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Q9ULG1

- INO80_HUMAN

UniProt

Q9ULG1 - INO80_HUMAN

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Protein

DNA helicase INO80

Gene

INO80

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

Functioni

DNA helicase and probable main scaffold component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; according to PubMed:20687897 the contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation. Recruited by YY1 to YY1-activated genes, where it acts as an essential coactivator. Binds DNA. In vitro, has double-stranded DNA-dependent ATPase activity. Involved in UV-damage excision repair, DNA replication and chromosome segregation during normal cell division cycle.7 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi543 – 5508ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. alpha-tubulin binding Source: UniProtKB
  2. ATPase activity Source: UniProtKB
  3. ATP binding Source: UniProtKB-KW
  4. DNA binding Source: UniProtKB
  5. DNA helicase activity Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cellular response to ionizing radiation Source: UniProtKB
  3. cellular response to UV Source: UniProtKB
  4. chromatin remodeling Source: UniProtKB
  5. DNA duplex unwinding Source: GOC
  6. double-strand break repair Source: UniProtKB
  7. double-strand break repair via homologous recombination Source: UniProtKB
  8. mitotic sister chromatid segregation Source: UniProtKB
  9. positive regulation of cell growth Source: UniProtKB
  10. positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
  11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  13. spindle assembly Source: UniProtKB
  14. UV-damage excision repair Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, Mitosis

Keywords - Ligandi

Actin-binding, ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA helicase INO80 (EC:3.6.4.12)
Short name:
hINO80
Alternative name(s):
INO80 complex subunit A
Putative DNA helicase INO80 complex homolog 1
Gene namesi
Name:INO80
Synonyms:INO80A, INOC1, KIAA1259
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:26956. INO80.

Subcellular locationi

Nucleus 3 PublicationsPROSITE-ProRule annotation
Note: Colocalizes with PCNA at replication forks during S-phase. Recruited to DNA damage sites in a ACTR8-dependent manner.

GO - Cellular componenti

  1. Ino80 complex Source: UniProtKB
  2. microtubule Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi653 – 6531E → Q: Abolishes DNA-dependent ATPase and nucleosome remodeling activities. 1 Publication

Organism-specific databases

PharmGKBiPA162392040.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15561556DNA helicase INO80PRO_0000248829Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181N6-acetyllysine1 Publication
Modified residuei1512 – 15121Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9ULG1.
PaxDbiQ9ULG1.
PRIDEiQ9ULG1.

PTM databases

PhosphoSiteiQ9ULG1.

Expressioni

Tissue specificityi

According to PubMed:10574462, widely expressed. According to PubMed:16298340, specifically expressed in brain, liver and pancreas.2 Publications

Gene expression databases

BgeeiQ9ULG1.
CleanExiHS_INO80.
ExpressionAtlasiQ9ULG1. baseline and differential.
GenevestigatoriQ9ULG1.

Organism-specific databases

HPAiHPA055495.

Interactioni

Subunit structurei

Component of the chromatin-remodeling INO80 complex; three different complex modules assemble on different domains of INO80. Interacts with DDB1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTR5Q9H9F96EBI-769345,EBI-769418
DDB1Q165314EBI-769345,EBI-350322
YY1P254905EBI-769345,EBI-765538

Protein-protein interaction databases

BioGridi120076. 25 interactions.
DIPiDIP-34296N.
IntActiQ9ULG1. 14 interactions.
STRINGi9606.ENSP00000355205.

Structurei

3D structure databases

ProteinModelPortaliQ9ULG1.
SMRiQ9ULG1. Positions 518-821, 1096-1241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 405126DBINOPROSITE-ProRule annotationAdd
BLAST
Domaini530 – 701172Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1105 – 1260156Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 266266Assembles INO80 complex module with putative regulatory components INO80E, INO80F, UCHL5, NFRKB, MCRS1 and IN80DAdd
BLAST
Regioni212 – 526315Assembles INO80 complex module consisting of conserved components ACTR8, ACTL6A and YY1Add
BLAST
Regioni521 – 15561036Assembles INO80 complex module consisting of conserved components INO80B, INO80C, ACTR5, RVBL1, RVBL2Add
BLAST

Domaini

The DBINO region is involved in binding to DNA.

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 DBINO domain.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00740000115601.
HOGENOMiHOG000231795.
HOVERGENiHBG057875.
InParanoidiQ9ULG1.
KOiK11665.
OMAiSLHMTSS.
OrthoDBiEOG7B05C6.
PhylomeDBiQ9ULG1.
TreeFamiTF324408.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF13892. DBINO. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51413. DBINO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ULG1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASELGARDD GGCTELAKPL YLQYLERALR LDHFLRQTSA IFNRNISSDD
60 70 80 90 100
SEDGLDDSNP LLPQSGDPLI QVKEEPPNSL LGETSGAGSS GMLNTYSLNG
110 120 130 140 150
VLQSESKCDK GNLYNFSKLK KSRKWLKSIL LSDESSEADS QSEDDDEEEL
160 170 180 190 200
NLSREELHNM LRLHKYKKLH QNKYSKDKEL QQYQYYSAGL LSTYDPFYEQ
210 220 230 240 250
QRHLLGPKKK KFKEEKKLKA KLKKVKKKRR RDEELSSEES PRRHHHQTKV
260 270 280 290 300
FAKFSHDAPP PGTKKKHLSI EQLNARRRKV WLSIVKKELP KANKQKASAR
310 320 330 340 350
NLFLTNSRKL AHQCMKEVRR AALQAQKNCK ETLPRARRLT KEMLLYWKKY
360 370 380 390 400
EKVEKEHRKR AEKEALEQRK LDEEMREAKR QQRKLNFLIT QTELYAHFMS
410 420 430 440 450
RKRDMGHDGI QEEILRKLED SSTQRQIDIG GGVVVNITQE DYDSNHFKAQ
460 470 480 490 500
ALKNAENAYH IHQARTRSFD EDAKESRAAA LRAANKSGTG FGESYSLANP
510 520 530 540 550
SIRAGEDIPQ PTIFNGKLKG YQLKGMNWLA NLYEQGINGI LADEMGLGKT
560 570 580 590 600
VQSIALLAHL AERENIWGPF LIISPASTLN NWHQEFTRFV PKFKVLPYWG
610 620 630 640 650
NPHDRKVIRR FWSQKTLYTQ DAPFHVVITS YQLVVQDVKY FQRVKWQYMV
660 670 680 690 700
LDEAQALKSS SSVRWKILLQ FQCRNRLLLT GTPIQNTMAE LWALLHFIMP
710 720 730 740 750
TLFDSHEEFN EWFSKDIESH AENKSAIDEN QLSRLHMILK PFMLRRIKKD
760 770 780 790 800
VENELSDKIE ILMYCQLTSR QKLLYQALKN KISIEDLLQS SMGSTQQAQN
810 820 830 840 850
TTSSLMNLVM QFRKVCNHPE LFERQETWSP FHISLKPYHI SKFIYRHGQI
860 870 880 890 900
RVFNHSRDRW LRVLSPFAPD YIQRSLFHRK GINEESCFSF LRFIDISPAE
910 920 930 940 950
MANLMLQGLL ARWLALFLSL KASYRLHQLR SWGAPEGESH QRYLRNKDFL
960 970 980 990 1000
LGVNFPLSFP NLCSCPLLKS LVFSSHCKAV SGYSDQVVHQ RRSATSSLRR
1010 1020 1030 1040 1050
CLLTELPSFL CVASPRVTAV PLDSYCNDRS AEYERRVLKE GGSLAAKQCL
1060 1070 1080 1090 1100
LNGAPELAAD WLNRRSQFFP EPAGGLWSIR PQNGWSFIRI PGKESLITDS
1110 1120 1130 1140 1150
GKLYALDVLL TRLKSQGHRV LIYSQMTRMI DLLEEYMVYR KHTYMRLDGS
1160 1170 1180 1190 1200
SKISERRDMV ADFQNRNDIF VFLLSTRAGG LGINLTAADT VIFYDSDWNP
1210 1220 1230 1240 1250
TVDQQAMDRA HRLGQTKQVT VYRLICKGTI EERILQRAKE KSEIQRMVIS
1260 1270 1280 1290 1300
GGNFKPDTLK PKEVVSLLLD DEELEKKLRL RQEEKRQQEE TNRVKERKRK
1310 1320 1330 1340 1350
REKYAEKKKK EDELDGKRRK EGVNLVIPFV PSADNSNLSA DGDDSFISVD
1360 1370 1380 1390 1400
SAMPSPFSEI SISSELHTGS IPLDESSSDM LVIVDDPASS APQSRATNSP
1410 1420 1430 1440 1450
ASITGSVSDT VNGISIQEMP AAGRGHSARS RGRPKGSGST AKGAGKGRSR
1460 1470 1480 1490 1500
KSTAGSAAAM AGAKAGAAAA SAAAYAAYGY NVSKGISASS PLQTSLVRPA
1510 1520 1530 1540 1550
GLADFGPSSA SSPLSSPLSK GNNVPGNPKN LHMTSSLAPD SLVRKQGKGT

NPSGGR
Length:1,556
Mass (Da):176,753
Last modified:September 5, 2006 - v2
Checksum:i712A1EEA26D6A720
GO

Sequence cautioni

The sequence BAA86573.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti882 – 8821I → V.
Corresponds to variant rs34153025 [ dbSNP | Ensembl ].
VAR_049500
Natural varianti1108 – 11081V → G.
Corresponds to variant rs34178030 [ dbSNP | Ensembl ].
VAR_061233

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033085 mRNA. Translation: BAA86573.1. Different initiation.
CH471125 Genomic DNA. Translation: EAW92469.1.
BC146785 mRNA. Translation: AAI46786.1.
AL137280 mRNA. Translation: CAB70675.1.
CCDSiCCDS10071.1.
PIRiT46350.
RefSeqiNP_060023.1. NM_017553.2.
UniGeneiHs.292949.

Genome annotation databases

EnsembliENST00000361937; ENSP00000355205; ENSG00000128908.
ENST00000401393; ENSP00000384686; ENSG00000128908.
GeneIDi54617.
KEGGihsa:54617.
UCSCiuc001zni.3. human.

Polymorphism databases

DMDMi114149322.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033085 mRNA. Translation: BAA86573.1 . Different initiation.
CH471125 Genomic DNA. Translation: EAW92469.1 .
BC146785 mRNA. Translation: AAI46786.1 .
AL137280 mRNA. Translation: CAB70675.1 .
CCDSi CCDS10071.1.
PIRi T46350.
RefSeqi NP_060023.1. NM_017553.2.
UniGenei Hs.292949.

3D structure databases

ProteinModelPortali Q9ULG1.
SMRi Q9ULG1. Positions 518-821, 1096-1241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120076. 25 interactions.
DIPi DIP-34296N.
IntActi Q9ULG1. 14 interactions.
STRINGi 9606.ENSP00000355205.

PTM databases

PhosphoSitei Q9ULG1.

Polymorphism databases

DMDMi 114149322.

Proteomic databases

MaxQBi Q9ULG1.
PaxDbi Q9ULG1.
PRIDEi Q9ULG1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361937 ; ENSP00000355205 ; ENSG00000128908 .
ENST00000401393 ; ENSP00000384686 ; ENSG00000128908 .
GeneIDi 54617.
KEGGi hsa:54617.
UCSCi uc001zni.3. human.

Organism-specific databases

CTDi 54617.
GeneCardsi GC15M041271.
HGNCi HGNC:26956. INO80.
HPAi HPA055495.
MIMi 610169. gene.
neXtProti NX_Q9ULG1.
PharmGKBi PA162392040.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00740000115601.
HOGENOMi HOG000231795.
HOVERGENi HBG057875.
InParanoidi Q9ULG1.
KOi K11665.
OMAi SLHMTSS.
OrthoDBi EOG7B05C6.
PhylomeDBi Q9ULG1.
TreeFami TF324408.

Miscellaneous databases

ChiTaRSi INO80. human.
GenomeRNAii 54617.
NextBioi 57137.
PROi Q9ULG1.
SOURCEi Search...

Gene expression databases

Bgeei Q9ULG1.
CleanExi HS_INO80.
ExpressionAtlasi Q9ULG1. baseline and differential.
Genevestigatori Q9ULG1.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF13892. DBINO. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 3 hits.
PROSITEi PS51413. DBINO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1302-1556.
    Tissue: Testis.
  5. Cited for: FUNCTION, IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Characterization of a human SWI2/SNF2 like protein hINO80: demonstration of catalytic and DNA binding activity."
    Bakshi R., Mehta A.K., Sharma R., Maiti S., Pasha S., Brahmachari V.
    Biochem. Biophys. Res. Commun. 339:313-320(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. Cited for: FUNCTION, INTERACTION WITH YY1.
  8. "A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
    Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
    Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE INO80 COMPLEX.
  9. "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
    Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
    Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The mammalian INO80 complex is recruited to DNA damage sites in an ARP8 dependent manner."
    Kashiwaba S., Kitahashi K., Watanabe T., Onoda F., Ohtsu M., Murakami Y.
    Biochem. Biophys. Res. Commun. 402:619-625(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Human INO80 chromatin-remodelling complex contributes to DNA double-strand break repair via the expression of Rad54B and XRCC3 genes."
    Park E.J., Hur S.K., Kwon J.
    Biochem. J. 431:179-187(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA REPAIR.
  15. "Roles of human INO80 chromatin remodeling enzyme in DNA replication and chromosome segregation suppress genome instability."
    Hur S.K., Park E.J., Han J.E., Kim Y.A., Kim J.D., Kang D., Kwon J.
    Cell. Mol. Life Sci. 67:2283-2296(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway."
    Jiang Y., Wang X., Bao S., Guo R., Johnson D.G., Shen X., Li L.
    Proc. Natl. Acad. Sci. U.S.A. 107:17274-17279(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH DDB1, FUNCTION OF THE INO80 COMPLEX.
  17. "Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
    Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
    J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE INO80 COMPLEX, MUTAGENESIS OF GLU-653.

Entry informationi

Entry nameiINO80_HUMAN
AccessioniPrimary (citable) accession number: Q9ULG1
Secondary accession number(s): A6H8X4, Q9NTG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: October 29, 2014
This is version 115 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3