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P02749

- APOH_HUMAN

UniProt

P02749 - APOH_HUMAN

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Protein

Beta-2-glycoprotein 1

Gene

APOH

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

Functioni

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.

GO - Molecular functioni

  1. glycoprotein binding Source: BHF-UCL
  2. heparin binding Source: UniProtKB-KW
  3. identical protein binding Source: IntAct
  4. lipid binding Source: BHF-UCL
  5. lipoprotein lipase activator activity Source: BHF-UCL
  6. phospholipid binding Source: BHF-UCL

GO - Biological processi

  1. blood coagulation, intrinsic pathway Source: BHF-UCL
  2. negative regulation of angiogenesis Source: BHF-UCL
  3. negative regulation of blood coagulation Source: BHF-UCL
  4. negative regulation of endothelial cell migration Source: BHF-UCL
  5. negative regulation of endothelial cell proliferation Source: BHF-UCL
  6. negative regulation of fibrinolysis Source: BHF-UCL
  7. negative regulation of myeloid cell apoptotic process Source: BHF-UCL
  8. negative regulation of smooth muscle cell apoptotic process Source: BHF-UCL
  9. plasminogen activation Source: BHF-UCL
  10. positive regulation of blood coagulation Source: BHF-UCL
  11. positive regulation of lipoprotein lipase activity Source: BHF-UCL
  12. regulation of fibrinolysis Source: BHF-UCL
  13. triglyceride metabolic process Source: BHF-UCL
  14. triglyceride transport Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:APOH
Synonyms:B2G1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:616. APOH.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. chylomicron Source: BHF-UCL
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProtKB
  5. high-density lipoprotein particle Source: BHF-UCL
  6. very-low-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24903.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19194 PublicationsAdd
BLAST
Chaini20 – 345326Beta-2-glycoprotein 1PRO_0000002059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 66
Disulfide bondi51 ↔ 79
Disulfide bondi84 ↔ 124
Disulfide bondi110 ↔ 137
Disulfide bondi142 ↔ 188
Glycosylationi149 – 1491O-linked (GalNAc...)
Glycosylationi162 – 1621N-linked (GlcNAc...) (complex)8 Publications
Disulfide bondi174 ↔ 200
Glycosylationi183 – 1831N-linked (GlcNAc...)4 Publications
Glycosylationi193 – 1931N-linked (GlcNAc...)4 Publications
Disulfide bondi205 ↔ 248
Disulfide bondi234 ↔ 260
Glycosylationi253 – 2531N-linked (GlcNAc...)5 Publications
Disulfide bondi264 ↔ 315
Disulfide bondi300 ↔ 325
Disulfide bondi307 ↔ 345

Post-translational modificationi

N- and O-glycosylated. PubMed:6587378 also reports glycosylation on 'Asn-188' for their allele.8 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP02749.
PaxDbiP02749.
PeptideAtlasiP02749.
PRIDEiP02749.

PTM databases

PhosphoSiteiP02749.

Miscellaneous databases

PMAP-CutDBP02749.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiP02749.
CleanExiHS_APOH.
ExpressionAtlasiP02749. baseline and differential.
GenevestigatoriP02749.

Organism-specific databases

HPAiCAB022214.
HPA001654.
HPA003732.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2114682,EBI-2114682
LPAP085194EBI-2114682,EBI-9232288
PLGP007472EBI-2114682,EBI-999394

Protein-protein interaction databases

BioGridi106847. 12 interactions.
DIPiDIP-46878N.
IntActiP02749. 10 interactions.
MINTiMINT-6743724.
STRINGi9606.ENSP00000205948.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243Combined sources
Beta strandi32 – 365Combined sources
Beta strandi39 – 413Combined sources
Beta strandi46 – 516Combined sources
Beta strandi55 – 573Combined sources
Beta strandi62 – 654Combined sources
Beta strandi79 – 813Combined sources
Beta strandi93 – 964Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi120 – 1245Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi151 – 1555Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi169 – 1746Combined sources
Beta strandi178 – 1825Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi192 – 1954Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi238 – 2425Combined sources
Beta strandi244 – 2485Combined sources
Beta strandi252 – 2554Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi267 – 2704Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi278 – 2814Combined sources
Helixi282 – 2854Combined sources
Turni286 – 2883Combined sources
Beta strandi295 – 3028Combined sources
Turni303 – 3064Combined sources
Beta strandi307 – 31610Combined sources
Turni331 – 3333Combined sources
Helixi339 – 3413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C1ZX-ray2.87A20-345[»]
1G4FNMR-A261-345[»]
1G4GNMR-A261-345[»]
1QUBX-ray2.70A20-345[»]
2KRINMR-A263-345[»]
3OP8X-ray1.90A/B263-345[»]
4JHSX-ray3.00A203-345[»]
ProteinModelPortaliP02749.
SMRiP02749. Positions 20-345.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02749.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 8161Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini82 – 13958Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini140 – 20263Sushi 3PROSITE-ProRule annotationAdd
BLAST
Domaini203 – 26260Sushi 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni263 – 34583Sushi-likeAdd
BLAST

Sequence similaritiesi

Contains 4 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG323950.
GeneTreeiENSGT00760000118803.
HOGENOMiHOG000034008.
HOVERGENiHBG004271.
InParanoidiP02749.
KOiK17305.
OMAiRFTCPLT.
OrthoDBiEOG7K6PV8.
PhylomeDBiP02749.
TreeFamiTF334137.

Family and domain databases

InterProiIPR015104. Sushi_2.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamiPF00084. Sushi. 4 hits.
PF09014. Sushi_2. 1 hit.
[Graphical view]
ProDomiPD012422. Sushi_2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00032. CCP. 4 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 5 hits.
PROSITEiPS50923. SUSHI. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02749-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MISPVLILFS SFLCHVAIAG RTCPKPDDLP FSTVVPLKTF YEPGEEITYS
60 70 80 90 100
CKPGYVSRGG MRKFICPLTG LWPINTLKCT PRVCPFAGIL ENGAVRYTTF
110 120 130 140 150
EYPNTISFSC NTGFYLNGAD SAKCTEEGKW SPELPVCAPI ICPPPSIPTF
160 170 180 190 200
ATLRVYKPSA GNNSLYRDTA VFECLPQHAM FGNDTITCTT HGNWTKLPEC
210 220 230 240 250
REVKCPFPSR PDNGFVNYPA KPTLYYKDKA TFGCHDGYSL DGPEEIECTK
260 270 280 290 300
LGNWSAMPSC KASCKVPVKK ATVVYQGERV KIQEKFKNGM LHGDKVSFFC
310 320 330 340
KNKEKKCSYT EDAQCIDGTI EVPKCFKEHS SLAFWKTDAS DVKPC
Length:345
Mass (Da):38,298
Last modified:June 1, 1994 - v3
Checksum:i63101704F8EDFE3F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211S → C AA sequence (PubMed:6587378)Curated
Sequence conflicti188 – 1881C → N AA sequence (PubMed:6587378)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51V → A.
Corresponds to variant rs3826358 [ dbSNP | Ensembl ].
VAR_048316
Natural varianti107 – 1071S → N in allele APOH*1. 3 Publications
Corresponds to variant rs1801692 [ dbSNP | Ensembl ].
VAR_008169
Natural varianti154 – 1541R → H.1 Publication
Corresponds to variant rs8178847 [ dbSNP | Ensembl ].
VAR_019155
Natural varianti266 – 2661V → L in 23% of the population. 2 Publications
Corresponds to variant rs4581 [ dbSNP | Ensembl ].
VAR_000673
Natural varianti325 – 3251C → G Loss of phosphatidylserine-binding. 1 Publication
Corresponds to variant rs1801689 [ dbSNP | Ensembl ].
VAR_008170
Natural varianti335 – 3351W → S in allele APOH*3W; loss of phosphatidylserine-binding. 2 Publications
Corresponds to variant rs1801690 [ dbSNP | Ensembl ].
VAR_008171

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11663.1.
PIRiS17178. NBHU.
RefSeqiNP_000033.2. NM_000042.2.
UniGeneiHs.445358.

Genome annotation databases

EnsembliENST00000205948; ENSP00000205948; ENSG00000091583.
GeneIDi350.
KEGGihsa:350.
UCSCiuc002jfn.4. human.

Polymorphism databases

DMDMi543826.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS11663.1.
PIRi S17178. NBHU.
RefSeqi NP_000033.2. NM_000042.2.
UniGenei Hs.445358.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 20-345 [» ]
2KRI NMR - A 263-345 [» ]
3OP8 X-ray 1.90 A/B 263-345 [» ]
4JHS X-ray 3.00 A 203-345 [» ]
ProteinModelPortali P02749.
SMRi P02749. Positions 20-345.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106847. 12 interactions.
DIPi DIP-46878N.
IntActi P02749. 10 interactions.
MINTi MINT-6743724.
STRINGi 9606.ENSP00000205948.

Chemistry

BindingDBi P02749.

PTM databases

PhosphoSitei P02749.

Polymorphism databases

DMDMi 543826.

Proteomic databases

MaxQBi P02749.
PaxDbi P02749.
PeptideAtlasi P02749.
PRIDEi P02749.

Protocols and materials databases

DNASUi 350.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000205948 ; ENSP00000205948 ; ENSG00000091583 .
GeneIDi 350.
KEGGi hsa:350.
UCSCi uc002jfn.4. human.

Organism-specific databases

CTDi 350.
GeneCardsi GC17M064208.
HGNCi HGNC:616. APOH.
HPAi CAB022214.
HPA001654.
HPA003732.
MIMi 138700. gene.
neXtProti NX_P02749.
PharmGKBi PA24903.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG323950.
GeneTreei ENSGT00760000118803.
HOGENOMi HOG000034008.
HOVERGENi HBG004271.
InParanoidi P02749.
KOi K17305.
OMAi RFTCPLT.
OrthoDBi EOG7K6PV8.
PhylomeDBi P02749.
TreeFami TF334137.

Miscellaneous databases

ChiTaRSi APOH. human.
EvolutionaryTracei P02749.
GeneWikii Apolipoprotein_H.
GenomeRNAii 350.
NextBioi 1441.
PMAP-CutDB P02749.
PROi P02749.
SOURCEi Search...

Gene expression databases

Bgeei P02749.
CleanExi HS_APOH.
ExpressionAtlasi P02749. baseline and differential.
Genevestigatori P02749.

Family and domain databases

InterProi IPR015104. Sushi_2.
IPR000436. Sushi_SCR_CCP.
[Graphical view ]
Pfami PF00084. Sushi. 4 hits.
PF09014. Sushi_2. 1 hit.
[Graphical view ]
ProDomi PD012422. Sushi_2. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00032. CCP. 4 hits.
[Graphical view ]
SUPFAMi SSF57535. SSF57535. 5 hits.
PROSITEi PS50923. SUSHI. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATES.
  16. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183 AND ASN-193.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND ASN-253.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162; ASN-183; ASN-193 AND ASN-253.
    Tissue: Liver.
  21. Cited for: GLYCOSYLATION AT ASN-162.
  22. "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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    Tissue: Plasma.
  25. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
  26. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-266.
  27. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-107.
  28. "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] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLY-325 AND SER-335.

Entry informationi

Entry nameiAPOH_HUMAN
AccessioniPrimary (citable) accession number: P02749
Secondary accession number(s): B2R9M3, Q9UCN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 175 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3