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Protein

Haptoglobin

Gene

HP

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

Functioni

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.1 Publication
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.1 Publication

GO - Molecular functioni

  • antioxidant activity Source: UniProtKB-KW
  • hemoglobin binding Source: BHF-UCL

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • defense response Source: ProtInc
  • defense response to bacterium Source: UniProtKB-KW
  • immune system process Source: UniProtKB-KW
  • negative regulation of hydrogen peroxide catabolic process Source: BHF-UCL
  • negative regulation of oxidoreductase activity Source: BHF-UCL
  • positive regulation of cell death Source: BHF-UCL
  • receptor-mediated endocytosis Source: Reactome
  • response to hydrogen peroxide Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Antioxidant, Serine protease homolog

Keywords - Biological processi

Acute phase, Immunity

Keywords - Ligandi

Hemoglobin-binding

Enzyme and pathway databases

ReactomeiREACT_160163. Scavenging of heme from plasma.

Protein family/group databases

MEROPSiS01.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Haptoglobin
Alternative name(s):
Zonulin
Cleaved into the following 2 chains:
Gene namesi
Name:HP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:5141. HP.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • endocytic vesicle lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • haptoglobin-hemoglobin complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Anhaptoglobinemia (AHP)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614081
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471I → T in AHP; causes reduced expression of the protein. 1 Publication
Corresponds to variant rs104894517 [ dbSNP | Ensembl ].
VAR_066214

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614081. phenotype.
PharmGKBiPA29415.

Polymorphism and mutation databases

BioMutaiHP.
DMDMi123508.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 406388HaptoglobinPRO_0000028456Add
BLAST
Chaini19 – 160142Haptoglobin alpha chainPRO_0000028457Add
BLAST
Chaini162 – 406245Haptoglobin beta chainPRO_0000028458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 – 33Interchain
Disulfide bondi52 ↔ 86
Disulfide bondi92 – 92Interchain
Disulfide bondi111 ↔ 145
Disulfide bondi149 ↔ 266Interchain (between alpha and beta chains)
Glycosylationi184 – 1841N-linked (GlcNAc...) (complex)4 Publications
Glycosylationi207 – 2071N-linked (GlcNAc...)5 Publications
Glycosylationi211 – 2111N-linked (GlcNAc...)4 Publications
Glycosylationi241 – 2411N-linked (GlcNAc...) (complex)6 Publications
Disulfide bondi309 ↔ 340
Disulfide bondi351 ↔ 381

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP00738.
PaxDbiP00738.
PRIDEiP00738.

2D gel databases

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

PTM databases

PhosphoSiteiP00738.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiP00738.
CleanExiHS_HP.
ExpressionAtlasiP00738. baseline and differential.
GenevisibleiP00738. HS.

Organism-specific databases

HPAiCAB003787.
HPA047750.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
APOA1P026473EBI-1220767,EBI-701692
APOEP026497EBI-1220767,EBI-1222467

Protein-protein interaction databases

BioGridi109480. 21 interactions.
IntActiP00738. 16 interactions.
STRINGi9606.ENSP00000348170.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi101 – 11111Combined sources
Beta strandi115 – 1217Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi133 – 1353Combined sources
Turni136 – 1383Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi186 – 1938Combined sources
Beta strandi196 – 1994Combined sources
Helixi201 – 2044Combined sources
Turni205 – 2073Combined sources
Helixi214 – 2174Combined sources
Helixi218 – 2203Combined sources
Beta strandi222 – 2254Combined sources
Turni226 – 2283Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi233 – 2386Combined sources
Turni240 – 2445Combined sources
Beta strandi248 – 2547Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi278 – 2836Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi297 – 3037Combined sources
Helixi306 – 3149Combined sources
Helixi319 – 3213Combined sources
Beta strandi327 – 3304Combined sources
Beta strandi338 – 3414Combined sources
Beta strandi358 – 3636Combined sources
Turni364 – 3674Combined sources
Beta strandi368 – 37710Combined sources
Turni381 – 3833Combined sources
Beta strandi387 – 3915Combined sources
Helixi392 – 3943Combined sources
Helixi396 – 40510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WJGX-ray3.102/C/H/M/R/W92-406[»]
4X0IX-ray3.09C148-406[»]
4X0LX-ray2.05C148-406[»]
ProteinModelPortaliP00738.
SMRiP00738. Positions 33-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 8858Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini90 – 14758Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 404243Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni318 – 3236Interaction with CD163By similarity

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG246387.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000112945.
HOVERGENiHBG005989.
InParanoidiP00738.
KOiK16142.
OrthoDBiEOG722J8R.
PhylomeDBiP00738.
TreeFamiTF334326.

Family and domain databases

InterProiIPR008292. Haptoglobin.
IPR001254. Peptidase_S1.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PANTHERiPTHR24265:SF25. PTHR24265:SF25. 1 hit.
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P00738-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSALGAVIAL LLWGQLFAVD SGNDVTDIAD DGCPKPPEIA HGYVEHSVRY
60 70 80 90 100
QCKNYYKLRT EGDGVYTLND KKQWINKAVG DKLPECEADD GCPKPPEIAH
110 120 130 140 150
GYVEHSVRYQ CKNYYKLRTE GDGVYTLNNE KQWINKAVGD KLPECEAVCG
160 170 180 190 200
KPKNPANPVQ RILGGHLDAK GSFPWQAKMV SHHNLTTGAT LINEQWLLTT
210 220 230 240 250
AKNLFLNHSE NATAKDIAPT LTLYVGKKQL VEIEKVVLHP NYSQVDIGLI
260 270 280 290 300
KLKQKVSVNE RVMPICLPSK DYAEVGRVGY VSGWGRNANF KFTDHLKYVM
310 320 330 340 350
LPVADQDQCI RHYEGSTVPE KKTPKSPVGV QPILNEHTFC AGMSKYQEDT
360 370 380 390 400
CYGDAGSAFA VHDLEEDTWY ATGILSFDKS CAVAEYGVYV KVTSIQDWVQ

KTIAEN
Length:406
Mass (Da):45,205
Last modified:July 21, 1986 - v1
Checksum:iA98B56B2B1BE891E
GO
Isoform 2 (identifier: P00738-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:347
Mass (Da):38,452
Checksum:i47EFE07D5FE15EB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701D → N in AAA52687 (PubMed:6310599).Curated
Sequence conflicti130 – 1301E → G in AAI07588 (PubMed:15489334).Curated

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 8759Missing in allele HP*1F and allele HP*1S. 2 Publications
VAR_017112Add
BLAST
Natural varianti129 – 1291N → D in allele HP*1F. 2 Publications
VAR_005294
Natural varianti130 – 1301E → K in allele HP*1F. 1 Publication
VAR_017113
Natural varianti247 – 2471I → T in AHP; causes reduced expression of the protein. 1 Publication
Corresponds to variant rs104894517 [ dbSNP | Ensembl ].
VAR_066214
Natural varianti397 – 3971D → H.
Corresponds to variant rs12646 [ dbSNP | Ensembl ].
VAR_017114

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei38 – 9659Missing in isoform 2. CuratedVSP_055024Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00422 mRNA. Translation: AAA52687.1.
K01763 mRNA. Translation: AAA52684.1.
L29394 mRNA. Translation: AAA52685.1.
X00637 mRNA. Translation: CAA25267.1.
X01793
, 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.
CCDSiCCDS45524.1. [P00738-1]
CCDS45525.1. [P00738-2]
PIRiA92532. HPHU2.
A93521. HPHU1.
RefSeqiNP_001119574.1. NM_001126102.1. [P00738-2]
NP_005134.1. NM_005143.3. [P00738-1]
XP_005255979.2. XM_005255922.3.
UniGeneiHs.513711.
Hs.702099.

Genome annotation databases

EnsembliENST00000355906; ENSP00000348170; ENSG00000257017. [P00738-1]
ENST00000398131; ENSP00000381199; ENSG00000257017. [P00738-2]
ENST00000570083; ENSP00000457629; ENSG00000257017. [P00738-2]
GeneIDi3240.
KEGGihsa:3240.
UCSCiuc002fbr.4. human. [P00738-1]
uc002fbt.5. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Haptoglobin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00422 mRNA. Translation: AAA52687.1.
K01763 mRNA. Translation: AAA52684.1.
L29394 mRNA. Translation: AAA52685.1.
X00637 mRNA. Translation: CAA25267.1.
X01793
, 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.
CCDSiCCDS45524.1. [P00738-1]
CCDS45525.1. [P00738-2]
PIRiA92532. HPHU2.
A93521. HPHU1.
RefSeqiNP_001119574.1. NM_001126102.1. [P00738-2]
NP_005134.1. NM_005143.3. [P00738-1]
XP_005255979.2. XM_005255922.3.
UniGeneiHs.513711.
Hs.702099.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WJGX-ray3.102/C/H/M/R/W92-406[»]
4X0IX-ray3.09C148-406[»]
4X0LX-ray2.05C148-406[»]
ProteinModelPortaliP00738.
SMRiP00738. Positions 33-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109480. 21 interactions.
IntActiP00738. 16 interactions.
STRINGi9606.ENSP00000348170.

Protein family/group databases

MEROPSiS01.972.

PTM databases

PhosphoSiteiP00738.

Polymorphism and mutation databases

BioMutaiHP.
DMDMi123508.

2D gel databases

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

Proteomic databases

MaxQBiP00738.
PaxDbiP00738.
PRIDEiP00738.

Protocols and materials databases

DNASUi3240.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355906; ENSP00000348170; ENSG00000257017. [P00738-1]
ENST00000398131; ENSP00000381199; ENSG00000257017. [P00738-2]
ENST00000570083; ENSP00000457629; ENSG00000257017. [P00738-2]
GeneIDi3240.
KEGGihsa:3240.
UCSCiuc002fbr.4. human. [P00738-1]
uc002fbt.5. human.

Organism-specific databases

CTDi3240.
GeneCardsiGC16P072089.
HGNCiHGNC:5141. HP.
HPAiCAB003787.
HPA047750.
MIMi140100. gene.
614081. phenotype.
neXtProtiNX_P00738.
PharmGKBiPA29415.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG246387.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000112945.
HOVERGENiHBG005989.
InParanoidiP00738.
KOiK16142.
OrthoDBiEOG722J8R.
PhylomeDBiP00738.
TreeFamiTF334326.

Enzyme and pathway databases

ReactomeiREACT_160163. Scavenging of heme from plasma.

Miscellaneous databases

GeneWikiiHaptoglobin.
GenomeRNAii3240.
NextBioi12895.
PROiP00738.
SOURCEiSearch...

Gene expression databases

BgeeiP00738.
CleanExiHS_HP.
ExpressionAtlasiP00738. baseline and differential.
GenevisibleiP00738. HS.

Family and domain databases

InterProiIPR008292. Haptoglobin.
IPR001254. Peptidase_S1.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PANTHERiPTHR24265:SF25. PTHR24265:SF25. 1 hit.
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 3-406.
  15. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-375.
  16. 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. 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. Cited for: IDENTIFICATION AS ZONULIN.
  27. Cited for: REVIEW.
  28. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  32. "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.

Entry informationi

Entry nameiHPT_HUMAN
AccessioniPrimary (citable) accession number: P00738
Secondary accession number(s): B0AZL5
, P00737, Q0VAC4, Q0VAC5, Q2PP15, Q3B7J0, Q6LBY9, Q9UC67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 173 of the entry and version 1 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

Caution

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.