P25799 (NFKB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear factor NF-kappa-B p105 subunit

Alternative name(s):
DNA-binding factor KBF1
EBP-1
NF-kappa-B1 p84/NF-kappa-B1 p98
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1

Cleaved into the following chain:

1. Nuclear factor NF-kappa-B p50 subunit

Gene names

Name:

Nfkb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	971 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes 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 and the heterodimeric p65-p50 complex appears to be most abundant one. 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. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. Plays a role in the regulation of apoptosis. Isoform 5, isoform 6 and isoform 7 act as inhibitors of transactivation of p50 NF-kappa-B subunit, probably by sequestering it in the cytoplasm. Isoform 3 (p98) (but not p84 or p105) acts as a transactivator of NF-kappa-B-regulated gene expression. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.
Subunit structure	Component of the NF-kappa-B p65-p50 complex. Component of the NF-kappa-B p65-p50 complex. Homodimer; component of the NF-kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50 complex. Component of the NF-kappa-B p50-c-Rel complex. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity. Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding. Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50. NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2. Interacts with GSK3B; the interaction prevents processing of p105 to p50. NFKB1/p50 interacts with NFKBIE By similarity. NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID. Directly interacts with MEN1 By similarity. Interacts with HIF1AN By similarity. Ref.13 Ref.14 Ref.15 Ref.16
Subcellular location	Nucleus Ref.2 Ref.11. Cytoplasm Ref.2 Ref.11. Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Ref.2 Ref.11 Isoform 5: Cytoplasm Ref.2 Ref.11. Isoform 6: Nucleus Ref.2 Ref.11. Cytoplasm Ref.2 Ref.11. Isoform 7: Nucleus Ref.2 Ref.11.
Induction	By phorbol ester and TNF-alpha.
Domain	The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation. Glycine-rich region (GRR) appears to be a critical element in the generation of p50.
Post-translational modification	While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p50 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing. Phosphorylation at 'Ser-930' and 'Ser-935' are required for BTRC/BTRCP-mediated proteolysis By similarity. Polyubiquitination seems to allow p105 processing. S-nitrosylation of Cys-59 affects DNA binding By similarity. The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation By similarity.
Sequence similarities	Contains 7 ANK repeats. Contains 1 death domain. Contains 1 RHD (Rel-like) domain.
Sequence caution	The sequence BAC35117.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Hydroxylation Lipoprotein Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to interleukin-1 Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara lymph node development Traceable author statement PubMed 10687308. Source: MGI negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of calcidiol 1-monooxygenase activity Inferred from electronic annotation. Source: Compara negative regulation of cytokine production Inferred from mutant phenotype PubMed 18566389. Source: BHF-UCL negative regulation of inflammatory response Inferred from mutant phenotype PubMed 18270204. Source: MGI negative regulation of interleukin-12 biosynthetic process Inferred from direct assay PubMed 14568984. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of hyaluronan biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 16081776PubMed 19666510. Source: MGI response to bacterium Inferred from electronic annotation. Source: Compara response to copper ion Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from electronic annotation. Source: Compara signal transduction Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay Ref.14. Source: MGI mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 10395695Ref.14PubMed 12970181PubMed 15220916PubMed 15728238PubMed 15817708PubMed 19404405PubMed 19734906PubMed 21982707. Source: MGI protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	double-stranded DNA binding Inferred from electronic annotation. Source: Compara nucleic acid binding transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 15220916. Source: MGI regulatory region DNA binding Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay PubMed 19404405. Source: MGI sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro transcription regulatory region sequence-specific DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Hdac1	O09106	2	EBI-643958,EBI-301912
NCOA1	Q15788	2	EBI-643958,EBI-455189	From a different organism.
Rela	Q04207	3	EBI-643958,EBI-644400

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P25799-1)

Also known as: p105;

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.

Isoform 2 (identifier: P25799-2)

Also known as: p84;

The sequence of this isoform differs from the canonical sequence as follows:
     780-971: VFDILNGKPY...GQEGPIEGKI → GT

Isoform 3 (identifier: P25799-3)

Also known as: p98;

The sequence of this isoform differs from the canonical sequence as follows:
     860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL

Isoform 4 (identifier: P25799-4)

The sequence of this isoform differs from the canonical sequence as follows:
     353-356: DKEE → GTWV
     357-971: Missing.

Isoform 5 (identifier: P25799-5)

Also known as: P70; I-kappa-B gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.

Isoform 6 (identifier: P25799-6)

Also known as: p63; I-kappa-B gamma-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.
     860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL

Isoform 7 (identifier: P25799-7)

Also known as: p55; I-kappa-B gamma-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.
     780-971: VFDILNGKPY...GQEGPIEGKI → GT

Note: Inhibits the activity of the p50 NF-kappa-B subunit.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 971

971

Nuclear factor NF-kappa-B p105 subunit

PRO_0000030312

Chain

1 – 431

431

Nuclear factor NF-kappa-B p50 subunit By similarity

PRO_0000030313

Regions

Domain

40 – 365

326

RHD

Repeat

538 – 567

30

ANK 1

Repeat

577 – 606

30

ANK 2

Repeat

610 – 639

30

ANK 3

Repeat

646 – 675

30

ANK 4

Repeat

680 – 710

31

ANK 5

Repeat

714 – 743

30

ANK 6

Repeat

767 – 797

31

ANK 7

Domain

801 – 888

88

Death

Region

370 – 392

23

GRR

Region

433 – 971

539

Interaction with CFLAR By similarity

Region

646 – 680

35

Essential for interaction with HIF1AN By similarity

Motif

358 – 363

6

Nuclear localization signal Potential

Compositional bias

373 – 431

59

Gly-rich

Sites

Site

431 – 432

2

Cleavage (when cotranslationally processed) By similarity

Amino acid modifications

Modified residue

59

1

S-nitrosocysteine; alternate By similarity

Modified residue

335

1

Phosphoserine; by PKA Potential

Modified residue

438

1

N6-acetyllysine; by EP300 By similarity

Modified residue

447

1

Phosphoserine Ref.17

Modified residue

674

1

(3S)-3-hydroxyasparagine; by HIF1AN By similarity

Modified residue

910

1

Phosphoserine; by GSK3-beta; in vitro By similarity

Modified residue

930

1

Phosphoserine; by IKKB By similarity

Modified residue

935

1

Phosphoserine; by IKKB By similarity

Modified residue

940

1

Phosphoserine By similarity

Lipidation

59

1

S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate By similarity

Natural variations

Alternative sequence

1 – 364

364

Missing in isoform 5, isoform 6 and isoform 7.

VSP_017236

Alternative sequence

353 – 356

4

DKEE → GTWV in isoform 4.

VSP_017237

Alternative sequence

357 – 971

615

Missing in isoform 4.

VSP_017238

Alternative sequence

780 – 971

192

VFDIL…IEGKI → GT in isoform 2 and isoform 7.

VSP_005583

Alternative sequence

860 – 971

112

VSGGT…IEGKI → MNSGIVTASVTVVWRHPSAN SALQSLLLETAHCYL in isoform 3 and isoform 6.

VSP_005584

Experimental info

Sequence conflict

111

1

L → P in AAR00341. Ref.9

Sequence conflict

265

1

E → G in BAC35117. Ref.10

Sequence conflict

530

1

H → D in BAE34261. Ref.10

Sequence conflict

546

1

A → G in BAE34261. Ref.10

Sequence conflict

684

1

A → P in AAA40415. Ref.1

Sequence conflict

684

1

A → P in AAB21851. Ref.2

Sequence conflict

684

1

A → P in AAB28573. Ref.3

Sequence conflict

732

1

A → T in BAE34261. Ref.10

Sequence conflict

950

1

P → A in BAE43399. Ref.10

Secondary structure

1

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971

Helix Strand Turn

Details...

Beta strand

41 – 46

6

Beta strand

50 – 52

3

Helix

58 – 60

3

Beta strand

62 – 64

3

Beta strand

74 – 76

3

Beta strand

81 – 85

5

Beta strand

92 – 98

7

Beta strand

100 – 103

4

Beta strand

108 – 113

6

Beta strand

117 – 119

3

Beta strand

120 – 124

5

Beta strand

131 – 133

3

Beta strand

138 – 140

3

Helix

144 – 146

3

Helix

147 – 160

14

Beta strand

162 – 164

3

Helix

165 – 169

5

Helix

171 – 173

3

Beta strand

179 – 182

4

Helix

188 – 203

16

Beta strand

209 – 219

11

Beta strand

221 – 223

3

Beta strand

225 – 228

4

Beta strand

232 – 239

8

Beta strand

240 – 242

3

Turn

243 – 246

4

Beta strand

250 – 254

5

Beta strand

256 – 259

4

Beta strand

265 – 271

7

Turn

275 – 277

3

Beta strand

279 – 284

6

Helix

287 – 289

3

Beta strand

292 – 295

4

Helix

300 – 302

3

Turn

305 – 307

3

Beta strand

308 – 312

5

Beta strand

325 – 332

8

Turn

334 – 336

3

Beta strand

343 – 348

6

Beta strand

351 – 354

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p105) [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 91EA9C595E375C30	FASTA	971	105,615
	10 20 30 40 50 60 MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ RGFRFRYVCE 70 80 90 100 110 120 GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN GKNIHLHAHS LVGKHCEDGV 130 140 150 160 170 180 CTVTAGPKDM VVGFANLGIL HVTKKKVFET LEARMTEACI RGYNPGLLVH SDLAYLQAEG 190 200 210 220 230 240 GGDRQLTDRE KEIIRQAAVQ QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS 250 260 270 280 290 300 KAPNASNLKI VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP 310 320 330 340 350 360 TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE IKDKEEVQRK 370 380 390 400 410 420 RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP GYGYSNYGFP PYGGITFHPG 430 440 450 460 470 480 VTKSNAGVTH GTINTKFKNG PKDCAKSDDE ESLTLPEKET EGEGPSLPMA CTKTEPIALA 490 500 510 520 530 540 STMEDKEQDM GFQDNLFLEK ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD 550 560 570 580 590 600 SVLHLAIIHL HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV 610 620 630 640 650 660 GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA IHIAVMSNSL 670 680 690 700 710 720 PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL LLEGDAHVDS TTYDGTTPLH 730 740 750 760 770 780 IAAGRGSTRL AALLKAAGAD PLVENFEPLY DLDDSWEKAG EDEGVVPGTT PLDMAANWQV 790 800 810 820 830 840 FDILNGKPYE PVFTSDDILP QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL 850 860 870 880 890 900 NNAFRLSPAP SKTLMDNYEV SGGTIKELME ALQQMGYTEA IEVIQAAFRT PATTASSPVT 910 920 930 940 950 960 TAQVHCLPLS SSSTRQHIDE LRDSDSVCDS GVETSFRKLS FTESLTGDSP LLSLNKMPHG 970 YGQEGPIEGK I
	Isoform 2 (p84) [UniParc]. Checksum: 51B98D66F21BF5EC	FASTA	781	84,817
	10 20 30 40 50 60 MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ RGFRFRYVCE 70 80 90 100 110 120 GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN GKNIHLHAHS LVGKHCEDGV 130 140 150 160 170 180 CTVTAGPKDM VVGFANLGIL HVTKKKVFET LEARMTEACI RGYNPGLLVH SDLAYLQAEG 190 200 210 220 230 240 GGDRQLTDRE KEIIRQAAVQ QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS 250 260 270 280 290 300 KAPNASNLKI VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP 310 320 330 340 350 360 TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE IKDKEEVQRK 370 380 390 400 410 420 RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP GYGYSNYGFP PYGGITFHPG 430 440 450 460 470 480 VTKSNAGVTH GTINTKFKNG PKDCAKSDDE ESLTLPEKET EGEGPSLPMA CTKTEPIALA 490 500 510 520 530 540 STMEDKEQDM GFQDNLFLEK ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD 550 560 570 580 590 600 SVLHLAIIHL HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV 610 620 630 640 650 660 GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA IHIAVMSNSL 670 680 690 700 710 720 PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL LLEGDAHVDS TTYDGTTPLH 730 740 750 760 770 780 IAAGRGSTRL AALLKAAGAD PLVENFEPLY DLDDSWEKAG EDEGVVPGTT PLDMAANWQG T
	Isoform 3 (p98) [UniParc]. Checksum: 8445F5C4CA02D7E4	FASTA	894	97,413
	10 20 30 40 50 60 MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ RGFRFRYVCE 70 80 90 100 110 120 GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN GKNIHLHAHS LVGKHCEDGV 130 140 150 160 170 180 CTVTAGPKDM VVGFANLGIL HVTKKKVFET LEARMTEACI RGYNPGLLVH SDLAYLQAEG 190 200 210 220 230 240 GGDRQLTDRE KEIIRQAAVQ QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS 250 260 270 280 290 300 KAPNASNLKI VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP 310 320 330 340 350 360 TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE IKDKEEVQRK 370 380 390 400 410 420 RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP GYGYSNYGFP PYGGITFHPG 430 440 450 460 470 480 VTKSNAGVTH GTINTKFKNG PKDCAKSDDE ESLTLPEKET EGEGPSLPMA CTKTEPIALA 490 500 510 520 530 540 STMEDKEQDM GFQDNLFLEK ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD 550 560 570 580 590 600 SVLHLAIIHL HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV 610 620 630 640 650 660 GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA IHIAVMSNSL 670 680 690 700 710 720 PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL LLEGDAHVDS TTYDGTTPLH 730 740 750 760 770 780 IAAGRGSTRL AALLKAAGAD PLVENFEPLY DLDDSWEKAG EDEGVVPGTT PLDMAANWQV 790 800 810 820 830 840 FDILNGKPYE PVFTSDDILP QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL 850 860 870 880 890 NNAFRLSPAP SKTLMDNYEM NSGIVTASVT VVWRHPSANS ALQSLLLETA HCYL
	Isoform 4 [UniParc]. Checksum: 09E32E7A3B63F46A	FASTA	356	39,756
	10 20 30 40 50 60 MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ RGFRFRYVCE 70 80 90 100 110 120 GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN GKNIHLHAHS LVGKHCEDGV 130 140 150 160 170 180 CTVTAGPKDM VVGFANLGIL HVTKKKVFET LEARMTEACI RGYNPGLLVH SDLAYLQAEG 190 200 210 220 230 240 GGDRQLTDRE KEIIRQAAVQ QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS 250 260 270 280 290 300 KAPNASNLKI VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP 310 320 330 340 350 TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE IKGTWV
	Isoform 5 (P70) (I-kappa-B gamma) [UniParc]. Checksum: 1B79975F022DF4E2	FASTA	607	64,782
	10 20 30 40 50 60 MPNFSDSFGG GSGAGAGGGG MFGSGGGGGS TGSPGPGYGY SNYGFPPYGG ITFHPGVTKS 70 80 90 100 110 120 NAGVTHGTIN TKFKNGPKDC AKSDDEESLT LPEKETEGEG PSLPMACTKT EPIALASTME 130 140 150 160 170 180 DKEQDMGFQD NLFLEKALQL ARRHANALFD YAVTGDVKML LAVQRHLTAV QDENGDSVLH 190 200 210 220 230 240 LAIIHLHAQL VRDLLEVTSG LISDDIINMR NDLYQTPLHL AVITKQEDVV EDLLRVGADL 250 260 270 280 290 300 SLLDRWGNSV LHLAAKEGHD RILSILLKSR KAAPLIDHPN GEGLNAIHIA VMSNSLPCLL 310 320 330 340 350 360 LLVAAGAEVN AQEQKSGRTA LHLAVEYDNI SLAGCLLLEG DAHVDSTTYD GTTPLHIAAG 370 380 390 400 410 420 RGSTRLAALL KAAGADPLVE NFEPLYDLDD SWEKAGEDEG VVPGTTPLDM AANWQVFDIL 430 440 450 460 470 480 NGKPYEPVFT SDDILPQGDM KQLTEDTRLQ LCKLLEIPDP DKNWATLAQK LGLGILNNAF 490 500 510 520 530 540 RLSPAPSKTL MDNYEVSGGT IKELMEALQQ MGYTEAIEVI QAAFRTPATT ASSPVTTAQV 550 560 570 580 590 600 HCLPLSSSST RQHIDELRDS DSVCDSGVET SFRKLSFTES LTGDSPLLSL NKMPHGYGQE GPIEGKI
	Isoform 6 (p63) (I-kappa-B gamma-1) [UniParc]. Checksum: C7384490B44048FC	FASTA	530	56,580
	10 20 30 40 50 60 MPNFSDSFGG GSGAGAGGGG MFGSGGGGGS TGSPGPGYGY SNYGFPPYGG ITFHPGVTKS 70 80 90 100 110 120 NAGVTHGTIN TKFKNGPKDC AKSDDEESLT LPEKETEGEG PSLPMACTKT EPIALASTME 130 140 150 160 170 180 DKEQDMGFQD NLFLEKALQL ARRHANALFD YAVTGDVKML LAVQRHLTAV QDENGDSVLH 190 200 210 220 230 240 LAIIHLHAQL VRDLLEVTSG LISDDIINMR NDLYQTPLHL AVITKQEDVV EDLLRVGADL 250 260 270 280 290 300 SLLDRWGNSV LHLAAKEGHD RILSILLKSR KAAPLIDHPN GEGLNAIHIA VMSNSLPCLL 310 320 330 340 350 360 LLVAAGAEVN AQEQKSGRTA LHLAVEYDNI SLAGCLLLEG DAHVDSTTYD GTTPLHIAAG 370 380 390 400 410 420 RGSTRLAALL KAAGADPLVE NFEPLYDLDD SWEKAGEDEG VVPGTTPLDM AANWQVFDIL 430 440 450 460 470 480 NGKPYEPVFT SDDILPQGDM KQLTEDTRLQ LCKLLEIPDP DKNWATLAQK LGLGILNNAF 490 500 510 520 530 RLSPAPSKTL MDNYEMNSGI VTASVTVVWR HPSANSALQS LLLETAHCYL
	Isoform 7 (p55) (I-kappa-B gamma-2) [UniParc]. Checksum: DEA2D2B56CDDC6D3	FASTA	417	43,983
	10 20 30 40 50 60 MPNFSDSFGG GSGAGAGGGG MFGSGGGGGS TGSPGPGYGY SNYGFPPYGG ITFHPGVTKS 70 80 90 100 110 120 NAGVTHGTIN TKFKNGPKDC AKSDDEESLT LPEKETEGEG PSLPMACTKT EPIALASTME 130 140 150 160 170 180 DKEQDMGFQD NLFLEKALQL ARRHANALFD YAVTGDVKML LAVQRHLTAV QDENGDSVLH 190 200 210 220 230 240 LAIIHLHAQL VRDLLEVTSG LISDDIINMR NDLYQTPLHL AVITKQEDVV EDLLRVGADL 250 260 270 280 290 300 SLLDRWGNSV LHLAAKEGHD RILSILLKSR KAAPLIDHPN GEGLNAIHIA VMSNSLPCLL 310 320 330 340 350 360 LLVAAGAEVN AQEQKSGRTA LHLAVEYDNI SLAGCLLLEG DAHVDSTTYD GTTPLHIAAG 370 380 390 400 410 RGSTRLAALL KAAGADPLVE NFEPLYDLDD SWEKAGEDEG VVPGTTPLDM AANWQGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the p50 DNA binding subunit of NF-kappa B: homology to rel and dorsal." Ghosh S., Gifford A.M., Riviere L.R., Tempst P., Nolan G.P., Baltimore D. Cell 62:1019-1029(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Lung and Spleen.
[2]	"I kappa B gamma, a 70 kd protein identical to the C-terminal half of p110 NF-kappa B: a new member of the I kappa B family." Inoue J., Kerr L.D., Kakizuka A., Verma I.M. Cell 68:1109-1120(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION.
[3]	"The activity of a 70 kilodalton I kappa B molecule identical to the carboxyl terminus of the p105 NF-kappa B precursor is modulated by protein kinase A." Gerondakis S., Morrice N., Richardson I.B., Wettenhall R., Fecondo J., Grumont R.J. Cell Growth Differ. 4:617-627(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PARTIAL PROTEIN SEQUENCE.
[4]	"Alternate RNA splicing of murine nfkb1 generates a nuclear isoform of the p50 precursor NF-kappa B1 that can function as a transactivator of NF-kappa B-regulated transcription." Grumont R.J., Fecondo J., Gerondakis S. Mol. Cell. Biol. 14:8460-8470(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[5]	"Mus musculus transcription factor NF-kappa-B DNA binding subunit(p105) mRNA, complete cds." Ohara O., Kitamura H., Nakagawa T. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6CrSlc. Tissue: Spleen.
[6]	Bleich A., Hedrich H.J., Schlegelberger B., Maehler M. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C3H/HeJBir and C57BL/6J.
[7]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] (ISOFORMS 1 AND 4). Tissue: Brain and Embryo.
[9]	Gerhauser I., Ulrich R., Baumgartner W. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-129. Strain: C57BL/6. Tissue: Lung carcinoma.
[10]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-971 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-971 (ISOFORM 1). Strain: C57BL/6J and NOD. Tissue: Inner ear, Kidney and Spleen.
[11]	"Alternative splicing of RNA transcripts encoded by the murine p105 NF-kappa B gene generates I kappa B gamma isoforms with different inhibitory activities." Grumont R.J., Gerondakis S. Proc. Natl. Acad. Sci. U.S.A. 91:4367-4371(1994) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), SUBCELLULAR LOCATION.
[12]	"Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome." Lin L., DeMartino G.N., Greene W.C. Cell 92:819-828(1998) [PubMed] [Europe PMC] [Abstract] Cited for: COTRANSLATIONAL FOLDING OF P105.
[13]	"A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory stimuli, negatively regulates nuclear factor-kappaB in the nuclei." Yamazaki S., Muta T., Takeshige K. J. Biol. Chem. 276:27657-27662(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NFKBIZ.
[14]	"Peptide-induced negative selection of thymocytes activates transcription of an NF-kappa B inhibitor." Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T., Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L., Clayton L.K. Mol. Cell 9:637-648(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NFKBID.
[15]	"A defect in nucleosome remodeling prevents IL-12(p35) gene transcription in neonatal dendritic cells." Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D., Willems F., Goldman M. J. Exp. Med. 199:1011-1016(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX.
[16]	"Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible nuclear protein IkappaBzeta." Yamamoto M., Yamazaki S., Uematsu S., Sato S., Hemmi H., Hoshino K., Kaisho T., Kuwata H., Takeuchi O., Takeshige K., Saitoh T., Yamaoka S., Yamamoto N., Yamamoto S., Muta T., Takeda K., Akira S. Nature 430:218-222(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NFKBIZ.
[17]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, MASS SPECTROMETRY. Tissue: Melanoma.
[18]	"Structure of NF-kappa B p50 homodimer bound to a kappa B site." Ghosh G., van Duyne G., Ghosh S., Sigler P.B. Nature 373:303-310(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-364.
[19]	"The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits." Huang D.B., Huxford T., Chen Y.Q., Ghosh G. Structure 5:1427-1436(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 245-350.
[20]	"The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation." Huxford T., Huang D.B., Malek S., Ghosh G. Cell 95:759-770(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 245-363.
[21]	"Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA." Chen F.E., Huang D.B., Chen Y.Q., Ghosh G. Nature 391:410-413(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 39-350.
[22]	"The X-ray crystal structure of the NF-kappa B p50.p65 heterodimer bound to the interferon beta -kappa B site." Berkowitz B., Huang D.B., Chen-Park F.E., Sigler P.B., Ghosh G. J. Biol. Chem. 277:24694-24700(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 39-350.
[23]	"The kappa B DNA sequence from the HIV long terminal repeat functions as an allosteric regulator of HIV transcription." Chen-Park F.E., Huang D.B., Noro B., Thanos D., Ghosh G. J. Biol. Chem. 277:24701-24708(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-350.
[24]	"Crystal structure of NF-kappaB (p50)2 complexed to a high-affinity RNA aptamer." Huang D.B., Vu D., Cassiday L.A., Zimmerman J.M., Maher L.J. III, Ghosh G. Proc. Natl. Acad. Sci. U.S.A. 100:9268-9273(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-351 HOMODIMER COMPLEXED WITH RNA APTAMER.
[25]	"X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites." Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G. J. Mol. Biol. 373:723-734(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH RELB.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M57999 mRNA. Translation: AAA40415.1.
S89033 mRNA. Translation: AAB21851.1.
S66656 mRNA. Translation: AAB28573.1.
AB119195 mRNA. Translation: BAC84979.1.
AY521462 mRNA. Translation: AAS00547.1.
AY521463 mRNA. Translation: AAS00548.1.
CH466532 Genomic DNA. Translation: EDL12143.1.
BC050841 mRNA. Translation: AAH50841.1.
BC138535 mRNA. Translation: AAI38536.1.
BC138536 mRNA. Translation: AAI38537.1.
AY423849 mRNA. Translation: AAR00341.1.
AK052726 mRNA. Translation: BAC35117.1. Different initiation.
AK089660 mRNA. Translation: BAE43399.1.
AK157915 mRNA. Translation: BAE34261.1.

IPI

IPI00113873.
IPI00221649.
IPI00719865.
IPI00719890.
IPI00742428.
IPI00742440.
IPI01007628.

PIR

A35697.

RefSeq

NP_032715.2. NM_008689.2.

UniGene

Mm.256765.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BFS	X-ray	2.20	A	245-350	[»]
1IKN	X-ray	2.30	C	245-363	[»]
1LE5	X-ray	2.75	B/F	39-350	[»]
1LE9	X-ray	3.00	B/F	39-350	[»]
1LEI	X-ray	2.70	B	39-350	[»]
1NFK	X-ray	2.30	A/B	39-363	[»]
1OOA	X-ray	2.45	A/B	39-363	[»]
1U36	X-ray	1.89	A	245-350	[»]
1U3J	X-ray	1.90	A	245-350	[»]
1U3Y	X-ray	1.90	A	245-350	[»]
1U3Z	X-ray	1.90	A	245-350	[»]
1U41	X-ray	2.20	A/B/C/D	245-350	[»]
1U42	X-ray	2.70	A	245-350	[»]
1VKX	X-ray	2.90	B	39-350	[»]
2I9T	X-ray	2.80	B	39-350	[»]
2V2T	X-ray	3.05	B	38-363	[»]
3JV4	X-ray	3.15	B/D/F	245-359	[»]

ProteinModelPortal

P25799.

SMR

P25799. Positions 39-350, 460-786, 802-885.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-85N.

IntAct

P25799. 8 interactions.

MINT

MINT-236136.

PTM databases

PhosphoSite

P25799.

Proteomic databases

PaxDb

P25799.

PRIDE

P25799.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163.
ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163.

GeneID

18033.

KEGG

mmu:18033.

UCSC

uc008rly.1. mouse.
uc012cyf.1. mouse.

Organism-specific databases

CTD

4790.

MGI

MGI:97312. Nfkb1.

Phylogenomic databases

eggNOG

COG0666.

GeneTree

ENSGT00500000044765.

HOVERGEN

HBG052613.

InParanoid

B2RRQ6.

KO

K02580.

OMA

PLDMAAN.

OrthoDB

EOG4SN1MX.

Gene expression databases

Bgee

P25799.

Genevestigator

P25799.

Family and domain databases

Gene3D

1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT_TIG_rcpt.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]

Pfam

PF12796. Ank_2. 2 hits.
PF00531. Death. 1 hit.
PF00554. RHD. 1 hit.
[Graphical view]

PRINTS

PR00057. NFKBTNSCPFCT.

SMART

SM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF47986. DEATH_like. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF49417. P53_like_DNA_bnd. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50017. DEATH_DOMAIN. False negative.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1949489.

ChiTaRS

NFKB1. mouse.

EvolutionaryTrace

P25799.

NextBio

293121.

SOURCE

Search...

Entry information

Entry name

NFKB1_MOUSE

Accession

Primary (citable) accession number: P25799
Secondary accession number(s): B2RRQ6 , Q3TZE8, Q3V2V6, Q6TDG8, Q75ZL1, Q80Y21, Q8C712

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 152 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program