P00738 (HPT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Haptoglobin

Alternative name(s):
Zonulin

Cleaved into the following 2 chains:

1. Haptoglobin alpha chain
2. Haptoglobin beta chain

Gene names

Name:

HP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.27 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.27
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.28
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 process	Acute phase Immunity
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Repeat Signal Sushi
Ligand	Hemoglobin-binding
Molecular function	Antibiotic Antimicrobial Antioxidant Serine protease homolog
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW cellular iron ion homeostasis Non-traceable author statement. Source: UniProtKB defense response Traceable author statement PubMed 7036344. Source: ProtInc defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW metabolic process Inferred from electronic annotation. Source: GOC 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_component	extracellular space Inferred from direct assay PubMed 19433579. Source: MGI haptoglobin-hemoglobin complex Inferred from direct assay PubMed 19740759. Source: BHF-UCL
Molecular_function	antioxidant 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Ref.15
	Chain	19 – 406	388	Haptoglobin		PRO_0000028456
	Chain	19 – 160	142	Haptoglobin alpha chain		PRO_0000028457
	Chain	162 – 406	245	Haptoglobin beta chain		PRO_0000028458
Regions
	Domain	31 – 88	58	Sushi 1
	Domain	90 – 147	58	Sushi 2
	Domain	162 – 404	243	Peptidase S1
	Region	318 – 323	6	Interaction with CD163 By similarity
Amino acid modifications
	Glycosylation	184	1	N-linked (GlcNAc...) Ref.19 Ref.20 Ref.22
	Glycosylation	207	1	N-linked (GlcNAc...) Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
	Glycosylation	211	1	N-linked (GlcNAc...) Ref.19 Ref.20 Ref.21 Ref.22
	Glycosylation	241	1	N-linked (GlcNAc...) (complex) Ref.18 Ref.19 Ref.20 Ref.22 Ref.23
	Disulfide bond	33		Interchain Ref.15 Ref.17
	Disulfide bond	52 ↔ 86		Ref.15 Ref.17
	Disulfide bond	92		Interchain Ref.15 Ref.17
	Disulfide bond	111 ↔ 145		Ref.15 Ref.17
	Disulfide bond	149 ↔ 266		Interchain (between alpha and beta chains) Ref.15 Ref.17
	Disulfide bond	309 ↔ 340		Ref.15 Ref.17
	Disulfide bond	351 ↔ 381		Ref.15 Ref.17
Natural variations
	Natural variant	29 – 87	59	Missing in allele HP*1F and allele HP*1S.		VAR_017112
	Natural variant	129	1	N → D in allele HP*1F. Ref.3 Ref.5		VAR_005294
	Natural variant	130	1	E → K in allele HP*1F. Ref.3		VAR_017113
	Natural variant	247	1	I → T in AHP; causes reduced expression of the protein. Ref.28 Corresponds to variant rs104894517 [ dbSNP | Ensembl ].		VAR_066214
	Natural variant	397	1	D → H. Corresponds to variant rs12646 [ dbSNP | Ensembl ].		VAR_017114
Experimental info
	Sequence conflict	70	1	D → N in AAA52687. Ref.2
	Sequence conflict	130	1	E → G in AAI07588. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P00738 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: A98B56B2B1BE891E	FASTA	406	45,205
	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

References

	« Hide 'large scale' referencesShow '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. , 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 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], VARIANT 29-ALA--GLU-87 DEL. Tissue: Liver.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Plasma.
[20]	"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, MASS SPECTROMETRY. Tissue: Plasma.
[21]	"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, MASS SPECTROMETRY. Tissue: Saliva.
[22]	"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, MASS SPECTROMETRY. Tissue: Liver.
[23]	"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, CARBOHYDRATE STRUCTURE, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[24]	"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.
[25]	"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.
[26]	"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].
[27]	"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.
[28]	"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

GeneReviews

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 , 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. BC107587 mRNA. Translation: AAI07588.1. BC121125 mRNA. Translation: AAI21126.1. M13192 mRNA. No translation available. AC004682 Genomic DNA. Translation: AAC27432.1. X00606 Genomic DNA. Translation: CAA25248.1.
IPI	IPI00641737.
PIR	HPHU2. A92532. HPHU1. A93521.
RefSeq	NP_001119574.1. NM_001126102.1. NP_005134.1. NM_005143.3.
UniGene	Hs.513711. Hs.702099.
3D structure databases
ProteinModelPortal	P00738.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00738. 14 interactions.
STRING	9606.ENSP00000348170.
Protein family/group databases
MEROPS	S01.972.
PTM databases
PhosphoSite	P00738.
Polymorphism databases
DMDM	123508.
2D gel databases
DOSAC-COBS-2DPAGE	P00738.
SWISS-2DPAGE	P00738.
Proteomic databases
PaxDb	P00738.
PRIDE	P00738.
Protocols and materials databases
DNASU	3240.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355906; ENSP00000348170; ENSG00000257017. ENST00000398131; ENSP00000381199; ENSG00000257017. ENST00000570083; ENSP00000457629; ENSG00000257017.
GeneID	3240.
KEGG	hsa:3240.
UCSC	uc002fbr.4. human.
Organism-specific databases
CTD	3240.
GeneCards	GC16P072089.
HGNC	HGNC:5141. HP.
HPA	CAB003787. HPA047750.
MIM	140100. gene. 614081. phenotype.
neXtProt	NX_P00738.
PharmGKB	PA29415.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG246387.
HOVERGEN	HBG005989.
InParanoid	P00738.
KO	K16142.
OrthoDB	EOG4XPQG5.
Enzyme and pathway databases
Pathway_Interaction_DB	amb2_neutrophils_pathway. amb2 Integrin signaling.
Gene expression databases
ArrayExpress	P00738.
Bgee	P00738.
CleanEx	HS_HP.
Genevestigator	P00738.
GermOnline	ENSG00000197711. Homo sapiens.
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR001314. Peptidase_S1A. IPR000436. Sushi_SCR_CCP. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00032. CCP. 2 hits. SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF57535. Complement_control_module. 2 hits. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50923. SUSHI. 2 hits. PS50240. TRYPSIN_DOM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	3240.
NextBio	12895.
SOURCE	Search...

Entry information

Entry name

HPT_HUMAN

Accession

Primary (citable) accession number: P00738
Secondary accession number(s): B0AZL5 , P00737, Q0VAC4, Q2PP15, Q3B7J0, Q6LBY9, Q9UC67

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.