Reviewed, UniProtKB/Swiss-Prot P0C0L5 (CO4B_HUMAN)

Names and origin

Protein names

Recommended name:
    Complement C4-B
Alternative name(s):
    Basic complement C4
    C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3
Cleaved into the following 6 chains:
    1- Recommended name:
            Complement C4 beta chain
    2- Recommended name:
            Complement C4-B alpha chain
    3- Recommended name:
            C4a anaphylatoxin
    4- Recommended name:
            C4b-B
    5- Recommended name:
            C4d-B
    6- Recommended name:
            Complement C4 gamma chain

Gene names

Name:	C4B
Synonyms:	CO4, CPAMD3

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	1744 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	C4 plays a central role in the activation of the classical pathway of the complement system. It is processed by activated C1 which removes from the alpha chain the C4a anaphylatoxin. The remaining alpha chain fragment C4b is the major activation product and is an essential subunit of the C3 convertase (C4b2a) and the C5 convertase (C3bC4b2a) enzymes of the classical complement pathway. Derived from proteolytic degradation of complement C4, C4a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.
Subunit structure	Circulates in blood as a disulfide-linked trimer of an alpha, beta and gamma chain.
Subcellular location	Secreted.
Post-translational modification	Prior to secretion, the single-chain precursor is enzymatically cleaved to yield the non-identical chains (alpha, beta and gamma). During activation, the alpha chain is cleaved by C1 into C4a and C4b, and C4b stays linked to the beta and gamma chains. Further degradation of C4b by C1 into the inactive fragments C4c and C4d blocks the generation of C3 convertase.
Polymorphism	Human complement component C4 is polymorphic at two loci, C4A and C4B. 13 alleles of C4A and 22 alleles of C4B have been detected. The C4A alleles carry the Rodgers (Rg) while the C4B alleles carry the Chido (Ch) blood group antigens.
Miscellaneous	C4A allotypes react more rapidly with the amino group of peptide antigens while C4B allotypes react more rapidly with the hydroxyl group of carbohydrate antigens.
Sequence similarities	Contains 1 anaphylatoxin-like domain. Contains 1 NTR domain.
Sequence caution	The sequence AAA99717.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Complement pathway Immune response Inflammatory response Innate immunity
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Blood group antigen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Sulfation Thioester bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: InterPro
Molecular function	endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19
	Chain	20 – 675	656	Complement C4 beta chain		PRO_0000042699
	Propeptide	676 – 679	4			PRO_0000042700
	Chain	680 – 1446	767	Complement C4-B alpha chain		PRO_0000042701
	Chain	680 – 756	77	C4a anaphylatoxin		PRO_0000042702
	Chain	757 – 1446	690	C4b-B		PRO_0000042703
	Chain	957 – 1336	380	C4d-B		PRO_0000042704
	Propeptide	1447 – 1453	7			PRO_0000042705
	Chain	1454 – 1744	291	Complement C4 gamma chain		PRO_0000042706
Regions
	Domain	702 – 736	35	Anaphylatoxin-like
	Domain	1595 – 1742	148	NTR
Amino acid modifications
	Modified residue	1417	1	Sulfotyrosine
	Modified residue	1420	1	Sulfotyrosine
	Modified residue	1422	1	Sulfotyrosine
	Glycosylation	226	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	862	1	N-linked (GlcNAc...) Potential
	Glycosylation	1328	1	N-linked (GlcNAc...) Ref.14
	Glycosylation	1391	1	N-linked (GlcNAc...) Ref.13
	Disulfide bond	702 ↔ 728		By similarity
	Disulfide bond	703 ↔ 735		By similarity
	Disulfide bond	716 ↔ 736		By similarity
	Disulfide bond	1595 ↔ 1673		By similarity
	Disulfide bond	1618 ↔ 1742		By similarity
	Cross-link	1010 ↔ 1013		Isoglutamyl cysteine thioester (Cys-Gln)
Natural variations
	Natural variant	347	1	S → Y: dbSNP rs392610. Ref.2		VAR_023729
	Natural variant	907	1	A → T: dbSNP rs429329. Ref.1 Ref.3		VAR_023730
	Natural variant	1073	1	D → G in allotype C4B1 and allotype C4B3. dbSNP rs2258218. Ref.8		VAR_023731
	Natural variant	1176	1	N → S in allotype C4B1, allotype C4B3 and allotype C4B5. dbSNP rs2746414. Ref.8		VAR_023732
	Natural variant	1201	1	S → T in allotype C4B. Ref.8 Ref.10		VAR_023733
	Natural variant	1207	1	V → A in allotype C4B1, allotype C4B2 and allotype C4B3. dbSNP rs2229403. Ref.8 Ref.10		VAR_023734
	Natural variant	1210	1	L → R in allotype C4B1, allotype C4B2 and allotype C4B3. dbSNP rs2229409. Ref.8 Ref.10		VAR_023735
	Natural variant	1286	1	S → A: dbSNP rs9501603. Ref.8 Ref.10		VAR_023736
Experimental info
	Sequence conflict	980 – 981	2	VT → LQ in AAA99717. Ref.1
	Sequence conflict	1013	1	Q → E AA sequence Ref.7
	Sequence conflict	1013	1	Q → E AA sequence Ref.8
	Sequence conflict	1013	1	Q → E AA sequence Ref.9
	Sequence conflict	1109 – 1110	2	SQ → IA AA sequence Ref.8
	Sequence conflict	1271	1	H → V AA sequence Ref.8
	Sequence conflict	1271	1	H → V AA sequence Ref.10
	Sequence conflict	1300	1	R → V AA sequence Ref.8
	Sequence conflict	1300	1	R → V AA sequence Ref.10
	Sequence conflict	1317	1	I → F in AAA99717. Ref.1
	Sequence conflict	1654	1	T → RA in AAA99717. Ref.1
	Sequence conflict	1698	1	H → Q in AAA99717. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0C0L5-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: C5C7AD86D2EA05D8	FASTA	1,744	192,793
	10 20 30 40 50 60 MRLLWGLIWA SSFFTLSLQK PRLLLFSPSV VHLGVPLSVG VQLQDVPRGQ VVKGSVFLRN 70 80 90 100 110 120 PSRNNVPCSP KVDFTLSSER DFALLSLQVP LKDAKSCGLH QLLRGPEVQL VAHSPWLKDS 130 140 150 160 170 180 LSRTTNIQGI NLLFSSRRGH LFLQTDQPIY NPGQRVRYRV FALDQKMRPS TDTITVMVEN 190 200 210 220 230 240 SHGLRVRKKE VYMPSSIFQD DFVIPDISEP GTWKISARFS DGLESNSSTQ FEVKKYVLPN 250 260 270 280 290 300 FEVKITPGKP YILTVPGHLD EMQLDIQARY IYGKPVQGVA YVRFGLLDED GKKTFFRGLE 310 320 330 340 350 360 SQTKLVNGQS HISLSKAEFQ DALEKLNMGI TDLQGLRLYV AAAIIESPGG EMEEAELTSW 370 380 390 400 410 420 YFVSSPFSLD LSKTKRHLVP GAPFLLQALV REMSGSPASG IPVKVSATVS SPGSVPEVQD 430 440 450 460 470 480 IQQNTDGSGQ VSIPIIIPQT ISELQLSVSA GSPHPAIARL TVAAPPSGGP GFLSIERPDS 490 500 510 520 530 540 RPPRVGDTLN LNLRAVGSGA TFSHYYYMIL SRGQIVFMNR EPKRTLTSVS VFVDHHLAPS 550 560 570 580 590 600 FYFVAFYYHG DHPVANSLRV DVQAGACEGK LELSVDGAKQ YRNGESVKLH LETDSLALVA 610 620 630 640 650 660 LGALDTALYA AGSKSHKPLN MGKVFEAMNS YDLGCGPGGG DSALQVFQAA GLAFSDGDQW 670 680 690 700 710 720 TLSRKRLSCP KEKTTRKKRN VNFQKAINEK LGQYASPTAK RCCQDGVTRL PMMRSCEQRA 730 740 750 760 770 780 ARVQQPDCRE PFLSCCQFAE SLRKKSRDKG QAGLQRALEI LQEEDLIDED DIPVRSFFPE 790 800 810 820 830 840 NWLWRVETVD RFQILTLWLP DSLTTWEIHG LSLSKTKGLC VATPVQLRVF REFHLHLRLP 850 860 870 880 890 900 MSVRRFEQLE LRPVLYNYLD KNLTVSVHVS PVEGLCLAGG GGLAQQVLVP AGSARPVAFS 910 920 930 940 950 960 VVPTAAAAVS LKVVARGSFE FPVGDAVSKV LQIEKEGAIH REELVYELNP LDHRGRTLEI 970 980 990 1000 1010 1020 PGNSDPNMIP DGDFNSYVRV TASDPLDTLG SEGALSPGGV ASLLRLPRGC GEQTMIYLAP 1030 1040 1050 1060 1070 1080 TLAASRYLDK TEQWSTLPPE TKDHAVDLIQ KGYMRIQQFR KADGSYAAWL SRDSSTWLTA 1090 1100 1110 1120 1130 1140 FVLKVLSLAQ EQVGGSPEKL QETSNWLLSQ QQADGSFQDL SPVIHRSMQG GLVGNDETVA 1150 1160 1170 1180 1190 1200 LTAFVTIALH HGLAVFQDEG AEPLKQRVEA SISKANSFLG EKASAGLLGA HAAAITAYAL 1210 1220 1230 1240 1250 1260 SLTKAPVDLL GVAHNNLMAM AQETGDNLYW GSVTGSQSNA VSPTPAPRNP SDPMPQAPAL 1270 1280 1290 1300 1310 1320 WIETTAYALL HLLLHEGKAE MADQASAWLT RQGSFQGGFR STQDTVIALD ALSAYWIASH 1330 1340 1350 1360 1370 1380 TTEERGLNVT LSSTGRNGFK SHALQLNNRQ IRGLEEELQF SLGSKINVKV GGNSKGTLKV 1390 1400 1410 1420 1430 1440 LRTYNVLDMK NTTCQDLQIE VTVKGHVEYT MEANEDYEDY EYDELPAKDD PDAPLQPVTP 1450 1460 1470 1480 1490 1500 LQLFEGRRNR RRREAPKVVE EQESRVHYTV CIWRNGKVGL SGMAIADVTL LSGFHALRAD 1510 1520 1530 1540 1550 1560 LEKLTSLSDR YVSHFETEGP HVLLYFDSVP TSRECVGFEA VQEVPVGLVQ PASATLYDYY 1570 1580 1590 1600 1610 1620 NPERRCSVFY GAPSKSRLLA TLCSAEVCQC AEGKCPRQRR ALERGLQDED GYRMKFACYY 1630 1640 1650 1660 1670 1680 PRVEYGFQVK VLREDSRAAF RLFETKITQV LHFTKDVKAA ANQMRNFLVR ASCRLRLEPG 1690 1700 1710 1720 1730 1740 KEYLIMGLDG ATYDLEGHPQ YLLDSNSWIE EMPSERLCRS TRQRAACAQL NDFLQEYGTQ GCQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of the complement C4 gene from the HLA-A1, B8, C4AQ0, C4B1, DR3 haplotype." Ulgiati D., Townend D.C., Christiansen F.T., Dawkins R.L., Abraham L.J. Immunogenetics 43:250-252(1996) [PubMed: 8575831] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-907. Tissue: Blood.
[2]	"Sequence determination of 300 kilobases of the human class III MHC locus." Rowen L., Dankers C., Baskin D., Faust J., Loretz C., Ahearn M.E., Banta A., Swartzell S., Smith T.M., Spies T., Hood L. Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-347.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-907.
[4]	"Complete primary structure of human C4a anaphylatoxin." Moon K.E., Gorski J.P., Hugli T.E. J. Biol. Chem. 256:8685-8692(1981) [PubMed: 6167582] [Abstract] Cited for: PROTEIN SEQUENCE OF 680-756.
[5]	"Importance of the alpha 3-fragment of complement C4 for the binding with C4b-binding protein." Hessing M., van 't Veer C., Hackeng T.M., Bouma B.N., Iwanaga S. FEBS Lett. 271:131-136(1990) [PubMed: 1699796] [Abstract] Cited for: PROTEIN SEQUENCE OF 757-771 AND 980-990.
[6]	"The structural basis of the multiple forms of human complement component C4." Belt K.T., Carroll M.C., Porter R.R. Cell 36:907-914(1984) [PubMed: 6546707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 956-1336. Tissue: Liver.
[7]	"Amino acid sequence around the thiol and reactive acyl groups of human complement component C4." Campbell R.D., Gagnon J., Porter R.R. Biochem. J. 199:359-370(1981) [PubMed: 6978711] [Abstract] Cited for: PROTEIN SEQUENCE OF 957-1044.
[8]	"The chemical structure of the C4d fragment of the human complement component C4." Chakravarti D.N., Campbell R.D., Porter R.R. Mol. Immunol. 24:1187-1197(1987) [PubMed: 3696167] [Abstract] Cited for: PROTEIN SEQUENCE OF 957-1336, VARIANTS GLY-1073; SER-1176; THR-1201; ALA-1207; ARG-1210 AND ALA-1286.
[9]	"Sequence determination of the thiolester site of the fourth component of human complement." Harrison R.A., Thomas M.L., Tack B.F. Proc. Natl. Acad. Sci. U.S.A. 78:7388-7392(1981) [PubMed: 6950384] [Abstract] Cited for: PROTEIN SEQUENCE OF 990-1037.
[10]	"Amino acid sequence of a polymorphic segment from fragment C4d of human complement component C4." Chakravarti D.N., Campbell R.D., Gagnon J. FEBS Lett. 154:387-390(1983) [PubMed: 6832377] [Abstract] Cited for: PROTEIN SEQUENCE OF 1199-1304, VARIANTS THR-1201; ALA-1207; ARG-1210 AND ALA-1286.
[11]	"Identification of the site of sulfation of the fourth component of human complement." Hortin G., Sims H., Strauss A.W. J. Biol. Chem. 261:1786-1793(1986) [PubMed: 3944109] [Abstract] Cited for: PROTEIN SEQUENCE OF 1405-1431, SULFATION.
[12]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-226.
[13]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1391, MASS SPECTROMETRY. Tissue: Plasma.
[14]	"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry." Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A. J. Proteome Res. 5:1493-1503(2006) [PubMed: 16740002] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1328, MASS SPECTROMETRY. Tissue: Saliva.
[15]	"Structural basis of the polymorphism of human complement components C4A and C4B: gene size, reactivity and antigenicity." Yu C.Y., Belt K.T., Giles C.M., Campbell R.D., Porter R.R. EMBO J. 5:2873-2881(1986) [PubMed: 2431902] [Abstract] Cited for: STRUCTURAL BASIS OF POLYMORPHISM.
+	Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

Cross-references

Sequence databases
EMBLGenBankDDBJ	U24578 Genomic DNA. Translation: AAA99717.1. Sequence problems. AF019413 Genomic DNA. Translation: AAB67980.1. AL049547 Genomic DNA. Translation: CAB89302.1. K02404 mRNA. Translation: AAA59651.1.
IPI	IPI00654875.
PIR	B20807.
RefSeq	NP_001002029.3.
UniGene	Hs.534847
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P0C0L5.
Protein family/group databases
MEROPS	I39.951.
2-D gel databases
SWISS-2DPAGE	P0C0L5.
DOSAC-COBS-2DPAGE	P0C0L5.
Proteomic databases
PRIDE	P0C0L5.
Genome annotation databases
Ensembl	ENST00000414246; ENSP00000403377; ENSG00000236625; Homo sapiens. [Genome view] ENST00000449788; ENSP00000414200; ENSG00000236625; Homo sapiens. [Genome view]
GeneID	721.
KEGG	hsa:721.
Organism-specific databases
CTD	721.
GeneCards	GC06P032060.
HGNC	HGNC:1324. C4B.
MIM	120790. phenotype. 120820. gene.
Orphanet	101992. Immunodeficiency with a complement cascade protein anomaly.
PharmGKB	PA25904.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P0C0L5.
Gene expression databases
Genevestigator	P0C0L5.
GermOnline	ENSG00000204319. Homo sapiens.
Family and domain databases
InterPro	IPR009048. A-macroglobulin_rcpt-bd. IPR011626. A2M_comp. IPR002890. A2M_N. IPR011625. A2M_N_2. IPR000020. Anaphylatoxin/fibulin. IPR018081. Anaphylatoxin_. IPR001840. Anaphylatoxn. IPR001599. MacrogloblnA2. IPR019742. MacrogloblnA2_CS. IPR019565. MacrogloblnA2_thiol-ester-bond. IPR001134. Netrin_domain. IPR018933. Netrin_module_non-TIMP. IPR008930. Terpenoid_cyclase/PrenylTrfase. [Graphical view]
Gene3D	G3DSA:2.60.40.690. A-macroglobulin_rcpt-bd. 1 hit. G3DSA:1.20.91.20. Anaphylatoxin. 1 hit.
Pfam	PF00207. A2M. 1 hit. PF07678. A2M_comp. 1 hit. PF01835. A2M_N. 1 hit. PF07703. A2M_N_2. 1 hit. PF07677. A2M_recep. 1 hit. PF01821. ANATO. 1 hit. PF01759. NTR. 1 hit. PF10569. Thiol-ester_cl. 1 hit. [Graphical view]
PRINTS	PR00004. ANAPHYLATOXN.
SMART	SM00104. ANATO. 1 hit. SM00643. C345C. 1 hit. [Graphical view]
PROSITE	PS00477. ALPHA_2_MACROGLOBULIN. 1 hit. PS01177. ANAPHYLATOXIN_1. 1 hit. PS01178. ANAPHYLATOXIN_2. 1 hit. PS50189. NTR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

CO4B_HUMAN

Accession

Primary (citable) accession number: P0C0L5
Secondary accession number(s): P01028 , P78445, Q13160, Q13906, Q14033, Q14835, Q9NPK5, Q9UIP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 8, 2005
Last modified:	November 24, 2009
This is version 53 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.