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Reviewed, UniProtKB/Swiss-Prot O60934 (NBN_HUMAN)

Last modified November 25, 2008. Version 67. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nibrin
Alternative name(s):
    Nijmegen breakage syndrome protein 1
    Cell cycle regulatory protein p95
Gene names
Name: NBN
Synonyms: NBS, NBS1, P95
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length754 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 processCell cycle
DNA damage
DNA repair
Meiosis
   Cellular componentChromosomal protein
Nucleus
Telomere
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   PTMPhosphoprotein
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processDNA 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 componentGolgi 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 functionprotein N-terminus binding Ref.2

Inferred from physical interaction. Source: UniProtKB

transcription factor binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 754754Nibrin
PRO_0000231043

Regions

Domain24 – 8360FHA
Domain105 – 18177BRCT
Motif461 – 4677Nuclear localization signal
Motif736 – 7438EEXXXDDL motif
Compositional bias448 – 4514Poly-Gln

Amino acid modifications

Modified residue2781Phosphoserine; by ATM
Modified residue3431Phosphoserine; by ATM
Modified residue3971Phosphoserine
Modified residue4321Phosphoserine
Modified residue6151Phosphoserine

Natural variations

Natural variant931S → L in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant.
VAR_025792
Natural variant951D → N in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant.
VAR_025793
Natural variant1051K → N: dbSNP rs13312858.
VAR_025794
Natural variant1501L → F in BC.
VAR_025795
Natural variant1711I → V in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant; associated with aplastic anemia at homozygosity.
VAR_025796
Natural variant1851E → Q: dbSNP rs1805794.
VAR_025797
Natural variant2101V → F
VAR_025798
Natural variant2151R → W
VAR_025799
Natural variant2161Q → K: dbSNP rs769416.
VAR_025800
Natural variant2661P → L: dbSNP rs769420.
VAR_025801
Natural variant4971T → A: dbSNP rs3026268.
VAR_025802
Natural variant5741L → I
VAR_025803

Experimental info

Mutagenesis281R → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation
Mutagenesis451H → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation
Mutagenesis136 – 1372GG → EE: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation
Mutagenesis1761Y → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation
Mutagenesis3431S → A: Abrogates ATM-dependent phosphorylation
Mutagenesis3971S → A: Abrogates ATM-dependent phosphorylation. No loss of interaction with KPNA2
Mutagenesis465 – 4662KR → AA: Blocks the association with KPNA2, and reduces nuclear foci formation in response to ionizing radiation
Mutagenesis5831Q → K: No loss of interaction with KPNA2
Mutagenesis6151S → A: Abrogates ATM-dependent phosphorylation
Mutagenesis736 – 7372EE → AA: Decreases ATM binding
Mutagenesis741 – 7422DD → AA: Decreases ATM binding
Mutagenesis745 – 7462RY → AA: Decreases ATM binding
Sequence conflict2471G → R in BAD96976. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O60934-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: CD602F09BA73DAB6

FASTA75484,959
        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 

« Hide

References

« Hide '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.

Cross-references

Sequence databases

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.
PIRT00393.
RefSeqNP_002476.2.
UniGeneHs.492208

3D structure databases