Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00738

- HPT_HUMAN

UniProt

P00738 - HPT_HUMAN

Protein

Haptoglobin

Gene

HP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. antioxidant activity Source: UniProtKB-KW
    2. catalytic activity Source: InterPro
    3. hemoglobin binding Source: BHF-UCL
    4. protein binding Source: IntAct

    GO - Biological processi

    1. acute-phase response Source: UniProtKB-KW
    2. defense response Source: ProtInc
    3. defense response to bacterium Source: UniProtKB-KW
    4. immune system process Source: UniProtKB-KW
    5. negative regulation of hydrogen peroxide catabolic process Source: BHF-UCL
    6. negative regulation of oxidoreductase activity Source: BHF-UCL
    7. positive regulation of cell death Source: BHF-UCL
    8. response to hydrogen peroxide Source: BHF-UCL

    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: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:5141. HP.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. endocytic vesicle lumen Source: Reactome
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. haptoglobin-hemoglobin complex Source: BHF-UCL

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP00738.
    BgeeiP00738.
    CleanExiHS_HP.
    GenevestigatoriP00738.

    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. 17 interactions.
    IntActiP00738. 16 interactions.
    STRINGi9606.ENSP00000348170.

    Structurei

    3D structure databases

    ProteinModelPortaliP00738.
    SMRiP00738. Positions 33-405.
    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.
    HOVERGENiHBG005989.
    InParanoidiP00738.
    KOiK16142.
    OMAiDDTWYAA.
    OrthoDBiEOG722J8R.
    PhylomeDBiP00738.
    TreeFamiTF334326.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR001314. Peptidase_S1A.
    IPR000436. Sushi_SCR_CCP.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    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. Align

    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

    MSALGAVIAL LLWGQLFAVD SGNDVTDIAD DGCPKPPEIA HGYVEHSVRY    50
    QCKNYYKLRT EGDGVYTLND KKQWINKAVG DKLPECEADD GCPKPPEIAH 100
    GYVEHSVRYQ CKNYYKLRTE GDGVYTLNNE KQWINKAVGD KLPECEAVCG 150
    KPKNPANPVQ RILGGHLDAK GSFPWQAKMV SHHNLTTGAT LINEQWLLTT 200
    AKNLFLNHSE NATAKDIAPT LTLYVGKKQL VEIEKVVLHP NYSQVDIGLI 250
    KLKQKVSVNE RVMPICLPSK DYAEVGRVGY VSGWGRNANF KFTDHLKYVM 300
    LPVADQDQCI RHYEGSTVPE KKTPKSPVGV QPILNEHTFC AGMSKYQEDT 350
    CYGDAGSAFA VHDLEEDTWY ATGILSFDKS CAVAEYGVYV KVTSIQDWVQ 400
    KTIAEN 406
    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. 1 Publication
    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:
    EMBL
    GenBank
    DDBJ
    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.
    NP_005134.1. NM_005143.3.
    UniGeneiHs.513711.
    Hs.702099.

    Genome annotation databases

    EnsembliENST00000355906; ENSP00000348170; ENSG00000257017. [P00738-1]
    ENST00000398131; ENSP00000381199; ENSG00000257017. [P00738-2]
    ENST00000565574; ENSP00000454966; ENSG00000257017.
    ENST00000570083; ENSP00000457629; ENSG00000257017. [P00738-2]
    GeneIDi3240.
    KEGGihsa:3240.
    UCSCiuc002fbr.4. human. [P00738-1]
    uc002fbt.5. human.

    Polymorphism databases

    DMDMi123508.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS45524.1. [P00738-1 ]
    CCDS45525.1. [P00738-2 ]
    PIRi A92532. HPHU2.
    A93521. HPHU1.
    RefSeqi NP_001119574.1. NM_001126102.1.
    NP_005134.1. NM_005143.3.
    UniGenei Hs.513711.
    Hs.702099.

    3D structure databases

    ProteinModelPortali P00738.
    SMRi P00738. Positions 33-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109480. 17 interactions.
    IntActi P00738. 16 interactions.
    STRINGi 9606.ENSP00000348170.

    Protein family/group databases

    MEROPSi S01.972.

    PTM databases

    PhosphoSitei P00738.

    Polymorphism databases

    DMDMi 123508.

    2D gel databases

    DOSAC-COBS-2DPAGE P00738.
    SWISS-2DPAGE P00738.

    Proteomic databases

    MaxQBi P00738.
    PaxDbi P00738.
    PRIDEi P00738.

    Protocols and materials databases

    DNASUi 3240.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355906 ; ENSP00000348170 ; ENSG00000257017 . [P00738-1 ]
    ENST00000398131 ; ENSP00000381199 ; ENSG00000257017 . [P00738-2 ]
    ENST00000565574 ; ENSP00000454966 ; ENSG00000257017 .
    ENST00000570083 ; ENSP00000457629 ; ENSG00000257017 . [P00738-2 ]
    GeneIDi 3240.
    KEGGi hsa:3240.
    UCSCi uc002fbr.4. human. [P00738-1 ]
    uc002fbt.5. human.

    Organism-specific databases

    CTDi 3240.
    GeneCardsi GC16P072089.
    HGNCi HGNC:5141. HP.
    HPAi CAB003787.
    HPA047750.
    MIMi 140100. gene.
    614081. phenotype.
    neXtProti NX_P00738.
    PharmGKBi PA29415.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG246387.
    HOVERGENi HBG005989.
    InParanoidi P00738.
    KOi K16142.
    OMAi DDTWYAA.
    OrthoDBi EOG722J8R.
    PhylomeDBi P00738.
    TreeFami TF334326.

    Enzyme and pathway databases

    Reactomei REACT_160163. Scavenging of heme from plasma.

    Miscellaneous databases

    GeneWikii Haptoglobin.
    GenomeRNAii 3240.
    NextBioi 12895.
    PROi P00738.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00738.
    Bgeei P00738.
    CleanExi HS_HP.
    Genevestigatori P00738.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR001314. Peptidase_S1A.
    IPR000436. Sushi_SCR_CCP.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00032. CCP. 2 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEi PS50923. SUSHI. 2 hits.
    PS50240. TRYPSIN_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 165 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

    Keywords - Technical termi

    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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3