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P00738 (HPT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Haptoglobin
Alternative name(s):
Zonulin

Cleaved into the following 2 chains:

  1. Haptoglobin alpha chain
  2. Haptoglobin beta chain
Gene names
Name:HP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an Antimicrobial; Antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidely cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway. Ref.29

Uncleaved haptoglogin, also known as zonulin, plays a role in intestinal permeability, allowing intercellular tight junction disassembly, and controlling the equilibrium between tolerance and immunity to non-self antigens. Ref.29

Subunit structure

Tetramer of two alpha and two beta chains; disufide-linked. The Hemoglobin/haptoglobin complex is composed of a haptoglobin dimer bound to two hemoglobin alpha-beta dimers. Interacts with CD163.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Polymorphism

In the human populations there are two major allelic forms, alpha-1 (1-1) with 83 residues and alpha-2 (2-2) with 142 residues. These alleles determine 3 possible genotypes, homozygous (1-1 or 2-2) and heterozygous (2-1), and 3 major phenotypes HP*1F/HP*1S and HP*2FS. The two main alleles of HP*1 are called HP*1F (fast) and HP*1S (slow). The alleles exhibit different oligomerization properties. In healthy males, but not in females, the Hp 2-2 phenotype is associated with higher serum iron, decreased Antimicrobial; Antioxidant capability, and less efficient clearance from the circulation, than Hp 1-1 and 2-1.

Involvement in disease

Anhaptoglobinemia (AHP) [MIM:614081]: A condition characterized by the absence of the serum glycoprotein haptoglobin. Serum levels of haptoglobin vary among normal persons: levels are low in the neonatal period and in the elderly, differ by population, and can be influenced by environmental factors, such as infection. Secondary hypohaptoglobinemia can occur as a consequence of hemolysis, during which haptoglobin binds to free hemoglobin. Congenital haptoglobin deficiency is a risk factor for anaphylactic non-hemolytic transfusion reactions.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.30

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Contains 2 Sushi (CCP/SCR) domains.

Caution

Although homologous to serine proteases, it has lost all essential catalytic residues and has no enzymatic activity.

Ontologies

Keywords
   Biological processAcute phase
Immunity
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
Sushi
   LigandHemoglobin-binding
   Molecular functionAntibiotic
Antimicrobial
Antioxidant
Serine protease homolog
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

defense response

Traceable author statement PubMed 7036344. Source: ProtInc

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of hydrogen peroxide catabolic process

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

negative regulation of oxidoreductase activity

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

positive regulation of cell death

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

response to hydrogen peroxide

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

endocytic vesicle lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 16502470PubMed 22664934. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

haptoglobin-hemoglobin complex

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

   Molecular_functionantioxidant activity

Inferred from electronic annotation. Source: UniProtKB-KW

catalytic activity

Inferred from electronic annotation. Source: InterPro

hemoglobin binding

Inferred from direct assay PubMed 19740759. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 19758344. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00738-1)

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: P00738-2)

The sequence of this isoform differs from the canonical sequence as follows:
     38-96: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.16
Chain19 – 406388Haptoglobin
PRO_0000028456
Chain19 – 160142Haptoglobin alpha chain
PRO_0000028457
Chain162 – 406245Haptoglobin beta chain
PRO_0000028458

Regions

Domain31 – 8858Sushi 1
Domain90 – 14758Sushi 2
Domain162 – 404243Peptidase S1
Region318 – 3236Interaction with CD163 By similarity

Amino acid modifications

Glycosylation1841N-linked (GlcNAc...) (complex) Ref.20 Ref.21 Ref.23 Ref.24
Glycosylation2071N-linked (GlcNAc...) Ref.19 Ref.20 Ref.21 Ref.22 Ref.23
Glycosylation2111N-linked (GlcNAc...) Ref.20 Ref.21 Ref.22 Ref.23
Glycosylation2411N-linked (GlcNAc...) (complex) Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25
Disulfide bond33Interchain Ref.16 Ref.18
Disulfide bond52 ↔ 86 Ref.16 Ref.18
Disulfide bond92Interchain Ref.16 Ref.18
Disulfide bond111 ↔ 145 Ref.16 Ref.18
Disulfide bond149 ↔ 266Interchain (between alpha and beta chains) Ref.16 Ref.18
Disulfide bond309 ↔ 340 Ref.16 Ref.18
Disulfide bond351 ↔ 381 Ref.16 Ref.18

Natural variations

Alternative sequence38 – 9659Missing in isoform 2.
VSP_055024
Natural variant29 – 8759Missing in allele HP*1F and allele HP*1S.
VAR_017112
Natural variant1291N → D in allele HP*1F. Ref.3 Ref.5
VAR_005294
Natural variant1301E → K in allele HP*1F. Ref.3
VAR_017113
Natural variant2471I → T in AHP; causes reduced expression of the protein. Ref.30
Corresponds to variant rs104894517 [ dbSNP | Ensembl ].
VAR_066214
Natural variant3971D → H.
Corresponds to variant rs12646 [ dbSNP | Ensembl ].
VAR_017114

Experimental info

Sequence conflict701D → N in AAA52687. Ref.2
Sequence conflict1301E → G in AAI07588. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A98B56B2B1BE891E

FASTA40645,205
        10         20         30         40         50         60 
MSALGAVIAL LLWGQLFAVD SGNDVTDIAD DGCPKPPEIA HGYVEHSVRY QCKNYYKLRT 

        70         80         90        100        110        120 
EGDGVYTLND KKQWINKAVG DKLPECEADD GCPKPPEIAH GYVEHSVRYQ CKNYYKLRTE 

       130        140        150        160        170        180 
GDGVYTLNNE KQWINKAVGD KLPECEAVCG KPKNPANPVQ RILGGHLDAK GSFPWQAKMV 

       190        200        210        220        230        240 
SHHNLTTGAT LINEQWLLTT AKNLFLNHSE NATAKDIAPT LTLYVGKKQL VEIEKVVLHP 

       250        260        270        280        290        300 
NYSQVDIGLI KLKQKVSVNE RVMPICLPSK DYAEVGRVGY VSGWGRNANF KFTDHLKYVM 

       310        320        330        340        350        360 
LPVADQDQCI RHYEGSTVPE KKTPKSPVGV QPILNEHTFC AGMSKYQEDT CYGDAGSAFA 

       370        380        390        400 
VHDLEEDTWY ATGILSFDKS CAVAEYGVYV KVTSIQDWVQ KTIAEN 

« Hide

Isoform 2 [UniParc].

Checksum: 47EFE07D5FE15EB8
Show »

FASTA34738,452

References

« Hide 'large scale' references
[1]"Molecular cloning of human haptoglobin cDNA: evidence for a single mRNA coding for alpha 2 and beta chains."
van der Straten A., Herzog A., Jacobs P., Cabezon T., Bollen A.
EMBO J. 2:1003-1007(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification and characterization of human haptoglobin cDNA."
Yang F., Brune J.L., Baldwin W.D., Barnett D.R., Bowman B.H.
Proc. Natl. Acad. Sci. U.S.A. 80:5875-5879(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Characterization of human haptoglobin cDNAs coding for alpha 2FS beta and alpha 1S beta variants."
van der Straten A., Herzog A., Cabezon T., Bollen A.
FEBS Lett. 168:103-107(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS 29-ALA--GLU-87 DEL; ASP-129 AND LYS-130.
Tissue: Liver.
[4]"Evolution of haptoglobin: comparison of complementary DNA encoding Hp alpha 1S and Hp alpha 2FS."
Brune J.L., Yang F., Barnett D.R., Bowman B.H.
Nucleic Acids Res. 12:4531-4538(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 29-ALA--GLU-87 DEL.
[5]"Structure and expression of the human haptoglobin locus."
Bensi G., Raugei G., Klefenz H., Cortese R.
EMBO J. 4:119-126(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-129.
[6]"Nucleotide sequence of the haptoglobin and haptoglobin-related gene pair. The haptoglobin-related gene contains a retrovirus-like element."
Maeda N.
J. Biol. Chem. 260:6698-6709(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Junctions between genes in the haptoglobin gene cluster of primates."
Erickson L.M., Kim H.S., Maeda N.
Genomics 14:948-958(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"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. expand/collapse author list , 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].
Tissue: Mammary gland.
[9]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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] (ALLELES HP*1F AND HP*1S).
Tissue: Liver.
[12]"Expression of cloned human haptoglobin and alpha 1-antitrypsin complementary DNAs in Saccharomyces cerevisiae."
van der Straten A., Falque J.-C., Loriau R., Bollen A., Cabezon T.
DNA 5:129-136(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-19.
[13]"Sequence of human haptoglobin cDNA: evidence that the alpha and beta subunits are coded by the same mRNA."
Raugei G., Bensi G., Colantuoni V., Romano V., Santoro C., Costanzo F., Cortese R.
Nucleic Acids Res. 11:5811-5819(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-406.
[14]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 3-406.
[15]"Duplication within the haptoglobin Hp2 gene."
Maeda N., Yang F., Barnett D.R., Bowman B.H., Smithies O.
Nature 309:131-135(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-375.
[16]"Covalent structure of human haptoglobin: a serine protease homolog."
Kurosky A., Barnett D.R., Lee T.-H., Touchstone B., Hay R.E., Arnott M.S., Bowman B.H., Fitch W.M.
Proc. Natl. Acad. Sci. U.S.A. 77:3388-3392(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-28; 88-160 AND 162-406, DISULFIDE BONDS.
[17]"Protein analysis of human maculae in relation to age-related maculopathy."
Kliffen M., de Jong P.T.V.M., Luider T.M.
Lab. Invest. 73:267-272(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 162-176.
Tissue: Eye.
[18]"Studies on the interchain disulfides of human haptoglobins."
Malchy B., Dixon G.H.
Can. J. Biochem. 51:249-264(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[19]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-207 AND ASN-241.
Tissue: Plasma and Serum.
[20]"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-184; ASN-207; ASN-211 AND ASN-241.
Tissue: Plasma.
[21]"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-184; ASN-207; ASN-211 AND ASN-241.
Tissue: Plasma.
[22]"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-207 AND ASN-211.
Tissue: Saliva.
[23]"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-184; ASN-207; ASN-211 AND ASN-241.
Tissue: Liver.
[24]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-184 AND ASN-241.
[25]"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-241, STRUCTURE OF CARBOHYDRATE.
Tissue: Cerebrospinal fluid.
[26]"Identification of human zonulin, a physiological modulator of tight junctions, as prehaptoglobin-2."
Tripathi A., Lammers K.M., Goldblum S., Shea-Donohue T., Netzel-Arnett S., Buzza M.S., Antalis T.M., Vogel S.N., Zhao A., Yang S., Arrietta M.C., Meddings J.B., Fasano A.
Proc. Natl. Acad. Sci. U.S.A. 106:16799-16804(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS ZONULIN.
[27]"Haptoglobin: basic and clinical aspects."
Levy A.P., Asleh R., Blum S., Levy N.S., Miller-Lotan R., Kalet-Litman S., Anbinder Y., Lache O., Nakhoul F.M., Asaf R., Farbstein D., Pollak M., Soloveichik Y.Z., Strauss M., Alshiek J., Livshits A., Schwartz A., Awad H., Jad K., Goldenstein H.
Antioxid. Redox Signal. 12:293-304(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Zonulin and its regulation of intestinal barrier function: the biological door to inflammation, autoimmunity, and cancer."
Fasano A.
Physiol. Rev. 91:151-175(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF ZONULIN.
[30]"A novel I247T missense mutation in the haptoglobin 2 beta-chain decreases the expression of the protein and is associated with ahaptoglobinemia."
Teye K., Quaye I.K., Koda Y., Soejima M., Pang H., Tsuneoka M., Amoah A.G., Adjei A., Kimura H.
Hum. Genet. 114:499-502(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AHP THR-247, CHARACTERIZATION OF VARIANT AHP THR-247.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Haptoglobin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K00422 mRNA. Translation: AAA52687.1.
K01763 mRNA. Translation: AAA52684.1.
L29394 mRNA. Translation: AAA52685.1.
X00637 mRNA. Translation: CAA25267.1.
X01793 expand/collapse EMBL AC list , X01786, X02206, X01789, X01791 Genomic DNA. Translation: CAA25926.1.
M10935 Genomic DNA. Translation: AAA88080.1.
M69197 Genomic DNA. Translation: AAA88078.1.
AK314700 mRNA. Translation: BAF98793.1.
DQ314870 Genomic DNA. Translation: ABC40729.1.
AC004682 Genomic DNA. Translation: AAC27432.1.
AC009087 Genomic DNA. No translation available.
BC107587 mRNA. Translation: AAI07588.1.
BC121124 mRNA. Translation: AAI21125.1.
BC121125 mRNA. Translation: AAI21126.1.
M13192 mRNA. No translation available.
X00606 Genomic DNA. Translation: CAA25248.1.
CCDSCCDS45524.1.
PIRHPHU2. A92532.
HPHU1. A93521.
RefSeqNP_001119574.1. NM_001126102.1.
NP_005134.1. NM_005143.3.
UniGeneHs.513711.
Hs.702099.

3D structure databases

ProteinModelPortalP00738.
SMRP00738. Positions 33-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109480. 30 interactions.
IntActP00738. 16 interactions.
STRING9606.ENSP00000348170.

Protein family/group databases

MEROPSS01.972.

PTM databases

PhosphoSiteP00738.

Polymorphism databases

DMDM123508.

2D gel databases

DOSAC-COBS-2DPAGEP00738.
SWISS-2DPAGEP00738.

Proteomic databases

MaxQBP00738.
PaxDbP00738.
PRIDEP00738.

Protocols and materials databases

DNASU3240.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355906; ENSP00000348170; ENSG00000257017.
ENST00000398131; ENSP00000381199; ENSG00000257017.
ENST00000565574; ENSP00000454966; ENSG00000257017.
ENST00000570083; ENSP00000457629; ENSG00000257017.
GeneID3240.
KEGGhsa:3240.
UCSCuc002fbr.4. human.
uc002fbt.5. human.

Organism-specific databases

CTD3240.
GeneCardsGC16P072089.
HGNCHGNC:5141. HP.
HPACAB003787.
HPA047750.
MIM140100. gene.
614081. phenotype.
neXtProtNX_P00738.
PharmGKBPA29415.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246387.
HOVERGENHBG005989.
InParanoidP00738.
KOK16142.
OMADDTWYAA.
OrthoDBEOG722J8R.
PhylomeDBP00738.
TreeFamTF334326.

Enzyme and pathway databases

ReactomeREACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP00738.
BgeeP00738.
CleanExHS_HP.
GenevestigatorP00738.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEPS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHaptoglobin.
GenomeRNAi3240.
NextBio12895.
PROP00738.
SOURCESearch...

Entry information

Entry nameHPT_HUMAN
AccessionPrimary (citable) accession number: P00738
Secondary accession number(s): B0AZL5 expand/collapse secondary AC list , P00737, Q0VAC4, Q0VAC5, Q2PP15, Q3B7J0, Q6LBY9, Q9UC67
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM