Reviewed, UniProtKB/Swiss-Prot O15111 (IKKA_HUMAN)

Names and origin

Protein names

Recommended name:
    Inhibitor of nuclear factor kappa-B kinase subunit alpha
      Short name=I-kappa-B kinase alpha
      Short name=IkBKA
      Short name=IKK-alpha
      Short name=IKK-A
      Short name=IkappaB kinase
    EC=2.7.11.10
Alternative name(s):
    I-kappa-B kinase 1
      Short name=IKK1
    Conserved helix-loop-helix ubiquitous kinase
    Nuclear factor NF-kappa-B inhibitor kinase alpha
      Short name=NFKBIKA
    Transcription factor 16
      Short name=TCF-16

Gene names

Name:	CHUK
Synonyms:	IKKA, TCF16

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

Protein attributes

Sequence length	745 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts as part of the IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. Also phosphorylates NCOA3. Phosphorylates 'Ser-10' of histone H3 at NF-kappa-B-regulated promoters during inflammatory responses triggered by cytokines. Ref.16
Catalytic activity	ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein].
Enzyme regulation	Activated when phosphorylated and inactivated when dephosphorylated.
Subunit structure	Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex. Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Directly interacts with IKK-gamma/NEMO and TRPC4AP By similarity. May interact with TRAF2. Interacts with NALP2. May interact with MAVS/IPS1. Interacts with ARRB1 and ARRB2. Ref.14 Ref.17 Ref.18 Ref.19
Subcellular location	Cytoplasm. Nucleus. Note: Shuttles between the cytoplasm and the nucleus. Ref.16
Tissue specificity	Widely expressed.
Post-translational modification	Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated. Ref.16 Ref.9 Ref.10 Ref.12
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	I-kappaB phosphorylation Ref.2 Traceable author statement. Source: ProtInc immune response Ref.3 Traceable author statement. Source: ProtInc
Cellular component	cytosol Ref.10 Inferred from Experiment. Source: Reactome nucleus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW IkappaB kinase activity Ref.2 Traceable author statement. Source: ProtInc identical protein binding Ref.9 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-81249,EBI-81249
FKBP5	Q13451	1	EBI-81249,EBI-306914
IKBKB	O14920	3	EBI-81249,EBI-81266
IKBKG	Q9Y6K9	3	EBI-81249,EBI-81279
MAP3K14	Q99558	2	EBI-81249,EBI-358011
MAVS	Q7Z434	1	EBI-81249,EBI-995373
NCOA3	Q9Y6Q9	1	EBI-81249,EBI-81196
NFKBIA	P25963	3	EBI-81249,EBI-307386
RELA	Q04206	1	EBI-81249,EBI-73886

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 745	745	Inhibitor of nuclear factor kappa-B kinase subunit alpha		PRO_0000086011
Regions
	Domain	15 – 302	288	Protein kinase
	Domain	455 – 476	22	Leucine-zipper
	Nucleotide binding	21 – 29	9	ATP By similarity
	Region	738 – 743	6	NEMO-binding
Sites
	Active site	144	1	Proton acceptor By similarity
	Binding site	44	1	ATP By similarity
Amino acid modifications
	Modified residue	23	1	Phosphothreonine; by PKB/AKT1 Ref.10
	Modified residue	176	1	Phosphoserine; by MAP3K14 Ref.9
Natural variations
	Natural variant	126	1	S → C: dbSNP rs34427437. Ref.21		VAR_040565
	Natural variant	155	1	V → A: dbSNP rs2230803. Ref.21		VAR_040566
	Natural variant	268	1	I → V: dbSNP rs2230804. Ref.21 Ref.3 Ref.5 Ref.6		VAR_021359
Experimental info
	Mutagenesis	23	1	T → A: Loss of phosphorylation and decrease of kinase activity. Ref.10
	Mutagenesis	44	1	K → A: Loss of kinase activity. Ref.3 Ref.1
	Mutagenesis	44	1	K → M: Loss of autophosphorylation. Ref.3 Ref.1
	Mutagenesis	176	1	S → A: Loss of phosphorylation and of activity. Ref.9 Ref.3
	Mutagenesis	176	1	S → E: Full activation. Ref.9 Ref.3
	Mutagenesis	179	1	T → A: No change in phosphorylation. Ref.9
	Mutagenesis	180	1	S → A: No change in phosphorylation. Ref.9
	Sequence conflict	543	1	E → G in AAC51671. Ref.2
	Sequence conflict	604	1	L → R in AAC50713. Ref.7
	Sequence conflict	679 – 680	2	TS → AY in AAC50713. Ref.7
	Sequence conflict	684	1	P → A Ref.3
	Sequence conflict	684	1	P → A in AAC50713. Ref.7
	Sequence conflict	686 – 687	2	TS → DL in AAC50713. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	O15111-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 7A90B59BC98A56C2	FASTA	745	84,654
	10 20 30 40 50 60 MERPPGLRPG AGGPWEMRER LGTGGFGNVC LYQHRELDLK IAIKSCRLEL STKNRERWCH 70 80 90 100 110 120 EIQIMKKLNH ANVVKACDVP EELNILIHDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ 130 140 150 160 170 180 ILSLLSDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKII HKIIDLGYAK DVDQGSLCTS 190 200 210 220 230 240 FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK 250 260 270 280 290 300 CIFACEEMSG EVRFSSHLPQ PNSLCSLIVE PMENWLQLML NWDPQQRGGP VDLTLKQPRC 310 320 330 340 350 360 FVLMDHILNL KIVHILNMTS AKIISFLLPP DESLHSLQSR IERETGINTG SQELLSETGI 370 380 390 400 410 420 SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSDCVNYI VQDSKIQLPI 430 440 450 460 470 480 IQLRKVWAEA VHYVSGLKED YSRLFQGQRA AMLSLLRYNA NLTKMKNTLI SASQQLKAKL 490 500 510 520 530 540 EFFHKSIQLD LERYSEQMTY GISSEKMLKA WKEMEEKAIH YAEVGVIGYL EDQIMSLHAE 550 560 570 580 590 600 IMELQKSPYG RRQGDLMESL EQRAIDLYKQ LKHRPSDHSY SDSTEMVKII VHTVQSQDRV 610 620 630 640 650 660 LKELFGHLSK LLGCKQKIID LLPKVEVALS NIKEADNTVM FMQGKRQKEI WHLLKIACTQ 670 680 690 700 710 720 SSARSLVGSS LEGAVTPQTS AWLPPTSAEH DHSLSCVVTP QDGETSAQMI EENLNCLGHL 730 740 STIIHEANEE QGNSMMNLDW SWLTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of an IkappaB kinase." Regnier C.H., Song H.Y., Gao X., Goeddel D.V., Cao Z., Rothe M. Cell 90:373-383(1997) [PubMed: 9244310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-44. Tissue: T-cell.
[2]	"A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB." DiDonato J.A., Hayakawa M., Rothwarf D.M., Zandi E., Karin M. Nature 388:548-554(1997) [PubMed: 9252186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]	"IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation." Mercurio F., Zhu H., Murray B.W., Shevchenko A., Bennett B.L., Li J.W., Young D.B., Barbosa M., Mann M., Manning A., Rao A. Science 278:860-866(1997) [PubMed: 9346484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT VAL-268, MUTAGENESIS OF LYS-44 AND SER-176. Tissue: Cervix carcinoma.
[4]	"IkappaB kinase-alpha and -beta genes are coexpressed in adult and embryonic tissues but localized to different human chromosomes." Hu M.C.-T., Wang Y.-P. Gene 222:31-40(1998) [PubMed: 9813230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[5]	SeattleSNPs variation discovery resource Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-268.
[6]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-268.
[7]	"CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase catalytic domain." Connelly M.A., Marcu K.B. Cell. Mol. Biol. Res. 41:537-549(1995) [PubMed: 8777433] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-745. Tissue: Cervix carcinoma.
[8]	"IKAP is a scaffold protein of the IkappaB kinase complex." Cohen L., Henzel W.J., Baeuerle P.A. Nature 395:292-296(1998) [PubMed: 9751059] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH IKBKB; NFKBIA; RELA; IKBKAP AND MAP3K14.
[9]	"NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176." Ling L., Cao Z., Goeddel D.V. Proc. Natl. Acad. Sci. U.S.A. 95:3792-3797(1998) [PubMed: 9520446] [Abstract] Cited for: PHOSPHORYLATION AT SER-176, MUTAGENESIS OF SER-176; THR-179 AND SER-180.
[10]	"NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase." Ozes O.N., Mayo L.D., Gustin J.A., Pfeffer S.R., Pfeffer L.M., Donner D.B. Nature 401:82-85(1999) [PubMed: 10485710] [Abstract] Cited for: PHOSPHORYLATION AT THR-23, MUTAGENESIS OF THR-23.
[11]	"Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation." Delhase M., Hayakawa M., Chen Y., Karin M. Science 284:309-313(1999) [PubMed: 10195894] [Abstract] Cited for: IKKA-IKKB BINDING.
[12]	"Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase." Nemoto S., DiDonato J.A., Lin A. Mol. Cell. Biol. 18:7336-7343(1998) [PubMed: 9819420] [Abstract] Cited for: IKK PHOSPHORYLATION.
[13]	"The I kappa B/NF-kappa B system: a key determinant of mucosal inflammation and protection." Jobin C., Sartor R.B. Am. J. Physiol. 278:C451-C462(2000) [PubMed: 10712233] [Abstract] Cited for: REVIEW.
[14]	"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase." Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W. Mol. Cell. Biol. 22:3549-3561(2002) [PubMed: 11971985] [Abstract] Cited for: SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; NCOA3; IKKB AND IKBKG.
[15]	"Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation." Tegethoff S., Behlke J., Scheidereit C. Mol. Cell. Biol. 23:2029-2041(2003) [PubMed: 12612076] [Abstract] Cited for: COMPOSITION OF THE IKK COMPLEX.
[16]	"Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression." Yamamoto Y., Verma U.N., Prajapati S., Kwak Y.T., Gaynor R.B. Nature 423:655-659(2003) [PubMed: 12789342] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[17]	"PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages." Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C., Reed J.C. J. Biol. Chem. 279:51897-51907(2004) [PubMed: 15456791] [Abstract] Cited for: INTERACTION WITH NALP2.
[18]	"beta-Arrestin inhibits NF-kappaB activity by means of its interaction with the NF-kappaB inhibitor IkappaBalpha." Witherow D.S., Garrison T.R., Miller W.E., Lefkowitz R.J. Proc. Natl. Acad. Sci. U.S.A. 101:8603-8607(2004) [PubMed: 15173580] [Abstract] Cited for: INTERACTION WITH ARRB1 AND ARRB2.
[19]	"Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus." Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J. Nature 437:1167-1172(2005) [PubMed: 16177806] [Abstract] Cited for: INTERACTION WITH MAVS.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-126; ALA-155 AND VAL-268.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF012890 mRNA. Translation: AAC51662.1.
AF009225 mRNA. Translation: AAC51671.1.
AF080157 mRNA. Translation: AAD08996.1.
AY652653 Genomic DNA. Translation: AAT49098.1.
AL138921 Genomic DNA. Translation: CAH72401.1.
U22512 mRNA. Translation: AAC50713.1.

IPI

IPI00005104.

RefSeq

NP_001269.3.

UniGene

Hs.198998

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BRT	X-ray	2.25	A/C	732-745	[»]

SMR

O15111. Positions 20-289, 709-744.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27526N.

IntAct

O15111. 41 interactions.

STRING

O15111.

PTM databases

PhosphoSite

O15111.

Proteomic databases

PRIDE

O15111.

Genome annotation databases

Ensembl

ENST00000370397; ENSP00000359424; ENSG00000213341; Homo sapiens. [Genome view]

GeneID

1147.

KEGG

hsa:1147.

UCSC

uc001kqp.1. human.

Organism-specific databases

CTD

1147.

GeneCards

GC10M101938.

H-InvDB

HIX0009119.

HGNC

HGNC:1974. CHUK.

HPA

CAB004240.
CAB018564.
HPA001402.

MIM

600664. gene.

PharmGKB

PA26510.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14699.

HOGENOM

HBG358635.

HOVERGEN

O15111.

InParanoid

O15111.

Enzyme and pathway databases

BRENDA

2.7.11.10. 247.

Pathway_Interaction_DB

nfkappabalternativepathway. Alternative NF-kappaB pathway.
bcr_5pathway. BCR signaling pathway.
nfkappabcanonicalpathway. Canonical NF-kappaB pathway.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
faspathway. FAS signaling pathway (CD95).
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
foxopathway. FoxO family signaling.
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
il1pathway. IL1-mediated signaling events.
avb3_opn_pathway. Osteopontin-mediated events.
p75ntrpathway. p75(NTR)-mediated signaling.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
tnfpathway. TNF receptor signaling pathway.
trail_pathway. TRAIL signaling pathway.

Reactome

REACT_11061. Signalling by NGF.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

O15111.

Bgee

O15111.

CleanEx

HS_CHUK.

Genevestigator

O15111.

GermOnline

ENSG00000107566. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

4772.

SOURCE

Search...

Entry information

Entry name

IKKA_HUMAN

Accession

Primary (citable) accession number: O15111
Secondary accession number(s): O14666 , Q13132, Q5W0I4, Q92467

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 114 of the entry and version 1 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.