu. IPR006910. Rad21_Rec8_N. [Graphical view]
Pfam	PF04824. Rad21_Rec8. 1 hit. PF04825. Rad21_Rec8_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RAD21. human.
GenomeRNAi	5885.
NextBio	22884.
PMAP-CutDB	O60216.
SOURCE	Search...

Entry information

Entry name

RAD21_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.