P02749 (APOH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-2-glycoprotein 1

Alternative name(s):
APC inhibitor
Activated protein C-binding protein
Anticardiolipin cofactor
Apolipoprotein H
Short name=Apo-H
Beta-2-glycoprotein I
Short name=B2GPI
Short name=Beta(2)GPI

Gene names

Name:	APOH
Synonyms:	B2G1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	345 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	Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.
Subcellular location	Secreted.
Tissue specificity	Expressed by the liver and secreted in plasma.
Post-translational modification	N- and O-glycosylated. Ref.10 also reports glycosylation on 'Asn-188' for their allele. Ref.10 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Sequence similarities	Contains 4 Sushi (CCP/SCR) domains.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Sushi
Ligand	Heparin-binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation, intrinsic pathway Inferred from direct assay. Source: BHF-UCL negative regulation of angiogenesis Inferred from direct assay. Source: BHF-UCL negative regulation of blood coagulation Inferred from direct assay. Source: BHF-UCL negative regulation of endothelial cell migration Inferred from direct assay. Source: BHF-UCL negative regulation of endothelial cell proliferation Inferred from direct assay. Source: BHF-UCL negative regulation of fibrinolysis Inferred from direct assay. Source: BHF-UCL negative regulation of myeloid cell apoptosis Inferred from direct assay. Source: BHF-UCL negative regulation of smooth muscle cell apoptosis Inferred from direct assay. Source: BHF-UCL plasminogen activation Inferred from direct assay. Source: BHF-UCL positive regulation of lipoprotein lipase activity Inferred from direct assay. Source: BHF-UCL triglyceride metabolic process Inferred from direct assay. Source: BHF-UCL triglyceride transport Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	cell surface Inferred from direct assay. Source: BHF-UCL chylomicron Inferred from direct assay. Source: BHF-UCL high-density lipoprotein particle Inferred from direct assay. Source: BHF-UCL very-low-density lipoprotein particle Inferred from direct assay. Source: BHF-UCL
Molecular function	eukaryotic cell surface binding Inferred from direct assay. Source: BHF-UCL glycoprotein binding Inferred from physical interaction. Source: BHF-UCL heparin binding Inferred from electronic annotation. Source: UniProtKB-KW lipoprotein lipase activator activity Inferred from direct assay. Source: BHF-UCL phospholipid binding Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.10 Ref.11 Ref.12 Ref.13

Chain

20 – 345

326

Beta-2-glycoprotein 1

PRO_0000002059

Regions

Domain

21 – 81

61

Sushi 1

Domain

82 – 139

58

Sushi 2

Domain

140 – 202

63

Sushi 3

Domain

203 – 262

60

Sushi 4

Region

263 – 345

83

Sushi-like

Amino acid modifications

Glycosylation

149

1

O-linked (GalNAc...)

Glycosylation

162

1

N-linked (GlcNAc...) (complex) Ref.10 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Glycosylation

183

1

N-linked (GlcNAc...) Ref.10 Ref.17 Ref.18 Ref.20

Glycosylation

193

1

N-linked (GlcNAc...) Ref.10 Ref.17 Ref.18 Ref.20

Glycosylation

253

1

N-linked (GlcNAc...) Ref.10 Ref.16 Ref.18 Ref.19 Ref.20

Disulfide bond

23 ↔ 66

Ref.10 Ref.14

Disulfide bond

51 ↔ 79

Ref.10 Ref.14

Disulfide bond

84 ↔ 124

Ref.10 Ref.14

Disulfide bond

110 ↔ 137

Ref.10 Ref.14

Disulfide bond

142 ↔ 188

Ref.10 Ref.14

Disulfide bond

174 ↔ 200

Ref.10 Ref.14

Disulfide bond

205 ↔ 248

Ref.10 Ref.14

Disulfide bond

234 ↔ 260

Ref.10 Ref.14

Disulfide bond

264 ↔ 315

Ref.10 Ref.14

Disulfide bond

300 ↔ 325

Ref.10 Ref.14

Disulfide bond

307 ↔ 345

Ref.10 Ref.14

Natural variations

Natural variant

5

1

V → A.
Corresponds to variant rs3826358 [ dbSNP | Ensembl ].

VAR_048316

Natural variant

107

1

S → N in allele APOH*1. Ref.7 Ref.8 Ref.25
Corresponds to variant rs1801692 [ dbSNP | Ensembl ].

VAR_008169

Natural variant

154

1

R → H. Ref.8
Corresponds to variant rs8178847 [ dbSNP | Ensembl ].

VAR_019155

Natural variant

266

1

V → L in 23% of the population. Ref.8 Ref.24
Corresponds to variant rs4581 [ dbSNP | Ensembl ].

VAR_000673

Natural variant

325

1

C → G Loss of phosphatidylserine-binding. Ref.26
Corresponds to variant rs1801689 [ dbSNP | Ensembl ].

VAR_008170

Natural variant

335

1

W → S in allele APOH*3W; loss of phosphatidylserine-binding. Ref.8 Ref.26
Corresponds to variant rs1801690 [ dbSNP | Ensembl ].

VAR_008171

Experimental info

Sequence conflict

121

1

S → C AA sequence Ref.10

Sequence conflict

188

1

C → N AA sequence Ref.10

Secondary structure

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345

Helix Strand Turn

Details...

Beta strand

23 – 25

3

Beta strand

32 – 36

5

Beta strand

39 – 41

3

Beta strand

46 – 51

6

Beta strand

55 – 60

6

Beta strand

63 – 65

3

Beta strand

79 – 81

3

Beta strand

93 – 96

4

Beta strand

105 – 110

6

Beta strand

114 – 118

5

Beta strand

120 – 124

5

Beta strand

128 – 132

5

Beta strand

136 – 139

4

Beta strand

151 – 155

5

Beta strand

163 – 165

3

Beta strand

169 – 174

6

Beta strand

178 – 182

5

Beta strand

184 – 188

5

Beta strand

192 – 194

3

Beta strand

199 – 202

4

Beta strand

214 – 217

4

Beta strand

229 – 234

6

Beta strand

238 – 242

5

Beta strand

244 – 248

5

Beta strand

252 – 255

4

Beta strand

260 – 262

3

Beta strand

267 – 270

4

Beta strand

272 – 275

4

Beta strand

278 – 281

4

Helix

282 – 285

4

Turn

286 – 288

3

Beta strand

295 – 301

7

Turn

303 – 305

3

Beta strand

308 – 314

7

Turn

331 – 333

3

Helix

339 – 341

3

Sequences

	Sequence		Length	Mass (Da)
	P02749 [UniParc]. Last modified June 1, 1994. Version 3. Checksum: 63101704F8EDFE3F	FASTA	345	38,298
	10 20 30 40 50 60 MISPVLILFS SFLCHVAIAG RTCPKPDDLP FSTVVPLKTF YEPGEEITYS CKPGYVSRGG 70 80 90 100 110 120 MRKFICPLTG LWPINTLKCT PRVCPFAGIL ENGAVRYTTF EYPNTISFSC NTGFYLNGAD 130 140 150 160 170 180 SAKCTEEGKW SPELPVCAPI ICPPPSIPTF ATLRVYKPSA GNNSLYRDTA VFECLPQHAM 190 200 210 220 230 240 FGNDTITCTT HGNWTKLPEC REVKCPFPSR PDNGFVNYPA KPTLYYKDKA TFGCHDGYSL 250 260 270 280 290 300 DGPEEIECTK LGNWSAMPSC KASCKVPVKK ATVVYQGERV KIQEKFKNGM LHGDKVSFFC 310 320 330 340 KNKEKKCSYT EDAQCIDGTI EVPKCFKEHS SLAFWKTDAS DVKPC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide and deduced amino acid sequence of human beta 2-glycoprotein I." Steinkasserer A., Estaller C., Weiss E., Sim R.B., Day A.J. Biochem. J. 277:387-391(1991) [PubMed: 1650181] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Molecular cloning and mammalian expression of human beta 2-glycoprotein I cDNA." Kristensen T., Schousboe I., Boel E., Mulvihill E.M., Hansen R.R., Moeller K.B., Moeller N.P.H., Sottrup-Jensen L. FEBS Lett. 289:183-186(1991) [PubMed: 1655523] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Nucleotide sequence and expression of the human gene encoding apolipoprotein H (beta 2-glycoprotein I)." Mehdi H., Nunn M., Steel D.M., Whitehead A.S., Perez M., Walker L., Peeples M.E. Gene 108:293-298(1991) [PubMed: 1748314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"Molecular cloning and sequence analysis of the cDNA encoding human apolipoprotein H (beta 2-glycoprotein I)." Day J.R., O'Hara P.J., Grant F.J., Lofton-Day C.E., Berkaw M.N., Werner P., Arnaud P. Int. J. Clin. Lab. Res. 21:256-263(1992) [PubMed: 1339416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Molecular definition of human beta 2-glycoprotein I (beta 2-GPI) by cDNA cloning and inter-species differences of beta 2-GPI in alternation of anticardiolipin binding." Matsuura E., Igarashi M., Igarashi Y., Nagae H., Ichikawa K., Yasuda T., Koike T. Int. Immunol. 3:1217-1221(1991) [PubMed: 1777418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Structure of the human beta2-glycoprotein I (apolipoprotein H) gene." Okkels H., Rasmussen T.E., Sanghera D.K., Kamboh M.I., Kristensen T. Eur. J. Biochem. 259:435-440(1999) [PubMed: 9914524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-107. Tissue: Liver.
[8]	SeattleSNPs variation discovery resource Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-107; HIS-154; LEU-266 AND SER-335.
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[10]	"Complete amino acid sequence of human plasma beta 2-glycoprotein I." Lozier J., Takahashi N., Putnam F.W. Proc. Natl. Acad. Sci. U.S.A. 81:3640-3644(1984) [PubMed: 6587378] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-345, GLYCOSYLATION AT ASN-162; ASN-183; ASN-193 AND ASN-253, DISULFIDE BONDS.
[11]	"Heterogeneity of anticardiolipin antibodies defined by the anticardiolipin cofactor." Matsuura E., Igarashi Y., Fujimoto M., Ichikawa K., Suzuki T., Sumida T., Yasuda T., Koike T. J. Immunol. 148:3885-3891(1992) [PubMed: 1602135] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-44.
[12]	"Anti-phospholipid antibodies are directed against a complex antigen that includes a lipid-binding inhibitor of coagulation: beta 2-glycoprotein I (apolipoprotein H)." McNeil H.P., Simpson R.J., Chesterman C.N., Krilis S.A. Proc. Natl. Acad. Sci. U.S.A. 87:4120-4124(1990) [PubMed: 2349221] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-43.
[13]	"Purification of apolipoprotein H (beta 2-glycoprotein I)-like protein from human follicular fluid." Aleporou-Marinou V., Pappa H., Yalouris P., Patargias T. Comp. Biochem. Physiol. 128B:537-542(2001) [PubMed: 11250549] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-38. Tissue: Ovarian follicular fluid.
[14]	"Activity, disulphide mapping and structural modelling of the fifth domain of human beta 2-glycoprotein I." Steinkkasserer A., Barlow P.N., Willis A.C., Kertesz Z., Campbell I.D., Sim R.B., Norman D.G. FEBS Lett. 313:193-197(1992) [PubMed: 1426288] [Abstract] Cited for: DISULFIDE BONDS IN C-TERMINAL DOMAIN.
[15]	"Qualitative analysis of the carbohydrate composition of apolipoprotein H." Gambino R., Ruiu G., Pagano G., Cassader M. J. Protein Chem. 16:205-212(1997) [PubMed: 9155091] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES.
[16]	"A proteomic analysis of human bile." Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A. Mol. Cell. Proteomics 3:715-728(2004) [PubMed: 15084671] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253, MASS SPECTROMETRY. Tissue: Bile.
[17]	"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-162; ASN-183 AND ASN-193, MASS SPECTROMETRY. Tissue: Plasma.
[18]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND ASN-253, MASS SPECTROMETRY. Tissue: Plasma.
[19]	"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-162 AND ASN-253, MASS SPECTROMETRY. Tissue: Saliva.
[20]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND ASN-253, MASS SPECTROMETRY. Tissue: Liver.
[21]	"Enrichment of glycopeptides for glycan structure and attachment site identification." Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G. Nat. Methods 6:809-811(2009) [PubMed: 19838169] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[22]	"Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids based on its crystal structure." Bouma B., de Groot P.G., van Den Elsen J.M.H., Ravelli R.B.G., Schouten A., Simmelink M.J.A., Derksen R.H.W.M., Kroon J., Gros P. EMBO J. 18:5166-5174(1999) [PubMed: 10508150] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). Tissue: Plasma.
[23]	"Crystal structure of human beta2-glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome." Schwarzenbacher R., Zeth K., Diederichs K., Gries A., Kostner G.M., Laggner P., Prassl R. EMBO J. 18:6228-6239(1999) [PubMed: 10562535] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
[24]	"Human beta 2-glycoprotein I: molecular analysis of DNA and amino acid polymorphism." Steinkasserer A., Doerner C., Wuerzner R., Sim R.B. Hum. Genet. 91:401-402(1993) [PubMed: 8099061] [Abstract] Cited for: VARIANT LEU-266.
[25]	"Molecular basis of the apolipoprotein H (beta 2-glycoprotein I) protein polymorphism." Sanghera D.K., Kristensen T., Hamman R.F., Kamboh M.I. Hum. Genet. 100:57-62(1997) [PubMed: 9225969] [Abstract] Cited for: VARIANT ASN-107.
[26]	"Identification of structural mutations in the fifth domain of apolipoprotein H (beta-2-glycoprotein I) which affect phospholipid binding." Sanghera D.K., Wagenknecht D.R., McIntyre J.A., Kamboh M.I. Hum. Mol. Genet. 6:311-316(1997) [PubMed: 9063752] [Abstract] Cited for: VARIANTS GLY-325 AND SER-335.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X58100 mRNA. Translation: CAA41113.1.
X53595 mRNA. Translation: CAA37664.1.
X57847 mRNA. Translation: CAA40977.1.
M62839 mRNA. Translation: AAA51766.1.
S80305 mRNA. Translation: AAB21330.1.
Y11493 , Y11494, Y11495, X53595, Y11496, Y11497, Y11498 Genomic DNA. Translation: CAA72279.1.
Y17754 Genomic DNA. Translation: CAA76845.1.
AK313838 mRNA. Translation: BAG36570.1.
AY322156 Genomic DNA. Translation: AAP72014.1.
BC020703 mRNA. Translation: AAH20703.1.
BC026283 mRNA. Translation: AAH26283.1.

IPI

IPI00298828.

PIR

NBHU. S17178.

RefSeq

NP_000033.2. NM_000042.2.

UniGene

Hs.445358.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C1Z	X-ray	2.87	A	20-345	[»]
1G4F	NMR	-	A	261-345	[»]
1G4G	NMR	-	A	261-345	[»]
1QUB	X-ray	2.70	A	20-329	[»]
2KRI	NMR	-	A	263-345	[»]
3OP8	X-ray	1.90	A/B	263-345	[»]

ProteinModelPortal

P02749.

SMR

P02749. Positions 20-345.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46878N.

IntAct

P02749. 7 interactions.

MINT

MINT-6743724.

STRING

P02749.

Polymorphism databases

DMDM

543826.

Proteomic databases

PeptideAtlas

P02749.

PRIDE

P02749.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000205948; ENSP00000205948; ENSG00000091583.

GeneID

350.

KEGG

hsa:350.

UCSC

uc002jfn.2. human.

Organism-specific databases

CTD

350.

GeneCards

GC17M064208.

H-InvDB

HIX0014098.

HGNC

HGNC:616. APOH.

HPA

CAB022214.
HPA001654.
HPA003732.

MIM

138700. gene.

neXtProt

NX_P02749.

PharmGKB

PA24903.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19347.

GeneTree

ENSGT00580000081405.

HOGENOM

HBG714340.

HOVERGEN

HBG004271.

InParanoid

P02749.

OMA

TEDAQCI.

OrthoDB

EOG4V9TR1.

PhylomeDB

P02749.

Gene expression databases

ArrayExpress

P02749.

Bgee

P02749.

CleanEx

HS_APOH.

Genevestigator

P02749.

GermOnline

ENSG00000091583. Homo sapiens.

Family and domain databases

InterPro

IPR016060. Complement_control_module.
IPR015104. Sushi_2.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Gene3D

G3DSA:2.10.70.10. Complement_control_module. 5 hits.

Pfam

PF00084. Sushi. 4 hits.
PF09014. Sushi_2. 1 hit.
[Graphical view]

ProDom

PD012422. Sushi_2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00032. CCP. 4 hits.
[Graphical view]

SUPFAM

SSF57535. Complement_control_module. 5 hits.

PROSITE

PS50923. SUSHI. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

1441.

PMAP-CutDB

P02749.

SOURCE

Search...

Entry information

Entry name

APOH_HUMAN

Accession

Primary (citable) accession number: P02749
Secondary accession number(s): B2R9M3, Q9UCN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 1, 1994
Last modified:	January 25, 2012
This is version 146 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.