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Q9H816 (DCR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
5' exonuclease Apollo

EC=3.1.-.-
Alternative name(s):
DNA cross-link repair 1B protein
SNM1 homolog B
Short name=SNMIB
Short name=hSNM1B
Gene names
Name:DCLRE1B
Synonyms:SNM1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15

Subunit structure

Interacts with TERF2; the interaction is direct. Interacts with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14. Interacts with SPAG5. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Chromosometelomere. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Mainly localizes to telomeres, recruited via its interaction with TERF2. During mitosis, localizes to the centrosome. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.15

Domain

The TBM domain mediates interaction with TERF2.

Post-translational modification

Ubiquitinated, leading to its degradation. Interaction with TERF2 protects it from ubiquitination. Ref.11

Involvement in disease

Hoyeraal-Hreidarsson syndrome (HHS) [MIM:305000]: A clinically severe variant of dyskeratosis congenita that is characterized by multisystem involvement, early onset in utero, and often results in death in childhood. Affected individuals show intrauterine growth retardation, microcephaly, cerebellar hypoplasia, delayed development, and bone marrow failure resulting in immunodeficiency.
Note: The gene represented in this entry may be involved in disease pathogenesis. An aberrant splice variant of DCLRE1B, designated Apollo-Delta, has been found in a patient with Hoyeraal-Hreidarsson syndrome (Ref.16). Apollo-Delta hampers the proper replication of telomeres, leading to major telomeric dysfunction and cellular senescence, but maintains its DNA interstrand cross-link repair function in the whole genome. Ref.16

Miscellaneous

Was named 'Apollo' in reference to the twin brother of 'Artemis' in Greek mythology (Ref.8 and Ref.7). Artemis/DCLRE1C is a related nuclease.

Sequence similarities

Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.

Sequence caution

The sequence BAB14284.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentChromosome
Cytoplasm
Cytoskeleton
Nucleus
Telomere
   Coding sequence diversityPolymorphism
   DiseaseDyskeratosis congenita
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle checkpoint

Inferred from mutant phenotype Ref.13. Source: UniProtKB

nucleic acid phosphodiester bond hydrolysis

Inferred from direct assay Ref.8Ref.15. Source: GOC

protection from non-homologous end joining at telomere

Inferred from mutant phenotype Ref.8. Source: UniProtKB

telomere maintenance

Inferred from mutant phenotype Ref.15. Source: UniProtKB

telomeric 3' overhang formation

Inferred from sequence or structural similarity. Source: UniProtKB

telomeric loop formation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay Ref.13. Source: UniProtKB

chromosome, telomeric region

Inferred from direct assay Ref.8Ref.15. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function5'-3' exonuclease activity

Inferred from direct assay Ref.8Ref.15. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.13Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TERF2Q155546EBI-3508943,EBI-706637

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5325325' exonuclease Apollo
PRO_0000209119

Regions

Motif496 – 51116TBM

Natural variations

Natural variant461R → L. Ref.2
Corresponds to variant rs28381069 [ dbSNP | Ensembl ].
VAR_023292
Natural variant611H → Y. Ref.2
Corresponds to variant rs11552449 [ dbSNP | Ensembl ].
VAR_023293
Natural variant4621D → N. Ref.2
Corresponds to variant rs28381079 [ dbSNP | Ensembl ].
VAR_023294
Natural variant5101N → Y.
Corresponds to variant rs35397235 [ dbSNP | Ensembl ].
VAR_048891

Experimental info

Mutagenesis141D → N in Apm3; abolishes exonuclease activity and function on telomere maintenance. Impairs interaction with SPAG5. Ref.13 Ref.15
Mutagenesis331H → A in Apm1; abolishes exonuclease activity and function on telomere maintenance; when associated with N-35. Ref.15
Mutagenesis351D → N in Apm2; abolishes exonuclease activity and function on telomere maintenance. In Apm1; abolishes exonuclease activity and function on telomere maintenance; when associated with A-33. Ref.15
Mutagenesis2761H → A: Slightly affects interaction with SPAG5. Ref.13
Mutagenesis5041Y → A: Abolishes interaction with TERF2. Ref.17
Mutagenesis5061L → A: Abolishes interaction with TERF2. Ref.17
Mutagenesis5081P → A: Abolishes interaction with TERF2. Ref.17
Sequence conflict2371I → T in BAB14284. Ref.1

Secondary structure

............................................................... 532
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H816 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 601A800CCD43CFDA

FASTA53260,002
        10         20         30         40         50         60 
MNGVLIPHTP IAVDFWSLRR AGTARLFFLS HMHSDHTVGL SSTWARPLYC SPITAHLLHR 

        70         80         90        100        110        120 
HLQVSKQWIQ ALEVGESHVL PLDEIGQETM TVTLLDANHC PGSVMFLFEG YFGTILYTGD 

       130        140        150        160        170        180 
FRYTPSMLKE PALTLGKQIH TLYLDNTNCN PALVLPSRQE AAHQIVQLIR KHPQHNIKIG 

       190        200        210        220        230        240 
LYSLGKESLL EQLALEFQTW VVLSPRRLEL VQLLGLADVF TVEEKAGRIH AVDHMEICHS 

       250        260        270        280        290        300 
NMLRWNQTHP TIAILPTSRK IHSSHPDIHV IPYSDHSSYS ELRAFVAALK PCQVVPIVSR 

       310        320        330        340        350        360 
RPCGGFQDSL SPRISVPLIP DSVQQYMSSS SRKPSLLWLL ERRLKRPRTQ GVVFESPEES 

       370        380        390        400        410        420 
ADQSQADRDS KKAKKEKLSP WPADLEKQPS HHPLRIKKQL FPDLYSKEWN KAVPFCESQK 

       430        440        450        460        470        480 
RVTMLTAPLG FSVHLRSTDE EFISQKTREE IGLGSPLVPM GDDDGGPEAT GNQSAWMGHG 

       490        500        510        520        530 
SPLSHSSKGT PLLATEFRGL ALKYLLTPVN FFQAGYSSRR FDQQVEKYHK PC 

« Hide

References

« Hide 'large scale' references
[1]"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: Retinoblastoma and Teratocarcinoma.
[2]NIEHS SNPs program
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-46; TYR-61 AND ASN-462.
[3]"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].
[4]"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: Placenta.
[5]"DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus formation."
Ishiai M., Kimura M., Namikoshi K., Yamazoe M., Yamamoto K., Arakawa H., Agematsu K., Matsushita N., Takeda S., Buerstedde J.-M., Takata M.
Mol. Cell. Biol. 24:10733-10741(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Human SNM1B is required for normal cellular response to both DNA interstrand crosslink-inducing agents and ionizing radiation."
Demuth I., Digweed M., Concannon P.
Oncogene 23:8611-8618(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase."
van Overbeek M., de Lange T.
Curr. Biol. 16:1295-1302(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2.
[8]"The Apollo 5' exonuclease functions together with TRF2 to protect telomeres from DNA repair."
Lenain C., Bauwens S., Amiard S., Brunori M., Giraud-Panis M.J., Gilson E.
Curr. Biol. 16:1303-1310(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2.
[9]"hSnm1B is a novel telomere-associated protein."
Freibaum B.D., Counter C.M.
J. Biol. Chem. 281:15033-15036(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TERF2.
[10]"Endogenous hSNM1B/Apollo interacts with TRF2 and stimulates ATM in response to ionizing radiation."
Demuth I., Bradshaw P.S., Lindner A., Anders M., Heinrich S., Kallenbach J., Schmelz K., Digweed M., Meyn M.S., Concannon P.
DNA Repair 7:1192-1201(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2.
[11]"The protein hSnm1B is stabilized when bound to the telomere-binding protein TRF2."
Freibaum B.D., Counter C.M.
J. Biol. Chem. 283:23671-23676(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH TERF2.
[12]"Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links."
Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X., Shen X., Li L., Legerski R.J.
Oncogene 27:5045-5056(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MUS81; MRE11 AND FANCD2.
[13]"SNM1B/Apollo interacts with astrin and is required for the prophase cell cycle checkpoint."
Liu L., Akhter S., Bae J.B., Mukhopadhyay S.S., Richie C.T., Liu X., Legerski R.
Cell Cycle 8:628-638(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPAG5, MUTAGENESIS OF ASP-14 AND HIS-276.
[14]"Evidence for hSNM1B/Apollo functioning in the HSP70 mediated DNA damage response."
Anders M., Mattow J., Digweed M., Demuth I.
Cell Cycle 8:1725-1732(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HSPA2; HSPA8 AND HSPA14.
[15]"TRF2 and Apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage."
Ye J., Lenain C., Bauwens S., Rizzo A., Saint-Leger A., Poulet A., Benarroch D., Magdinier F., Morere J., Amiard S., Verhoeyen E., Britton S., Calsou P., Salles B., Bizard A., Nadal M., Salvati E., Sabatier L. expand/collapse author list , Wu Y., Biroccio A., Londono-Vallejo A., Giraud-Panis M.J., Gilson E.
Cell 142:230-242(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, MUTAGENESIS OF ASP-14; HIS-33 AND ASP-35.
[16]"Function of Apollo (SNM1B) at telomere highlighted by a splice variant identified in a patient with Hoyeraal-Hreidarsson syndrome."
Touzot F., Callebaut I., Soulier J., Gaillard L., Azerrad C., Durandy A., Fischer A., de Villartay J.P., Revy P.
Proc. Natl. Acad. Sci. U.S.A. 107:10097-10102(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN HHS.
[17]"A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins."
Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T., Lei M.
Science 319:1092-1096(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 496-530 IN COMPLEX WITH TERF2, MUTAGENESIS OF TYR-504; LEU-506 AND PRO-508.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK022872 mRNA. Translation: BAB14284.1. Different initiation.
AK024060 mRNA. Translation: BAB14807.1.
AY849379 Genomic DNA. Translation: AAV97812.1.
AL137856 Genomic DNA. Translation: CAI19076.1.
BC029687 mRNA. Translation: AAH29687.1.
CCDSCCDS866.1.
RefSeqNP_073747.1. NM_022836.3.
UniGeneHs.591412.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BUAX-ray2.50E/F/G/H495-530[»]
3ZDKX-ray2.16A1-335[»]
ProteinModelPortalQ9H816.
SMRQ9H816. Positions 1-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122331. 6 interactions.
DIPDIP-42669N.
IntActQ9H816. 3 interactions.
MINTMINT-3372972.
STRING9606.ENSP00000358576.

PTM databases

PhosphoSiteQ9H816.

Polymorphism databases

DMDM73620756.

Proteomic databases

PaxDbQ9H816.
PRIDEQ9H816.

Protocols and materials databases

DNASU64858.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369563; ENSP00000358576; ENSG00000118655.
GeneID64858.
KEGGhsa:64858.
UCSCuc001eeg.3. human.

Organism-specific databases

CTD64858.
GeneCardsGC01P114447.
HGNCHGNC:17641. DCLRE1B.
MIM305000. phenotype.
609683. gene.
neXtProtNX_Q9H816.
PharmGKBPA27175.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1236.
HOGENOMHOG000043118.
HOVERGENHBG081420.
InParanoidQ9H816.
KOK15341.
OMAPCQVVPI.
OrthoDBEOG71VSSC.
PhylomeDBQ9H816.
TreeFamTF329572.

Gene expression databases

BgeeQ9H816.
CleanExHS_DCLRE1B.
GenevestigatorQ9H816.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR011084. DRMBL.
[Graphical view]
PfamPF07522. DRMBL. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9H816.
GeneWikiDCLRE1B.
GenomeRNAi64858.
NextBio67007.
PROQ9H816.
SOURCESearch...

Entry information

Entry nameDCR1B_HUMAN
AccessionPrimary (citable) accession number: Q9H816
Secondary accession number(s): Q9H9E5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 107 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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