Reviewed, UniProtKB/Swiss-Prot O60934 (NBN_HUMAN)

Names and origin

Protein names

Recommended name:
    Nibrin
Alternative name(s):
    Nijmegen breakage syndrome protein 1
    Cell cycle regulatory protein p95

Gene names

Name:	NBN
Synonyms:	NBS, NBS1, P95

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	754 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the MRE11/RAD50/NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability.
Subunit structure	Component of the MRN complex composed of two heterodimers RAD50/MRE11A associated with a single NBN. Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50 and MRE11A By similarity. Interacts with histone H2AFX this requires phosphorylation of H2AFX on 'Ser-139'. Interacts with HJURP, KPNA2 and TERF2.
Subcellular location	NucleusBy similarity. TelomereBy similarity. Note= Localizes to discrete nuclear foci after treatment with genotoxic agents By similarity.
Tissue specificity	Ubiquitous. Expressed at high levels in testis.
Domain	The FHA and BRCT domains are likely to have a crucial role for both binding to histone H2AFX and for relocalization of MRE11/RAD50 complex to the vicinity of DNA damage. The C-terminal domain contains a MRE11-binding site, and this interaction is required for the nuclear localization of the MRN complex. The EEXXXDDL motif at the C-terminus is required for the interaction with ATM and its recruitment to sites of DNA damage and promote the phosphorylation of ATM substrates, leading to the events of DNA damage response.
Post-translational modification	Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance.
Involvement in disease	Defects in NBN are the cause of Nijmegen breakage syndrome (NBS) [MIM:251260]. NBS is an autosomal recessive syndrome characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, immunodeficiency and predisposition to cancer, particularly to lymphoid malignancies. Defects in NBN are a cause of genetic susceptibility to breast cancer (BC) [MIM:114480]. BC is an extremely common malignancy, affecting one in eight women during their lifetime. A positive family history has been identified as major contributor to risk of development of the disease, and this link is striking for early-onset breast cancer. Defects in NBN may be associated with aplastic anemia [MIM:609135]. Aplastic anemia is a disease of bone-marrow failure characterized by peripheral pancytopenia and marrow hypoplasia. Most of the cases of aplastic anemia are idiopathic, some are familial and some are due to a viral infection or to exposure to chemicals and radiation. Defects in NBN might play a role in the pathogenesis of childhood acute lymphoblastic leukemia (ALL).
Miscellaneous	In case of infection by adenovirus E4, the MRN complex is inactivated and degraded by viral oncoproteins, thereby preventing concatenation of viral genomes in infected cells.
Sequence similarities	Contains 1 BRCT domain. Contains 1 FHA domain.
Sequence caution	The sequence AAI08651.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence starting in position 550.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair Meiosis
Cellular component	Chromosomal protein Nucleus Telomere
Coding sequence diversity	Polymorphism
Disease	Disease mutation
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator Ref.2 Traceable author statement. Source: UniProtKB G1/S transition checkpoint Inferred from direct assay. Source: UniProtKB cell cycle arrest Ref.2 Traceable author statement. Source: UniProtKB double-strand break repair Ref.2 Inferred from direct assay. Source: UniProtKB meiosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle G2/M transition DNA damage checkpoint Inferred from direct assay. Source: UniProtKB regulation of DNA replication initiation Ref.2 Traceable author statement. Source: UniProtKB telomere maintenance Inferred from mutant phenotype. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA Mre11 complex Ref.2 Inferred from direct assay. Source: UniProtKB chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-KW nuclear inclusion body Inferred from direct assay. Source: UniProtKB nucleoplasm Ref.15 Inferred from Experiment. Source: Reactome
Molecular function	protein N-terminus binding Ref.2 Inferred from physical interaction. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCNE1	P24864	1	EBI-494844,EBI-519526
H2AFX	P16104	6	EBI-494844,EBI-494830
MDC1	Q14676	2	EBI-494844,EBI-495644
MRE11A	P49959	1	EBI-494844,EBI-396513

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 754	754	Nibrin		PRO_0000231043
Regions
	Domain	24 – 83	60	FHA
	Domain	105 – 181	77	BRCT
	Motif	461 – 467	7	Nuclear localization signal
	Motif	736 – 743	8	EEXXXDDL motif
	Compositional bias	448 – 451	4	Poly-Gln
Amino acid modifications
	Modified residue	278	1	Phosphoserine; by ATM
	Modified residue	343	1	Phosphoserine; by ATM
	Modified residue	397	1	Phosphoserine
	Modified residue	432	1	Phosphoserine
	Modified residue	615	1	Phosphoserine
Natural variations
	Natural variant	93	1	S → L in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant.		VAR_025792
	Natural variant	95	1	D → N in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant.		VAR_025793
	Natural variant	105	1	K → N: dbSNP rs13312858.		VAR_025794
	Natural variant	150	1	L → F in BC.		VAR_025795
	Natural variant	171	1	I → V in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant; associated with aplastic anemia at homozygosity.		VAR_025796
	Natural variant	185	1	E → Q: dbSNP rs1805794.		VAR_025797
	Natural variant	210	1	V → F		VAR_025798
	Natural variant	215	1	R → W		VAR_025799
	Natural variant	216	1	Q → K: dbSNP rs769416.		VAR_025800
	Natural variant	266	1	P → L: dbSNP rs769420.		VAR_025801
	Natural variant	497	1	T → A: dbSNP rs3026268.		VAR_025802
	Natural variant	574	1	L → I		VAR_025803
Experimental info
	Mutagenesis	28	1	R → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation
	Mutagenesis	45	1	H → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation
	Mutagenesis	136 – 137	2	GG → EE: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation
	Mutagenesis	176	1	Y → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation
	Mutagenesis	343	1	S → A: Abrogates ATM-dependent phosphorylation
	Mutagenesis	397	1	S → A: Abrogates ATM-dependent phosphorylation. No loss of interaction with KPNA2
	Mutagenesis	465 – 466	2	KR → AA: Blocks the association with KPNA2, and reduces nuclear foci formation in response to ionizing radiation
	Mutagenesis	583	1	Q → K: No loss of interaction with KPNA2
	Mutagenesis	615	1	S → A: Abrogates ATM-dependent phosphorylation
	Mutagenesis	736 – 737	2	EE → AA: Decreases ATM binding
	Mutagenesis	741 – 742	2	DD → AA: Decreases ATM binding
	Mutagenesis	745 – 746	2	RY → AA: Decreases ATM binding
	Sequence conflict	247	1	G → R in BAD96976. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O60934-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: CD602F09BA73DAB6	FASTA	754	84,959
	10 20 30 40 50 60 MWKLLPAAGP AGGEPYRLLT GVEYVVGRKN CAILIENDQS ISRNHAVLTA NFSVTNLSQT 70 80 90 100 110 120 DEIPVLTLKD NSKYGTFVNE EKMQNGFSRT LKSGDGITFG VFGSKFRIEY EPLVACSSCL 130 140 150 160 170 180 DVSGKTALNQ AILQLGGFTV NNWTEECTHL VMVSVKVTIK TICALICGRP IVKPEYFTEF 190 200 210 220 230 240 LKAVESKKQP PQIESFYPPL DEPSIGSKNV DLSGRQERKQ IFKGKTFIFL NAKQHKKLSS 250 260 270 280 290 300 AVVFGGGEAR LITEENEEEH NFFLAPGTCV VDTGITNSQT LIPDCQKKWI QSIMDMLQRQ 310 320 330 340 350 360 GLRPIPEAEI GLAVIFMTTK NYCDPQGHPS TGLKTTTPGP SLSQGVSVDE KLMPSAPVNT 370 380 390 400 410 420 TTYVADTESE QADTWDLSER PKEIKVSKME QKFRMLSQDA PTVKESCKTS SNNNSMVSNT 430 440 450 460 470 480 LAKMRIPNYQ LSPTKLPSIN KSKDRASQQQ QTNSIRNYFQ PSTKKRERDE ENQEMSSCKS 490 500 510 520 530 540 ARIETSCSLL EQTQPATPSL WKNKEQHLSE NEPVDTNSDN NLFTDTDLKS IVKNSASKSH 550 560 570 580 590 600 AAEKLRSNKK REMDDVAIED EVLEQLFKDT KPELEIDVKV QKQEEDVNVR KRPRMDIETN 610 620 630 640 650 660 DTFSDEAVPE SSKISQENEI GKKRELKEDS LWSAKEISNN DKLQDDSEML PKKLLLTEFR 670 680 690 700 710 720 SLVIKNSTSR NPSGINDDYG QLKNFKKFKK VTYPGAGKLP HIIGGSDLIA HHARKNTELE 730 740 750 EWLRQEMEVQ NQHAKEESLA DDLFRYNPYL KRRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nibrin, a novel DNA double-strand break repair protein, is mutated in Nijmegen breakage syndrome." Varon R., Vissinga C., Platzer M., Cerosaletti K.M., Chrzanowska K.H., Saar K., Beckmann G., Seemanova E., Cooper P.R., Nowak N.J., Stumm M., Weemaes C.M.R., Gatti R.A., Wilson R.K., Digweed M., Rosenthal A., Sperling K., Concannon P., Reis A. Cell 93:467-476(1998) [PubMed: 9590180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN NIJMEGEN BREAKAGE SYNDROME, VARIANT GLN-185.
[2]	"The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response." Carney J.P., Maser R.S., Olivares H., Davis E.M., Le Beau M., Yates J.R. III, Hays L., Morgan W.F., Petrini J.H.J. Cell 93:477-486(1998) [PubMed: 9590181] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 189-209; 238-250; 289-299; 300-320; 335-351; 395-405; 409-423; 426-441; 457-465; 503-529; 552-568; 595-613; 625-635; 653-660; 671-683 AND 736-745, VARIANT GLN-185, INTERACTION WITH MRE11 AND RAD50.
[3]	"Positional cloning of the gene for Nijmegen breakage syndrome." Matsuura S., Tauchi H., Nakamura A., Kondo N., Sakamoto S., Endo S., Smeets D., Solder B., Belohradsky B.H., Kaloustian V.M., Oshimura M., Isomura M., Nakamura Y., Komatsu K. Nat. Genet. 19:179-181(1998) [PubMed: 9620777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Sequence analysis of an 800-kb genomic DNA region on chromosome 8q21 that contains the Nijmegen breakage syndrome gene, NBS1." Tauchi H., Matsuura S., Isomura M., Kinjo T., Nakamura A., Sakamoto S., Kondo N., Endo S., Komatsu K., Nakamura Y. Genomics 55:242-247(1999) [PubMed: 9933573] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Fibroblast.
[5]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Synovial cell.
[6]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Chambers S.W., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A. Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-105; GLN-185; LYS-216; LEU-266 AND ALA-497.
[7]	The German cDNA consortium Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-754. Tissue: Colon endothelium.
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-550. Tissue: Skin.
[9]	"Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95." Trujillo K.M., Yuan S.-S.F., Lee E.Y.-H.P., Sung P. J. Biol. Chem. 273:21447-21450(1998) [PubMed: 9705271] [Abstract] Cited for: FUNCTION IN DSB REPAIR, IDENTIFICATION IN THE MRN COMPLEX WITH MRE11A AND RAD50.
[10]	"Distinct functional domains of nibrin mediate Mre11 binding, focus formation, and nuclear localization." Desai-Mehta A., Cerosaletti K.M., Concannon P. Mol. Cell. Biol. 21:2184-2191(2001) [PubMed: 11238951] [Abstract] Cited for: INTERACTION WITH MRE11.
[11]	"ATM-dependent phosphorylation of nibrin in response to radiation exposure." Gatei M., Young D., Cerosaletti K.M., Desai-Mehta A., Spring K., Kozlov S., Lavin M.F., Gatti R.A., Concannon P., Khanna K.K. Nat. Genet. 25:115-119(2000) [PubMed: 10802669] [Abstract] Cited for: PHOSPHORYLATION AT SER-343, MUTAGENESIS OF ARG-28; HIS-45; 136-GLY-GLY-137 AND TYR-176.
[12]	"Functional link between ataxia-telangiectasia and Nijmegen breakage syndrome gene products." Zhao S., Weng Y.-C., Yuan S.-S.F., Lin Y.-T., Hsu H.-C., Lin S.-C., Gerbino E., Song M.-H., Zdzienicka M.Z., Gatti R.A., Shay J.W., Ziv Y., Shiloh Y., Lee E.Y.-H.P. Nature 405:473-477(2000) [PubMed: 10839544] [Abstract] Cited for: PHOSPHORYLATION AT SER-278.
[13]	"ATM phosphorylation of Nijmegen breakage syndrome protein is required in a DNA damage response." Wu X., Ranganathan V., Weisman D.S., Heine W.F., Ciccone D.N., O'Neill T.B., Crick K.E., Pierce K.A., Lane W.S., Rathbun G., Livingston D.M., Weaver D.T. Nature 405:477-482(2000) [PubMed: 10839545] [Abstract] Cited for: PHOSPHORYLATION AT SER-343; SER-397 AND SER-615, MUTAGENESIS OF SER-343; SER-397 AND SER-615.
[14]	"Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres." Zhu X.-D., Kuester B., Mann M., Petrini J.H.J., de Lange T. Nat. Genet. 25:347-352(2000) [PubMed: 10888888] [Abstract] Cited for: FUNCTION IN TELOMERES, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH TERF2.
[15]	"NBS1 localizes to gamma-H2AX foci through interaction with the FHA/BRCT domain." Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K., Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K. Curr. Biol. 12:1846-1851(2002) [PubMed: 12419185] [Abstract] Cited for: INTERACTION WITH H2AFX.
[16]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Importin KPNA2 is required for proper nuclear localization and multiple functions of NBS1." Tseng S.-F., Chang C.-Y., Wu K.-J., Teng S.-C. J. Biol. Chem. 280:39594-39600(2005) [PubMed: 16188882] [Abstract] Cited for: INTERACTION WITH KPNA2, MUTAGENESIS OF SER-397; 465-LYS-ARG-466 AND GLN-583.
[18]	"Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage." Falck J., Coates J., Jackson S.P. Nature 434:605-611(2005) [PubMed: 15758953] [Abstract] Cited for: DOMAIN, MUTAGENESIS OF 736-GLU-GLU-737; 741-ASP-ASP-742 AND 745-ARG-TYR-746.
[19]	"Nbs1 is required for ATR-dependent phosphorylation events." Stiff T., Reis C., Alderton G.K., Woodbine L., O'Driscoll M., Jeggo P.A. EMBO J. 24:199-208(2005) [PubMed: 15616588] [Abstract] Cited for: FUNCTION.
[20]	"The role of NBS1 in DNA double strand break repair, telomere stability, and cell cycle checkpoint control." Zhang Y., Zhou J., Lim C.U. Cell Res. 16:45-54(2006) [PubMed: 16467875] [Abstract] Cited for: REVIEW.
[21]	"Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex." Stracker T.H., Carson C.T., Weitzman M.D. Nature 418:348-352(2002) [PubMed: 12124628] [Abstract] Cited for: INACTIVATION BY ADENOVIRUS ONCOPROTEINS.
[22]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"Activation of Holliday junction recognizing protein involved in the chromosomal stability and immortality of cancer cells." Kato T., Sato N., Hayama S., Yamabuki T., Ito T., Miyamoto M., Kondo S., Nakamura Y., Daigo Y. Cancer Res. 67:8544-8553(2007) [PubMed: 17823411] [Abstract] Cited for: INTERACTION WITH HJURP.
[24]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-397, MASS SPECTROMETRY.
[25]	"Mutations in the Nijmegen breakage syndrome gene (NBS1) in childhood acute lymphoblastic leukemia (ALL)." Varon R., Reis A., Henze G., von Einsiedel H.G., Sperling K., Seeger K. Cancer Res. 61:3570-3572(2001) [PubMed: 11325820] [Abstract] Cited for: VARIANTS LEU-93; ASN-95; VAL-171; PHE-210 AND TRP-215, POSSIBLE INVOLVEMENT IN CHILDHOOD ACUTE LYMPHOBLASTIC ANEMIA.
[26]	"Mutation screening of Mre11 complex genes: indication of RAD50 involvement in breast and ovarian cancer susceptibility." Heikkinen K., Karppinen S.-M., Soini Y., Maekinen M., Winqvist R. J. Med. Genet. 40:E131-E131(2003) [PubMed: 14684699] [Abstract] Cited for: VARIANT BC PHE-150, VARIANTS GLN-185 AND ILE-574.
[27]	"Polymorphisms in DNA repair and metabolic genes in bladder cancer." Sanyal S., Festa F., Sakano S., Zhang Z., Steineck G., Norming U., Wijkstroem H., Larsson P., Kumar R., Hemminki K. Carcinogenesis 25:729-734(2004) [PubMed: 14688016] [Abstract] Cited for: VARIANT GLN-185.
[28]	"First case of aplastic anemia in a Japanese child with a homozygous missense mutation in the NBS1 gene (I171V) associated with genomic instability." Shimada H., Shimizu K., Mimaki S., Sakiyama T., Mori T., Shimasaki N., Yokota J., Nakachi K., Ohta T., Ohki M. Hum. Genet. 115:372-376(2004) [PubMed: 15338273] [Abstract] Cited for: VARIANT VAL-171.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF051334 mRNA. Translation: AAC39732.1. AF058696 mRNA. Translation: AAC39752.1. AB013139 Genomic DNA. Translation: BAA28616.1. AF069291 Genomic DNA. Translation: AAC62232.1. AK223256 mRNA. Translation: BAD96976.1. Different initiation. AY566246 Genomic DNA. Translation: AAS59158.1. BC108650 mRNA. Translation: AAI08651.1. Sequence problems. BX640816 mRNA. Translation: CAH56160.1. Different initiation.
PIR	T00393.
RefSeq	NP_002476.2.
UniGene	Hs.492208
3D structure databases