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Protein

Nuclear factor related to kappa-B-binding protein

Gene

NFRKB

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

Functioni

Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'.1 Publication
Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Modulates the deubiquitinase activity of UCHL5 in the INO80 complex.1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • protease binding Source: UniProtKB

GO - Biological processi

  • DNA recombination Source: UniProtKB-KW
  • DNA repair Source: UniProtKB-KW
  • inflammatory response Source: ProtInc
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-5696394. DNA Damage Recognition in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor related to kappa-B-binding protein
Alternative name(s):
DNA-binding protein R kappa-B
INO80 complex subunit G
Gene namesi
Name:NFRKB
Synonyms:INO80G
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7802. NFRKB.

Subcellular locationi

GO - Cellular componenti

  • Ino80 complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31606.

Polymorphism and mutation databases

BioMutaiNFRKB.
DMDMi90101417.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12991299Nuclear factor related to kappa-B-binding proteinPRO_0000227807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei298 – 2981PhosphoserineCombined sources
Modified residuei351 – 3511PhosphoserineCombined sources
Cross-linki488 – 488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1022 – 10221PhosphoserineCombined sources
Modified residuei1237 – 12371N6-acetyllysineCombined sources
Modified residuei1291 – 12911PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6P4R8.
MaxQBiQ6P4R8.
PaxDbiQ6P4R8.
PRIDEiQ6P4R8.

PTM databases

iPTMnetiQ6P4R8.
PhosphoSiteiQ6P4R8.

Expressioni

Tissue specificityi

Expressed in thymus, brain, testes, spleen and liver.1 Publication

Gene expression databases

BgeeiQ6P4R8.
CleanExiHS_NFRKB.
ExpressionAtlasiQ6P4R8. baseline and differential.
GenevisibleiQ6P4R8. HS.

Organism-specific databases

HPAiHPA007082.
HPA007128.

Interactioni

Subunit structurei

Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the N-terminus of INO80. Interacts with UCHL5; NFRKB competes with ADRM1 for interaction with UCHL5.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UCHL5Q9Y5K512EBI-2511210,EBI-1051183

GO - Molecular functioni

  • protease binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110864. 43 interactions.
IntActiQ6P4R8. 17 interactions.
MINTiMINT-2807205.
STRINGi9606.ENSP00000436926.

Structurei

Secondary structure

1
1299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 443Combined sources
Helixi46 – 527Combined sources
Helixi55 – 606Combined sources
Helixi64 – 7310Combined sources
Beta strandi78 – 803Combined sources
Helixi81 – 9414Combined sources
Beta strandi98 – 1014Combined sources
Helixi103 – 11210Combined sources
Turni113 – 1164Combined sources
Helixi118 – 15134Combined sources
Helixi379 – 38810Combined sources
Beta strandi391 – 3944Combined sources
Helixi395 – 40612Combined sources
Helixi409 – 4135Combined sources
Helixi417 – 4193Combined sources
Helixi424 – 4263Combined sources
Helixi427 – 4348Combined sources
Beta strandi448 – 4525Combined sources
Turni453 – 4564Combined sources
Beta strandi457 – 4604Combined sources
Helixi468 – 48114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U21X-ray2.18A/B370-495[»]
4UF5X-ray3.70B40-170[»]
4UF6X-ray3.69C/F/I/L40-101[»]
4WLPX-ray3.10B40-153[»]
ProteinModelPortaliQ6P4R8.
SMRiQ6P4R8. Positions 40-153, 372-481.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6P4R8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 495126Winged-helix like domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi309 – 32719Lys-richAdd
BLAST
Compositional biasi665 – 6728Poly-Ala
Compositional biasi684 – 803120Ser-richAdd
BLAST
Compositional biasi716 – 73924Pro-richAdd
BLAST
Compositional biasi1245 – 127127Gln-richAdd
BLAST

Domaini

NFRKB seems to be mostly disordered. The wing-helix like domain doesn't bind DNA.

Sequence similaritiesi

Belongs to the NFRKB family.Curated

Phylogenomic databases

eggNOGiKOG1927. Eukaryota.
ENOG410YHF2. LUCA.
GeneTreeiENSGT00390000016213.
HOGENOMiHOG000113775.
HOVERGENiHBG082022.
InParanoidiQ6P4R8.
KOiK11671.
OMAiFLPQFPE.
OrthoDBiEOG70CR66.
PhylomeDBiQ6P4R8.
TreeFamiTF324944.

Family and domain databases

InterProiIPR024867. NFRKB.
IPR025220. NFRKB_winged_dom.
[Graphical view]
PANTHERiPTHR13052. PTHR13052. 2 hits.
PfamiPF14465. NFRKB_winged. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6P4R8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDSLDHMLTD PLELGPCGDG HGTRIMEDCL LGGTRVSLPE DLLEDPEIFF
60 70 80 90 100
DVVSLSTWQE VLSDSQREHL QQFLPQFPED SAEQQNELIL ALFSGENFRF
110 120 130 140 150
GNPLHIAQKL FRDGHFNPEV VKYRQLCFKS QYKRYLNSQQ QYFHRLLKQI
160 170 180 190 200
LASRSDLLEM ARRSGPALPF RQKRPSPSRT PEEREWRTQQ RYLKVLREVK
210 220 230 240 250
EECGDTALSS DEEDLSSWLP SSPARSPSPA VPLRVVPTLS TTDMKTADKV
260 270 280 290 300
ELGDSDLKIM LKKHHEKRKH QPDHPDLLTG DLTLNDIMTR VNAGRKGSLA
310 320 330 340 350
ALYDLAVLKK KVKEKEEKKK KKIKTIKSEA EDLAEPLSST EGVAPLSQAP
360 370 380 390 400
SPLAIPAIKE EPLEDLKPCL GINEISSSFF SLLLEILLLE SQASLPMLEE
410 420 430 440 450
RVLDWQSSPA SSLNSWFSAA PNWAELVLPA LQYLAGESRA VPSSFSPFVE
460 470 480 490 500
FKEKTQQWKL LGQSQDNEKE LAALFQLWLE TKDQAFCKQE NEDSSDATTP
510 520 530 540 550
VPRVRTDYVV RPSTGEEKRV FQEQERYRYS QPHKAFTFRM HGFESVVGPV
560 570 580 590 600
KGVFDKETSL NKAREHSLLR SDRPAYVTIL SLVRDAAARL PNGEGTRAEI
610 620 630 640 650
CELLKDSQFL APDVTSTQVN TVVSGALDRL HYEKDPCVKY DIGRKLWIYL
660 670 680 690 700
HRDRSEEEFE RIHQAQAAAA KARKALQQKP KPPSKVKSSS KESSIKVLSS
710 720 730 740 750
GPSEQSQMSL SDSSMPPTPV TPVTPTTPAL PAIPISPPPV SAVNKSGPST
760 770 780 790 800
VSEPAKSSSG VLLVSSPTMP HLGTMLSPAS SQTAPSSQAA ARVVSHSGSA
810 820 830 840 850
GLSQVRVVAQ PSLPAVPQQS GGPAQTLPQM PAGPQIRVPA TATQTKVVPQ
860 870 880 890 900
TVMATVPVKA QTTAATVQRP GPGQTGLTVT SLPATASPVS KPATSSPGTS
910 920 930 940 950
APSASTAAVI QNVTGQNIIK QVAITGQLGV KPQTGNSIPL TATNFRIQGK
960 970 980 990 1000
DVLRLPPSSI TTDAKGQTVL RITPDMMATL AKSQVTTVKL TQDLFGTGGN
1010 1020 1030 1040 1050
TTGKGISATL HVTSNPVHAA DSPAKASSAS APSSTPTGTT VVKVTPDLKP
1060 1070 1080 1090 1100
TEASSSAFRL MPALGVSVAD QKGKSTVASS EAKPAATIRI VQGLGVMPPK
1110 1120 1130 1140 1150
AGQTITVATH AKQGASVASG SGTVHTSAVS LPSMNAAVSK TVAVASGAAS
1160 1170 1180 1190 1200
TPISISTGAP TVRQVPVSTT VVSTSQAGKL PTRITVPLSV ISQPMKGKSV
1210 1220 1230 1240 1250
VTAPIIKGNL GANLSGLGRN IILTTMPAGT KLIAGNKPVS FLTAQQLQQL
1260 1270 1280 1290
QQQGQATQVR IQTVPASHLQ QGTASGSSKA VSTVVVTTAP SPKQAPEQQ
Length:1,299
Mass (Da):139,001
Last modified:March 21, 2006 - v2
Checksum:i087B212E283C3820
GO
Isoform 2 (identifier: Q6P4R8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHVFVQSTCGEETM
     213-213: E → EATLDLQEQFSFE

Show »
Length:1,324
Mass (Da):141,860
Checksum:i52A003376E91C5D9
GO
Isoform 3 (identifier: Q6P4R8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     687-687: Missing.

Note: No experimental confirmation available.
Show »
Length:1,298
Mass (Da):138,873
Checksum:iAE550B9B7DF44736
GO

Sequence cautioni

The sequence AAA17871.1 differs from that shown. Reason: Frameshift at position 1267. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1178 – 11781G → E in AAH63280 (PubMed:15489334).Curated
Sequence conflicti1213 – 12131N → D in AAH63280 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MHVFVQSTCGEETM in isoform 2. 2 PublicationsVSP_017592
Alternative sequencei213 – 2131E → EATLDLQEQFSFE in isoform 2. 2 PublicationsVSP_017593
Alternative sequencei687 – 6871Missing in isoform 3. 1 PublicationVSP_017594

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08191 mRNA. Translation: AAA17871.1. Sequence problems.
X80878 mRNA. Translation: CAA56846.1.
BC063280 mRNA. Translation: AAH63280.1.
AL512730 mRNA. Translation: CAC21663.1.
CCDSiCCDS44770.1. [Q6P4R8-1]
CCDS8483.1. [Q6P4R8-2]
PIRiS52863.
RefSeqiNP_001137307.1. NM_001143835.1. [Q6P4R8-1]
NP_006156.2. NM_006165.3. [Q6P4R8-2]
XP_011541153.1. XM_011542851.1. [Q6P4R8-2]
XP_011541154.1. XM_011542852.1. [Q6P4R8-2]
UniGeneiHs.530539.

Genome annotation databases

EnsembliENST00000446488; ENSP00000400476; ENSG00000170322. [Q6P4R8-1]
ENST00000524746; ENSP00000433572; ENSG00000170322. [Q6P4R8-1]
ENST00000524794; ENSP00000436926; ENSG00000170322. [Q6P4R8-2]
GeneIDi4798.
KEGGihsa:4798.
UCSCiuc001qfg.4. human. [Q6P4R8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08191 mRNA. Translation: AAA17871.1. Sequence problems.
X80878 mRNA. Translation: CAA56846.1.
BC063280 mRNA. Translation: AAH63280.1.
AL512730 mRNA. Translation: CAC21663.1.
CCDSiCCDS44770.1. [Q6P4R8-1]
CCDS8483.1. [Q6P4R8-2]
PIRiS52863.
RefSeqiNP_001137307.1. NM_001143835.1. [Q6P4R8-1]
NP_006156.2. NM_006165.3. [Q6P4R8-2]
XP_011541153.1. XM_011542851.1. [Q6P4R8-2]
XP_011541154.1. XM_011542852.1. [Q6P4R8-2]
UniGeneiHs.530539.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U21X-ray2.18A/B370-495[»]
4UF5X-ray3.70B40-170[»]
4UF6X-ray3.69C/F/I/L40-101[»]
4WLPX-ray3.10B40-153[»]
ProteinModelPortaliQ6P4R8.
SMRiQ6P4R8. Positions 40-153, 372-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110864. 43 interactions.
IntActiQ6P4R8. 17 interactions.
MINTiMINT-2807205.
STRINGi9606.ENSP00000436926.

PTM databases

iPTMnetiQ6P4R8.
PhosphoSiteiQ6P4R8.

Polymorphism and mutation databases

BioMutaiNFRKB.
DMDMi90101417.

Proteomic databases

EPDiQ6P4R8.
MaxQBiQ6P4R8.
PaxDbiQ6P4R8.
PRIDEiQ6P4R8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000446488; ENSP00000400476; ENSG00000170322. [Q6P4R8-1]
ENST00000524746; ENSP00000433572; ENSG00000170322. [Q6P4R8-1]
ENST00000524794; ENSP00000436926; ENSG00000170322. [Q6P4R8-2]
GeneIDi4798.
KEGGihsa:4798.
UCSCiuc001qfg.4. human. [Q6P4R8-1]

Organism-specific databases

CTDi4798.
GeneCardsiNFRKB.
HGNCiHGNC:7802. NFRKB.
HPAiHPA007082.
HPA007128.
MIMi164013. gene.
neXtProtiNX_Q6P4R8.
PharmGKBiPA31606.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1927. Eukaryota.
ENOG410YHF2. LUCA.
GeneTreeiENSGT00390000016213.
HOGENOMiHOG000113775.
HOVERGENiHBG082022.
InParanoidiQ6P4R8.
KOiK11671.
OMAiFLPQFPE.
OrthoDBiEOG70CR66.
PhylomeDBiQ6P4R8.
TreeFamiTF324944.

Enzyme and pathway databases

ReactomeiR-HSA-5696394. DNA Damage Recognition in GG-NER.

Miscellaneous databases

ChiTaRSiNFRKB. human.
EvolutionaryTraceiQ6P4R8.
GeneWikiiNFRKB.
GenomeRNAii4798.
NextBioi18488.
PROiQ6P4R8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P4R8.
CleanExiHS_NFRKB.
ExpressionAtlasiQ6P4R8. baseline and differential.
GenevisibleiQ6P4R8. HS.

Family and domain databases

InterProiIPR024867. NFRKB.
IPR025220. NFRKB_winged_dom.
[Graphical view]
PANTHERiPTHR13052. PTHR13052. 2 hits.
PfamiPF14465. NFRKB_winged. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of R kappa B, a novel DNA-binding protein that recognizes the interleukin-2 receptor alpha chain kappa B site."
    Adams B.S., Leung K.Y., Hanley E.W., Nabel G.J.
    New Biol. 3:1063-1073(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DNA-BINDING, TISSUE SPECIFICITY.
  2. Nieters A., Bouwmeester T., Scheidereit C.
    Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  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] (ISOFORM 1).
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 654-1299 (ISOFORM 3).
    Tissue: Fetal brain.
  5. Cited for: IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN THE INO80 COMPLEX, INTERACTION WITH UCHL5, FUNCTION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-1237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-1022 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: IDENTIFICATION IN THE INO80 COMPLEX.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 370-495.

Entry informationi

Entry nameiNFRKB_HUMAN
AccessioniPrimary (citable) accession number: Q6P4R8
Secondary accession number(s): Q12869, Q15312, Q9H048
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: May 11, 2016
This is version 114 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

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.