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Q96NY9

- MUS81_HUMAN

UniProt

Q96NY9 - MUS81_HUMAN

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Protein

Crossover junction endonuclease MUS81

Gene

MUS81

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Interacts with EME1 and EME2 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks.9 Publications

Cofactori

Mg2+1 Publication

GO - Molecular functioni

  1. 3'-flap endonuclease activity Source: UniProtKB
  2. DNA binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: MGI
  2. DNA recombination Source: UniProtKB-KW
  3. DNA repair Source: UniProtKB
  4. response to intra-S DNA damage checkpoint signaling Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Crossover junction endonuclease MUS81 (EC:3.1.22.-)
Gene namesi
Name:MUS81
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:29814. MUS81.

Subcellular locationi

Nucleusnucleolus 4 Publications
Note: Recruited to foci of DNA damage in S-phase cells.

GO - Cellular componenti

  1. intercellular bridge Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi306 – 3072GD → AE: Loss of activity. 1 Publication
Mutagenesisi333 – 3342ER → AG: Loss of activity. 1 Publication
Mutagenesisi338 – 3392DD → AA: Loss of activity. 2 Publications

Organism-specific databases

PharmGKBiPA134881809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Crossover junction endonuclease MUS81PRO_0000198858Add
BLAST

Proteomic databases

MaxQBiQ96NY9.
PaxDbiQ96NY9.
PRIDEiQ96NY9.

PTM databases

PhosphoSiteiQ96NY9.

Expressioni

Tissue specificityi

Widely expressed.

Developmental stagei

Expressed in S phase and G2 phase.1 Publication

Inductioni

Up-regulated in cells treated with agents that damage DNA or block replication. This up-regulation seems to be independent of transcription.1 Publication

Gene expression databases

BgeeiQ96NY9.
CleanExiHS_MUS81.
ExpressionAtlasiQ96NY9. baseline and differential.
GenevestigatoriQ96NY9.

Organism-specific databases

HPAiHPA050711.
HPA059530.

Interactioni

Subunit structurei

May self-associate. Interacts with EME1, EME2 and CHEK2. Interacts with BLM, and this interaction may stimulate the endonuclease activity of MUS81. Interacts with SLX4/BTBD12; this interaction is direct and links the MUS81-EME1 complex to SLX4, which may coordinate the action of the structure-specific endonuclease during DNA repair. Interacts with DCLRE1B/Apollo.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EME1Q96AY25EBI-2370806,EBI-2370825
FEN1P397485EBI-2370806,EBI-707816
SLX4Q8IY928EBI-2370806,EBI-2370740

Protein-protein interaction databases

BioGridi123170. 13 interactions.
DIPiDIP-48630N.
IntActiQ96NY9. 6 interactions.
MINTiMINT-3056813.
STRINGi9606.ENSP00000307853.

Structurei

Secondary structure

1
551
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi137 – 14913Combined sources
Helixi152 – 1543Combined sources
Helixi160 – 17011Combined sources
Helixi184 – 1907Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi203 – 2053Combined sources
Helixi207 – 21913Combined sources
Turni220 – 2223Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi266 – 2749Combined sources
Beta strandi275 – 2773Combined sources
Helixi287 – 2937Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi307 – 31610Combined sources
Beta strandi325 – 33612Combined sources
Helixi337 – 3459Combined sources
Helixi348 – 35710Combined sources
Turni358 – 3603Combined sources
Beta strandi363 – 3697Combined sources
Beta strandi371 – 3733Combined sources
Helixi381 – 39313Combined sources
Beta strandi398 – 4014Combined sources
Helixi405 – 42218Combined sources
Turni423 – 4253Combined sources
Beta strandi428 – 4303Combined sources
Beta strandi452 – 4554Combined sources
Helixi456 – 4627Combined sources
Turni465 – 4673Combined sources
Helixi471 – 4799Combined sources
Helixi487 – 49610Combined sources
Helixi500 – 50910Combined sources
Helixi513 – 5175Combined sources
Turni518 – 5225Combined sources
Turni526 – 5294Combined sources
Helixi535 – 54511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MC3NMR-A127-230[»]
2ZIXX-ray3.50A246-551[»]
4P0PX-ray2.80A246-551[»]
4P0QX-ray2.85A246-551[»]
4P0RX-ray6.50A/C246-551[»]
4P0SX-ray6.00A/C/E/G246-551[»]
ProteinModelPortaliQ96NY9.
SMRiQ96NY9. Positions 11-90, 128-230, 256-551.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96NY9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini270 – 372103ERCC4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 244120Interaction with BLMAdd
BLAST

Sequence similaritiesi

Belongs to the XPF family.Curated
Contains 1 ERCC4 domain.Curated

Phylogenomic databases

eggNOGiCOG1948.
GeneTreeiENSGT00390000005498.
HOGENOMiHOG000113699.
HOVERGENiHBG052538.
InParanoidiQ96NY9.
KOiK08991.
OMAiKCGRLQR.
OrthoDBiEOG7TXKGV.
PhylomeDBiQ96NY9.
TreeFamiTF315113.

Family and domain databases

Gene3Di1.10.8.310. 1 hit.
3.40.50.10130. 1 hit.
InterProiIPR010996. DNA_pol_b-like_N.
IPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027420. PolB_N.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
PfamiPF02732. ERCC4. 1 hit.
[Graphical view]
SMARTiSM00891. ERCC4. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96NY9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPVRLGRK RPLPACPNPL FVRWLTEWRD EATRSRRRTR FVFQKALRSL
60 70 80 90 100
RRYPLPLRSG KEAKILQHFG DGLCRMLDER LQRHRTSGGD HAPDSPSGEN
110 120 130 140 150
SPAPQGRLAE VQDSSMPVPA QPKAGGSGSY WPARHSGARV ILLVLYREHL
160 170 180 190 200
NPNGHHFLTK EELLQRCAQK SPRVAPGSAR PWPALRSLLH RNLVLRTHQP
210 220 230 240 250
ARYSLTPEGL ELAQKLAESE GLSLLNVGIG PKEPPGEETA VPGAASAELA
260 270 280 290 300
SEAGVQQQPL ELRPGEYRVL LCVDIGETRG GGHRPELLRE LQRLHVTHTV
310 320 330 340 350
RKLHVGDFVW VAQETNPRDP ANPGELVLDH IVERKRLDDL CSSIIDGRFR
360 370 380 390 400
EQKFRLKRCG LERRVYLVEE HGSVHNLSLP ESTLLQAVTN TQVIDGFFVK
410 420 430 440 450
RTADIKESAA YLALLTRGLQ RLYQGHTLRS RPWGTPGNPE SGAMTSPNPL
460 470 480 490 500
CSLLTFSDFN AGAIKNKAQS VREVFARQLM QVRGVSGEKA AALVDRYSTP
510 520 530 540 550
ASLLAAYDAC ATPKEQETLL STIKCGRLQR NLGPALSRTL SQLYCSYGPL

T
Length:551
Mass (Da):61,173
Last modified:February 5, 2008 - v3
Checksum:iD0F331CC2269D847
GO

Sequence cautioni

The sequence BAB14953.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371R → H.3 Publications
Corresponds to variant rs13817 [ dbSNP | Ensembl ].
VAR_025340
Natural varianti115 – 1151S → F.
Corresponds to variant rs34381357 [ dbSNP | Ensembl ].
VAR_061988
Natural varianti180 – 1801R → P.3 Publications
Corresponds to variant rs545500 [ dbSNP | Ensembl ].
VAR_038521
Natural varianti189 – 1891L → F.
Corresponds to variant rs2298447 [ dbSNP | Ensembl ].
VAR_021990
Natural varianti350 – 3501R → W.
Corresponds to variant rs34891773 [ dbSNP | Ensembl ].
VAR_038522
Natural varianti481 – 4811Q → H.
Corresponds to variant rs765593 [ dbSNP | Ensembl ].
VAR_025341

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF425646 mRNA. Translation: AAL28065.1.
BC009999 mRNA. Translation: AAH09999.2.
AK024665 mRNA. Translation: BAB14953.1. Different initiation.
CCDSiCCDS8115.1.
RefSeqiNP_079404.3. NM_025128.4.
UniGeneiHs.288798.

Genome annotation databases

EnsembliENST00000308110; ENSP00000307853; ENSG00000172732.
GeneIDi80198.
KEGGihsa:80198.
UCSCiuc001ofv.4. human.

Polymorphism databases

DMDMi166898077.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF425646 mRNA. Translation: AAL28065.1 .
BC009999 mRNA. Translation: AAH09999.2 .
AK024665 mRNA. Translation: BAB14953.1 . Different initiation.
CCDSi CCDS8115.1.
RefSeqi NP_079404.3. NM_025128.4.
UniGenei Hs.288798.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MC3 NMR - A 127-230 [» ]
2ZIX X-ray 3.50 A 246-551 [» ]
4P0P X-ray 2.80 A 246-551 [» ]
4P0Q X-ray 2.85 A 246-551 [» ]
4P0R X-ray 6.50 A/C 246-551 [» ]
4P0S X-ray 6.00 A/C/E/G 246-551 [» ]
ProteinModelPortali Q96NY9.
SMRi Q96NY9. Positions 11-90, 128-230, 256-551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123170. 13 interactions.
DIPi DIP-48630N.
IntActi Q96NY9. 6 interactions.
MINTi MINT-3056813.
STRINGi 9606.ENSP00000307853.

PTM databases

PhosphoSitei Q96NY9.

Polymorphism databases

DMDMi 166898077.

Proteomic databases

MaxQBi Q96NY9.
PaxDbi Q96NY9.
PRIDEi Q96NY9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308110 ; ENSP00000307853 ; ENSG00000172732 .
GeneIDi 80198.
KEGGi hsa:80198.
UCSCi uc001ofv.4. human.

Organism-specific databases

CTDi 80198.
GeneCardsi GC11P065627.
H-InvDB HIX0009809.
HGNCi HGNC:29814. MUS81.
HPAi HPA050711.
HPA059530.
MIMi 606591. gene.
neXtProti NX_Q96NY9.
PharmGKBi PA134881809.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1948.
GeneTreei ENSGT00390000005498.
HOGENOMi HOG000113699.
HOVERGENi HBG052538.
InParanoidi Q96NY9.
KOi K08991.
OMAi KCGRLQR.
OrthoDBi EOG7TXKGV.
PhylomeDBi Q96NY9.
TreeFami TF315113.

Miscellaneous databases

ChiTaRSi MUS81. human.
EvolutionaryTracei Q96NY9.
GeneWikii MUS81.
GenomeRNAii 80198.
NextBioi 70556.
PROi Q96NY9.
SOURCEi Search...

Gene expression databases

Bgeei Q96NY9.
CleanExi HS_MUS81.
ExpressionAtlasi Q96NY9. baseline and differential.
Genevestigatori Q96NY9.

Family and domain databases

Gene3Di 1.10.8.310. 1 hit.
3.40.50.10130. 1 hit.
InterProi IPR010996. DNA_pol_b-like_N.
IPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027420. PolB_N.
IPR011335. Restrct_endonuc-II-like.
[Graphical view ]
Pfami PF02732. ERCC4. 1 hit.
[Graphical view ]
SMARTi SM00891. ERCC4. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view ]
SUPFAMi SSF47802. SSF47802. 1 hit.
SSF52980. SSF52980. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-37 AND PRO-180, FUNCTION, COFACTOR, INTERACTION WITH CHEK2, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF 306-GLY-ASP-307; 333-GLU-ARG-334 AND 338-ASP-ASP-339.
    Tissue: Cerebellum.
  2. "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], VARIANTS HIS-37 AND PRO-180.
    Tissue: Brain.
  3. "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] OF 24-551, VARIANTS HIS-37 AND PRO-180.
  4. "Holliday junction resolution in human cells: two junction endonucleases with distinct substrate specificities."
    Constantinou A., Chen X.-B., McGowan C.H., West S.C.
    EMBO J. 21:5577-5585(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Identification and characterization of human MUS81-MMS4 structure-specific endonuclease."
    Oegruenc M., Sancar A.
    J. Biol. Chem. 278:21715-21720(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EME1.
  6. "Identification and characterization of the human mus81-eme1 endonuclease."
    Ciccia A., Constantinou A., West S.C.
    J. Biol. Chem. 278:25172-25178(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EME1.
  7. "Mus81 endonuclease localizes to nucleoli and to regions of DNA damage in human S-phase cells."
    Gao H., Chen X.-B., McGowan C.H.
    Mol. Biol. Cell 14:4826-4834(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  8. "RNA interference inhibition of Mus81 reduces mitotic recombination in human cells."
    Blais V., Gao H., Elwell C.A., Boddy M.N., Gaillard P.-H.L., Russell P., McGowan C.H.
    Mol. Biol. Cell 15:552-562(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH EME1, SUBCELLULAR LOCATION, MUTAGENESIS OF 338-ASP-ASP-339.
  9. Cited for: FUNCTION, INTERACTION WITH BLM, SUBCELLULAR LOCATION.
  10. "Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM."
    Ciccia A., Ling C., Coulthard R., Yan Z., Xue Y., Meetei A.R., Laghmani el H., Joenje H., McDonald N., de Winter J.P., Wang W., West S.C.
    Mol. Cell 25:331-343(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EME1 AND EME2.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: INTERACTION WITH DCLRE1B.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: FUNCTION, INTERACTION WITH SLX4.
  15. "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair."
    Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W.
    Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLX4.
  16. "Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases."
    Fekairi S., Scaglione S., Chahwan C., Taylor E.R., Tissier A., Coulon S., Dong M.-Q., Ruse C., Yates J.R. III, Russell P., Fuchs R.P., McGowan C.H., Gaillard P.-H.L.
    Cell 138:78-89(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLX4.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiMUS81_HUMAN
AccessioniPrimary (citable) accession number: Q96NY9
Secondary accession number(s): Q9H7D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 5, 2008
Last modified: November 26, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3