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Protein

Proto-oncogene c-Rel

Gene

REL

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

Functioni

Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
SignaLinkiQ04864.

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene c-Rel
Gene namesi
Name:REL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9954. REL.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • I-kappaB/NF-kappaB complex Source: GO_Central
  • nucleoplasm Source: GO_Central
  • nucleus Source: CACAO
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA34321.

Polymorphism and mutation databases

BioMutaiREL.
DMDMi548720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 619618Proto-oncogene c-RelPRO_0000205165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei267 – 2671Phosphoserine; by PKASequence Analysis
Modified residuei503 – 5031Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ04864.
PaxDbiQ04864.
PRIDEiQ04864.

PTM databases

PhosphoSiteiQ04864.

Expressioni

Gene expression databases

BgeeiQ04864.
CleanExiHS_REL.
GenevisibleiQ04864. HS.

Organism-specific databases

HPAiCAB004404.

Interactioni

Subunit structurei

Component of the NF-kappa-B p65-c-Rel complex. Component of the NF-kappa-B p50-c-Rel complex. Component of the NF-kappa-B p52-c-Rel complex. Homodimer; component of the NF-kappa-B c-Rel-c-Rel complex (By similarity). Interacts with NKIRAS1. Interacts with NFKBIB (By similarity). Interacts with NFKBIE.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A8K5H93EBI-307352,EBI-10174421
B2R8Y43EBI-307352,EBI-10175581
Q96BA43EBI-307352,EBI-10282301
A1CFQ9NQ943EBI-307352,EBI-2809489
ACOT8O147343EBI-307352,EBI-1237371
AESQ081173EBI-307352,EBI-717810
AGPAT4Q9NRZ53EBI-307352,EBI-1754287
ALOX5P099173EBI-307352,EBI-79934
ARIH2O953763EBI-307352,EBI-711158
ASAP3Q8TDY43EBI-307352,EBI-2609717
ATG9AQ7Z3C63EBI-307352,EBI-727146
ATPAF2Q8N5M13EBI-307352,EBI-1166928
ATXN1P542533EBI-307352,EBI-930964
BARHL2Q9NY433EBI-307352,EBI-10316571
BIDP559573EBI-307352,EBI-519672
BIDP55957-23EBI-307352,EBI-10215147
BMFQ96LC93EBI-307352,EBI-3919268
C11orf68Q9H3H33EBI-307352,EBI-721765
C1orf109Q9NX043EBI-307352,EBI-8643161
C20orf195Q9BVV23EBI-307352,EBI-744935
C9orf72Q96LT73EBI-307352,EBI-2961725
CABP5Q9NP863EBI-307352,EBI-10311131
CCNJLF6RF563EBI-307352,EBI-10177725
CDKN2CP427733EBI-307352,EBI-711290
CEP19Q96LK03EBI-307352,EBI-741885
CGGBP1Q9UFW83EBI-307352,EBI-723153
CHAF1AQ131113EBI-307352,EBI-1020839
CHCHD2Q9Y6H13EBI-307352,EBI-2321769
CIB3Q96Q773EBI-307352,EBI-10292696
CINPQ9BW663EBI-307352,EBI-739784
CKS1BP610243EBI-307352,EBI-456371
COL20A1Q9P218-23EBI-307352,EBI-10318410
COL8A1P276583EBI-307352,EBI-747133
COMMD1Q8N6683EBI-307352,EBI-1550112
CPNE2Q96FN43EBI-307352,EBI-7097057
CPSF1Q105703EBI-307352,EBI-347859
CTNNBIP1Q9NSA33EBI-307352,EBI-747082
DHPSP493663EBI-307352,EBI-741925
DMRT3Q9NQL93EBI-307352,EBI-9679045
DNTTP040533EBI-307352,EBI-1220259
DYNC1LI1Q9Y6G93EBI-307352,EBI-2556107
EFHC1Q5JVL46EBI-307352,EBI-743105
EGLN3Q9H6Z93EBI-307352,EBI-1175354
EIF3AQ24JU43EBI-307352,EBI-10239221
EIF3DO153713EBI-307352,EBI-353818
EIF4E2O605733EBI-307352,EBI-398610
EIF4EBP1Q135413EBI-307352,EBI-74090
EIF5AP632413EBI-307352,EBI-373150
EIF5A2Q9GZV43EBI-307352,EBI-748028
EML2O958343EBI-307352,EBI-1054588
EPHB6O15197-23EBI-307352,EBI-10182490
EPM2AIP1Q7L7753EBI-307352,EBI-6255981
EXOSC1Q9Y3B23EBI-307352,EBI-371892
EXOSC5Q9NQT43EBI-307352,EBI-371876
EXOSC8Q96B263EBI-307352,EBI-371922
FHL2Q141923EBI-307352,EBI-701903
FKBP1BP681063EBI-307352,EBI-6693977
FLAD1Q8NFF53EBI-307352,EBI-742815
FLNAP21333-23EBI-307352,EBI-9641086
FOXO4P981773EBI-307352,EBI-4481939
FUT11Q495W53EBI-307352,EBI-2907712
GADD45GO952573EBI-307352,EBI-448202
GLYCTKQ8IVS83EBI-307352,EBI-748515
GRB2P629933EBI-307352,EBI-401755
HAT1O149293EBI-307352,EBI-2339359
HDAC7Q8WUI4-53EBI-307352,EBI-10276431
HIP1O002913EBI-307352,EBI-473886
HLA-DOAP063403EBI-307352,EBI-10194851
HSPB7Q9UBY93EBI-307352,EBI-739361
IL36RNQ9UBH03EBI-307352,EBI-465156
KIAA0100Q08E863EBI-307352,EBI-10226057
KLHL32Q5THT13EBI-307352,EBI-10247181
KRTAP9-4Q9BYQ23EBI-307352,EBI-10185730
LASP1Q148473EBI-307352,EBI-742828
LGALS14Q8TCE93EBI-307352,EBI-10274069
LMO1P258003EBI-307352,EBI-8639312
LMO2P257913EBI-307352,EBI-739696
LNPEPQ9UIQ63EBI-307352,EBI-2805360
LSM2Q9Y3333EBI-307352,EBI-347416
MAD2L2Q9UI953EBI-307352,EBI-77889
MAGOHBQ96A723EBI-307352,EBI-746778
MAP3K7CLP57077-43EBI-307352,EBI-10215880
MEMO1Q9Y3163EBI-307352,EBI-1104564
MIEN1Q9BRT33EBI-307352,EBI-6137472
MORF4L1Q9UBU83EBI-307352,EBI-399246
MRPL10Q7Z7H83EBI-307352,EBI-723524
NAGKQ9UJ703EBI-307352,EBI-372578
NCK2O436393EBI-307352,EBI-713635
NDUFAF3Q9BU61-23EBI-307352,EBI-10298649
NECAP1A8K3C23EBI-307352,EBI-10174302
NEDD9Q145113EBI-307352,EBI-2108053
NEIL2Q969S23EBI-307352,EBI-10281234
NEUROG3Q9Y4Z23EBI-307352,EBI-10328570
NFKB2Q006533EBI-307352,EBI-307326
NGBQ9NPG23EBI-307352,EBI-10311409
NME7Q9Y5B83EBI-307352,EBI-744782
NOL9Q5SY163EBI-307352,EBI-1055462
NR2C2APQ86WQ03EBI-307352,EBI-10260040
NUDT14O958483EBI-307352,EBI-536866
NXT2Q9NPJ83EBI-307352,EBI-752122
OAZ3Q9UMX23EBI-307352,EBI-10281601
OSGIN1Q9UJX03EBI-307352,EBI-9057006
OSTF1Q928823EBI-307352,EBI-1051152
OTUB2Q96DC93EBI-307352,EBI-746259
OTUD4Q018043EBI-307352,EBI-1054396
PARVGQ9HBI03EBI-307352,EBI-3921217
PATE1Q8WXA23EBI-307352,EBI-10277790
PIH1D2Q8WWB53EBI-307352,EBI-10232538
PLCB4Q151473EBI-307352,EBI-998637
PLEKHN1Q494U13EBI-307352,EBI-10241513
POLE2P562823EBI-307352,EBI-713847
POLR1AO956023EBI-307352,EBI-359472
POLR2LP628753EBI-307352,EBI-359527
POP5Q969H63EBI-307352,EBI-366525
PRDM10Q9NQV63EBI-307352,EBI-10312448
PSMA1P257863EBI-307352,EBI-359352
PTGER3Q147X83EBI-307352,EBI-10234038
PTK6Q138823EBI-307352,EBI-1383632
R3HDM2Q9Y2K5-23EBI-307352,EBI-10326419
RAB41Q5JT253EBI-307352,EBI-10244509
RABIFP472243EBI-307352,EBI-713992
RASSF5Q8WWW03EBI-307352,EBI-367390
RBM39Q14498-33EBI-307352,EBI-6654703
RECKQ6P9E23EBI-307352,EBI-10253121
RELAQ04206-33EBI-307352,EBI-10223388
REXO1L1PQ8IX063EBI-307352,EBI-10262361
RIPPLY1Q0D2K33EBI-307352,EBI-10226430
RNF213Q63HN8-63EBI-307352,EBI-10248548
RTDR1Q9UHP63EBI-307352,EBI-748350
SATQ6ICU93EBI-307352,EBI-10178867
SDCBPO005603EBI-307352,EBI-727004
SEC14L4Q9UDX33EBI-307352,EBI-10320311
SEC31AO949793EBI-307352,EBI-1767898
SEPT7Q16181-23EBI-307352,EBI-10176094
SLC39A13Q96H723EBI-307352,EBI-10287091
SLC41A3Q96GZ63EBI-307352,EBI-7225508
SLC6A12P480653EBI-307352,EBI-3843589
SNRNP25Q9BV903EBI-307352,EBI-9675976
STK16O757163EBI-307352,EBI-749295
STRA13A8MT693EBI-307352,EBI-5529694
SZT2Q5T011-53EBI-307352,EBI-10245139
TENC1Q63HR23EBI-307352,EBI-949753
TMEM8AQ9HCN33EBI-307352,EBI-10310808
TRAPPC2LQ9UL333EBI-307352,EBI-747601
TRIM74Q86UV6-23EBI-307352,EBI-10259086
TSSC4Q9Y5U23EBI-307352,EBI-717229
TSSK3Q96PN83EBI-307352,EBI-3918381
TSTD2Q5T7W73EBI-307352,EBI-8994397
TTC19Q6DKK23EBI-307352,EBI-948354
TXNL4BQ9NX013EBI-307352,EBI-10309345
UBASH3AP570753EBI-307352,EBI-2105393
UBE2KP610863EBI-307352,EBI-473850
UBE2ZQ9H8323EBI-307352,EBI-720977
VPS25Q9BRG13EBI-307352,EBI-741945
ZDHHC24Q6UX983EBI-307352,EBI-10254561
ZNF417Q8TAU33EBI-307352,EBI-740727
ZNF550Q7Z3983EBI-307352,EBI-10256834
ZNF564Q8TBZ83EBI-307352,EBI-10273713
ZNF572Q7Z3I73EBI-307352,EBI-10257016
ZNF765Q7L2R63EBI-307352,EBI-9676069

Protein-protein interaction databases

BioGridi111898. 211 interactions.
DIPiDIP-301N.
IntActiQ04864. 175 interactions.
MINTiMINT-1137552.
STRINGi9606.ENSP00000295025.

Structurei

3D structure databases

ProteinModelPortaliQ04864.
SMRiQ04864. Positions 8-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 297290RHDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi290 – 2956Nuclear localization signalSequence Analysis

Sequence similaritiesi

Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG119056.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000264257.
HOVERGENiHBG017916.
InParanoidiQ04864.
KOiK09254.
OMAiWEAKGIF.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ04864.
TreeFamiTF325632.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR030505. c-Rel.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
IPR030492. RHD_CS.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF4. PTHR24169:SF4. 1 hit.
PfamiPF00554. RHD. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q04864-1) [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
MASGAYNPYI EIIEQPRQRG MRFRYKCEGR SAGSIPGEHS TDNNRTYPSI
60 70 80 90 100
QIMNYYGKGK VRITLVTKND PYKPHPHDLV GKDCRDGYYE AEFGQERRPL
110 120 130 140 150
FFQNLGIRCV KKKEVKEAII TRIKAGINPF NVPEKQLNDI EDCDLNVVRL
160 170 180 190 200
CFQVFLPDEH GNLTTALPPV VSNPIYDNRA PNTAELRICR VNKNCGSVRG
210 220 230 240 250
GDEIFLLCDK VQKDDIEVRF VLNDWEAKGI FSQADVHRQV AIVFKTPPYC
260 270 280 290 300
KAITEPVTVK MQLRRPSDQE VSESMDFRYL PDEKDTYGNK AKKQKTTLLF
310 320 330 340 350
QKLCQDHVET GFRHVDQDGL ELLTSGDPPT LASQSAGITV NFPERPRPGL
360 370 380 390 400
LGSIGEGRYF KKEPNLFSHD AVVREMPTGV SSQAESYYPS PGPISSGLSH
410 420 430 440 450
HASMAPLPSS SWSSVAHPTP RSGNTNPLSS FSTRTLPSNS QGIPPFLRIP
460 470 480 490 500
VGNDLNASNA CIYNNADDIV GMEASSMPSA DLYGISDPNM LSNCSVNMMT
510 520 530 540 550
TSSDSMGETD NPRLLSMNLE NPSCNSVLDP RDLRQLHQMS SSSMSAGANS
560 570 580 590 600
NTTVFVSQSD AFEGSDFSCA DNSMINESGP SNSTNPNSHG FVQDSQYSGI
610
GSMQNEQLSD SFPYEFFQV
Length:619
Mass (Da):68,520
Last modified:June 1, 1994 - v1
Checksum:i03E1033BDF7B1B30
GO
Isoform 2 (identifier: Q04864-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     308-339: Missing.

Note: No experimental confirmation available.
Show »
Length:587
Mass (Da):65,225
Checksum:iE312A59CF1D306A2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei308 – 33932Missing in isoform 2. 1 PublicationVSP_055857Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75042 mRNA. Translation: CAA52954.1.
DQ314888 Genomic DNA. Translation: ABC40747.1.
AC010733 Genomic DNA. No translation available.
BC117191 mRNA. Translation: AAI17192.1.
BC143885 mRNA. Translation: AAI43886.1.
M11595 Genomic DNA. Translation: AAA52073.1.
CCDSiCCDS1864.1. [Q04864-1]
CCDS74515.1. [Q04864-2]
PIRiA60646.
RefSeqiNP_001278675.1. NM_001291746.1. [Q04864-2]
NP_002899.1. NM_002908.3. [Q04864-1]
UniGeneiHs.631886.
Hs.633256.

Genome annotation databases

EnsembliENST00000295025; ENSP00000295025; ENSG00000162924. [Q04864-1]
ENST00000394479; ENSP00000377989; ENSG00000162924. [Q04864-2]
GeneIDi5966.
KEGGihsa:5966.
UCSCiuc002sam.1. human. [Q04864-1]
uc002san.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75042 mRNA. Translation: CAA52954.1.
DQ314888 Genomic DNA. Translation: ABC40747.1.
AC010733 Genomic DNA. No translation available.
BC117191 mRNA. Translation: AAI17192.1.
BC143885 mRNA. Translation: AAI43886.1.
M11595 Genomic DNA. Translation: AAA52073.1.
CCDSiCCDS1864.1. [Q04864-1]
CCDS74515.1. [Q04864-2]
PIRiA60646.
RefSeqiNP_001278675.1. NM_001291746.1. [Q04864-2]
NP_002899.1. NM_002908.3. [Q04864-1]
UniGeneiHs.631886.
Hs.633256.

3D structure databases

ProteinModelPortaliQ04864.
SMRiQ04864. Positions 8-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111898. 211 interactions.
DIPiDIP-301N.
IntActiQ04864. 175 interactions.
MINTiMINT-1137552.
STRINGi9606.ENSP00000295025.

PTM databases

PhosphoSiteiQ04864.

Polymorphism and mutation databases

BioMutaiREL.
DMDMi548720.

Proteomic databases

MaxQBiQ04864.
PaxDbiQ04864.
PRIDEiQ04864.

Protocols and materials databases

DNASUi5966.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295025; ENSP00000295025; ENSG00000162924. [Q04864-1]
ENST00000394479; ENSP00000377989; ENSG00000162924. [Q04864-2]
GeneIDi5966.
KEGGihsa:5966.
UCSCiuc002sam.1. human. [Q04864-1]
uc002san.1. human.

Organism-specific databases

CTDi5966.
GeneCardsiGC02P061108.
HGNCiHGNC:9954. REL.
HPAiCAB004404.
MIMi164910. gene.
neXtProtiNX_Q04864.
PharmGKBiPA34321.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG119056.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000264257.
HOVERGENiHBG017916.
InParanoidiQ04864.
KOiK09254.
OMAiWEAKGIF.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ04864.
TreeFamiTF325632.

Enzyme and pathway databases

ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
SignaLinkiQ04864.

Miscellaneous databases

GeneWikiiREL.
GenomeRNAii5966.
NextBioi23226.
PROiQ04864.
SOURCEiSearch...

Gene expression databases

BgeeiQ04864.
CleanExiHS_REL.
GenevisibleiQ04864. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR030505. c-Rel.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
IPR030492. RHD_CS.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF4. PTHR24169:SF4. 1 hit.
PfamiPF00554. RHD. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human rel proto-oncogene cDNA containing an Alu fragment as a potential coding exon."
    Brownell E., Mittereder N., Rice N.R.
    Oncogene 4:935-942(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORM 2).
    Tissue: Colon.
  5. "Genetic characterization of human c-rel sequences."
    Brownell E., O'Brien S.J., Nash W.G., Rice N.R.
    Mol. Cell. Biol. 5:2826-2831(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-284.
  6. "A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a DNA element involved in the phorbol ester induction of the human urokinase gene."
    Hansen S.K., Nerlov C., Zabel U., Verde P., Johnsen M., Baeuerle P.A., Blasi F.
    EMBO J. 11:205-213(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
  7. "Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor necrosis factor."
    Beg A.A., Baldwin A.S. Jr.
    Oncogene 9:1487-1492(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P52-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
  8. "Regulation of intercellular adhesion molecule-1 gene by tumor necrosis factor-alpha is mediated by the nuclear factor-kappaB heterodimers p65/p65 and p65/c-Rel in the absence of p50."
    Aoudjit F., Brochu N., Belanger B., Stratowa C., Hiscott J., Audette M.
    Cell Growth Differ. 8:335-342(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
  9. "A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription."
    Li Z., Nabel G.J.
    Mol. Cell. Biol. 17:6184-6190(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBIE.
  10. "Tumor necrosis factor-alpha activation of NF-kappa B requires the phosphorylation of Ser-471 in the transactivation domain of c-Rel."
    Martin A.G., Fresno M.
    J. Biol. Chem. 275:24383-24391(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-503.
  11. "Leishmania major amastigotes induce p50/c-Rel NF-kappa B transcription factor in human macrophages: involvement in cytokine synthesis."
    Guizani-Tabbane L., Ben-Aissa K., Belghith M., Sassi A., Dellagi K.
    Infect. Immun. 72:2582-2589(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX.
  12. "Inhibition of NF-kappaB activity by IkappaBbeta in association with kappaB-Ras."
    Chen Y., Vallee S., Wu J., Vu D., Sondek J., Ghosh G.
    Mol. Cell. Biol. 24:3048-3056(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NKIRAS1.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiREL_HUMAN
AccessioniPrimary (citable) accession number: Q04864
Secondary accession number(s): Q17RU2, Q2PNZ7, Q6LDY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 144 of the entry and version 1 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 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.