Non-POU domain-containing octamer-binding protein

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Reviewed, UniProtKB/Swiss-Prot Q15233 (NONO_HUMAN)

Last modified January 19, 2010. Version 111. 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

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Names and origin

Protein names

Recommended name:
    Non-POU domain-containing octamer-binding protein
      Short name=NonO protein
Alternative name(s):
    54 kDa nuclear RNA- and DNA-binding protein
    p54(nrb)
      Short name=p54nrb
    55 kDa nuclear protein
    NMT55
    DNA-binding p52/p100 complex, 52 kDa subunit

Gene names

Name:	NONO
Synonyms:	NRB54

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site By similarity. Involved in pre-mRNA splicing, probably as an heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. Nono is involved in transcriptional regulation. The SFPQ-NONO-NR5A1/SF-1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription By similarity. Ref.11 Ref.12 Ref.13 Ref.15
Subunit structure	Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. NONO is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with PSPC1 and SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Part of a complex consisting of SFPQ, NONO and NR5A1/SF-1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SPI1 By similarity. Interacts with RNF43. Ref.15 Ref.7 Ref.14 Ref.16 Ref.25
Subcellular location	Nucleus.
Tissue specificity	Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines. Ref.3
Post-translational modification	The N-terminus is blocked.
Involvement in disease	A chromosomal aberration involving NONO may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;X)(p11.2;q13.1) with TFE3.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

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Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement
Domain	Coiled coil Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW RNA splicing Ref.1 Traceable author statement. Source: ProtInc mRNA processing Ref.2 Traceable author statement. Source: ProtInc regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.2 Traceable author statement. Source: ProtInc
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Ref.16 Inferred from physical interaction. Source: IntAct nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-350527,EBI-350527
PSPC1	Q8WXF1	4	EBI-350527,EBI-1392258
Rxra	P28700	1	EBI-350527,EBI-346715	From a different organism.
SFPQ	P23246-1	1	EBI-350527,EBI-355463

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 471

471

Non-POU domain-containing octamer-binding protein

PRO_0000081683

Regions

Domain

74 – 141

RRM 1

Domain

148 – 229

RRM 2

Region

54 – 373

320

DBHS

Coiled coil

268 – 372

105

Potential

Compositional bias

30 – 35

Poly-Gln

Compositional bias

36 – 42

Poly-Pro

Compositional bias

348 – 351

Poly-Arg

Sites

Site

377 – 378

Breakpoint for translocation to form NONO-TFE3

Amino acid modifications

Modified residue

N6-acetyllysine Ref.29

Modified residue

N6-acetyllysine Ref.29

Modified residue

N6-acetyllysine Ref.29

Modified residue

147

Phosphoserine Ref.22 Ref.24

Modified residue

198

N6-acetyllysine Ref.29

Modified residue

428

Phosphothreonine Ref.19 Ref.23 Ref.27 Ref.28

Modified residue

450

Phosphothreonine Ref.22 Ref.24 Ref.19 Ref.23 Ref.27 Ref.28 Ref.17 Ref.18 Ref.20 Ref.21

Modified residue

467

N6-acetyllysine Ref.29

Experimental info

Sequence conflict

H → K Ref.5

Sequence conflict

151

T → H in AAC37578. Ref.1

Sequence conflict

358 – 359

QQ → HE Ref.3

Sequence conflict

358 – 359

QQ → HE Ref.4

Sequence conflict

366 – 367

QQ → HE Ref.3

Sequence conflict

366 – 367

QQ → HE Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

Q15233-1 [UniParc].

Last modified July 5, 2005. Version 4.
Checksum: 26BBD3828F5B9E49
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FASTA

471

54,232

        10         20         30         40         50         60 
MQSNKTFNLE KQNHTPRKHH QHHHQQQHHQ QQQQQPPPPP IPANGQQASS QNEGLTIDLK 

        70         80         90        100        110        120 
NFRKPGEKTF TQRSRLFVGN LPPDITEEEM RKLFEKYGKA GEVFIHKDKG FGFIRLETRT 

       130        140        150        160        170        180 
LAEIAKVELD NMPLRGKQLR VRFACHSASL TVRNLPQYVS NELLEEAFSV FGQVERAVVI 

       190        200        210        220        230        240 
VDDRGRPSGK GIVEFSGKPA ARKALDRCSE GSFLLTTFPR PVTVEPMDQL DDEEGLPEKL 

       250        260        270        280        290        300 
VIKNQQFHKE REQPPRFAQP GSFEYEYAMR WKALIEMEKQ QQDQVDRNIK EAREKLEMEM 

       310        320        330        340        350        360 
EAARHEHQVM LMRQDLMRRQ EELRRMEELH NQEVQKRKQL ELRQEEERRR REEEMRRQQE 

       370        380        390        400        410        420 
EMMRRQQEGF KGTFPDAREQ EIRMGQMAMG GAMGINNRGA MPPAPVPAGT PAPPGPATMM 

       430        440        450        460        470 
PDGTLGLTPP TTERFGQAAT MEGIGAIGGT PPAFNRAAPG AEFAPNKRRR Y

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification and cDNA cloning of HeLa cell p54nrb, a nuclear protein with two RNA recognition motifs and extensive homology to human splicing factor PSF and Drosophila NONA/BJ6." Dong B., Horowitz D.S., Kobayashi R., Krainer A.R. Nucleic Acids Res. 21:4085-4092(1993) [PubMed: 8371983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 252-267; 273-279 AND 283-289.
[2]	"Loss of expression of a 55 kDa nuclear protein (nmt55) in estrogen receptor-negative human breast cancer." Traish A.M., Huang Y.-H., Ashba J., Pronovost M., Pavao M., McAneny D.B., Moreland R.B. Diagn. Mol. Pathol. 6:209-221(1997) [PubMed: 9360842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary carcinoma.
[3]	"AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as candidate genes of X-linked dystonia parkinsonism." Peters U., Haberhausen G., Kostrzewa M., Nolte D., Mueller U. Hum. Genet. 100:569-572(1997) [PubMed: 9341872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Tissue: Blood.
[4]	"54 kDa human protein." Honore B., Rasmussen H.H., Celis J.E. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"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]. Tissue: Cervix, Kidney, Muscle and Skin.
[7]	"Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells." Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H. Biochem. J. 290:267-272(1993) [PubMed: 8439294] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21 AND 133-153, BLOCKAGE OF N-TERMINUS, SUBUNIT.
[8]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 76-91; 127-135; 177-184; 257-270 AND 435-456, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[9]	"Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma." Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D., Hamoudi R., Linehan W.M., Shipley J., Cooper C.S. Oncogene 15:2233-2239(1997) [PubMed: 9393982] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION.
[10]	"The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction." Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O., Westergaard O., Boege F. J. Biol. Chem. 273:26261-26264(1998) [PubMed: 9756848] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SFPQ AND TOP1.
[11]	"PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between separate DNA helices." Straub T., Knudsen B.R., Boege F. Biochemistry 39:7552-7558(2000) [PubMed: 10858305] [Abstract] Cited for: FUNCTION IN DNA UNWINDING.
[12]	"The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs." Zhang Z., Carmichael G.G. Cell 106:465-475(2001) [PubMed: 11525732] [Abstract] Cited for: FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
[13]	"Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription." Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R. Endocrinology 143:1280-1290(2002) [PubMed: 11897684] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN TRANSCRIPTION REGULATION, IDENTIFICATION IN A COMPLEX WITH SFPQ AND NR5A1.
[14]	"PSF and p54nrb bind a conserved stem in U5 snRNA." Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G. RNA 8:1334-1347(2002) [PubMed: 12403470] [Abstract] Cited for: INTERACTION WITH PSQF AND U5 SNRNA, IDENTIFICATION IN IN U5/4/6 SNRNP SND SPLICEOSOME COMPLEXES.
[15]	"Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor." Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S. J. Biol. Chem. 280:5205-5210(2005) [PubMed: 15590677] [Abstract] Cited for: FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING, SUBUNIT.
[16]	"P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner." Fox A.H., Bond C.S., Lamond A.I. Mol. Biol. Cell 16:5304-5315(2005) [PubMed: 16148043] [Abstract] Cited for: INTERACTION WITH PSPC1.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"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 THR-450, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY. Tissue: Epithelium.
[20]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY.
[21]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY.
[22]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND THR-450, MASS SPECTROMETRY.
[23]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY.
[24]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND THR-450, MASS SPECTROMETRY.
[25]	"Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein-interacting proteins." Miyamoto K., Sakurai H., Sugiura T. Proteomics 8:2907-2910(2008) [PubMed: 18655028] [Abstract] Cited for: INTERACTION WITH RNF43.
[26]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[27]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY.
[28]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY. Tissue: T-cell.
[29]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-11; LYS-96; LYS-198 AND LYS-467, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases
EMBL GenBank DDBJ	L14599 mRNA. Translation: AAC37578.1. U89867 mRNA. Translation: AAC51852.1. Y11289 Y11298 Genomic DNA. Translation: CAA72157.1. U02493 mRNA. Translation: AAA03427.1. CR456761 mRNA. Translation: CAG33042.1. BC002364 mRNA. Translation: AAH02364.1. BC003129 mRNA. Translation: AAH03129.1. BC012141 mRNA. Translation: AAH12141.1. BC028299 mRNA. Translation: AAH28299.1. BC069616 mRNA. Translation: AAH69616.1. BC069639 mRNA. Translation: AAH69639.1.
IPI	IPI00304596.
PIR	G01211. S29769. S41768.
RefSeq	NP_001138880.1. NP_001138881.1. NP_001138882.1. NP_031389.3.
UniGene	Hs.533282 Hs.700344
3D structure databases
SMR	Q15233. Positions 67-151, 72-206.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29951N.
IntAct	Q15233. 23 interactions.
STRING	Q15233.
PTM databases
PhosphoSite	Q15233.
2-D gel databases
SWISS-2DPAGE	Q15233.
REPRODUCTION-2DPAGE	IPI00304596.
Proteomic databases
PeptideAtlas	Q15233.
PRIDE	Q15233.
Genome annotation databases
Ensembl	ENST00000276079; ENSP00000276079; ENSG00000147140; Homo sapiens. [Genome view] ENST00000373841; ENSP00000362947; ENSG00000147140; Homo sapiens. [Genome view] ENST00000373856; ENSP00000362963; ENSG00000147140; Homo sapiens. [Genome view]
GeneID	4841.
KEGG	hsa:4841.
NMPDR	fig\|9606.3.peg.32966.
UCSC	uc004dzn.1. human.
Organism-specific databases
CTD	4841.
GeneCards	GC0XP070420.
H-InvDB	HIX0016862. HIX0038889.
HGNC	HGNC:7871. NONO.
HPA	CAB022069.
MIM	300084. gene.
PharmGKB	PA31680.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18466.
HOGENOM	HBG715412.
HOVERGEN	Q15233.
InParanoid	Q15233.
OMA	KQNHAPR.
OrthoDB	EOG941SXM.
PhylomeDB	Q15233.
Enzyme and pathway databases
Pathway_Interaction_DB	circadianpathway. Circadian rhythm pathway.
Gene expression databases
ArrayExpress	Q15233.
Bgee	Q15233.
CleanEx	HS_NONO.
Genevestigator	Q15233.
GermOnline	ENSG00000147140. Homo sapiens.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR012975. NOPS. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
Pfam	PF08075. NOPS. 1 hit. PF00076. RRM_1. 2 hits. [Graphical view]
SMART	SM00360. RRM. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	18654.
PMAP-CutDB	Q15233.
SOURCE	Search...

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Entry information

Entry name

NONO_HUMAN

Accession

Primary (citable) accession number: Q15233
Secondary accession number(s): O00201

Q9BQC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 5, 2005
Last modified:	January 19, 2010
This is version 111 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents