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P19827 (ITIH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inter-alpha-trypsin inhibitor heavy chain H1

Short name=ITI heavy chain H1
Short name=ITI-HC1
Short name=Inter-alpha-inhibitor heavy chain 1
Alternative name(s):
Inter-alpha-trypsin inhibitor complex component III
Serum-derived hyaluronan-associated protein
Short name=SHAP
Gene names
Name:ITIH1
Synonyms:IGHEP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.

Contains a potential peptide which could stimulate a broad spectrum of phagocytotic cells.

Subunit structure

I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin.

Subcellular location

Secreted.

Post-translational modification

Heavy chains are linked to bikunin via chondroitin 4-sulfate esterified to the alpha-carboxyl of the C-terminal aspartate after propeptide cleavage.

The S-linked glycan is composed of two 6-carbon sugars, possibly Glc or Gal.

Polymorphism

There are 3 common alleles; ITIH1*1 with Glu-585/Gln-595, ITIH1*2 with Val-585/Arg-595 and ITIH1*3 with Glu-585/Arg-595.

Sequence similarities

Belongs to the ITIH family.

Contains 1 VIT domain.

Contains 1 VWFA domain.

Mass spectrometry

Molecular mass is 76258 Da from positions 28 - 672. Determined by MALDI. Ref.15

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19827-1)

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: P19827-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-142: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P19827-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-288: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 347
PRO_0000016506
Chain35 – 672638Inter-alpha-trypsin inhibitor heavy chain H1
PRO_0000016507
Propeptide673 – 911239
PRO_0000016508

Regions

Domain37 – 166130VIT
Domain290 – 450161VWFA
Region387 – 911525Hyaluronan-binding
Motif181 – 1844Phagocytosis uptake signal Potential

Amino acid modifications

Modified residue4021Phosphothreonine Ref.19
Modified residue4071Phosphothreonine Ref.19
Modified residue6721Aspartate 1-(chondroitin 4-sulfate)-ester
Glycosylation601S-linked (Hex...) Ref.16
Glycosylation2851N-linked (GlcNAc...) (complex) Ref.15 Ref.16 Ref.17 Ref.21
CAR_000138
Glycosylation5881N-linked (GlcNAc...) (complex) Ref.15 Ref.16 Ref.18
CAR_000139
Glycosylation6531O-linked (GalNAc...) Ref.16
CAR_000213
Glycosylation7501N-linked (GlcNAc...) Ref.20
Disulfide bond244 ↔ 247 Ref.16
Disulfide bond268 ↔ 540 Ref.16

Natural variations

Alternative sequence1 – 288288Missing in isoform 3.
VSP_045419
Alternative sequence1 – 142142Missing in isoform 2.
VSP_045420
Natural variant2631S → T. Ref.1
Corresponds to variant rs1042777 [ dbSNP | Ensembl ].
VAR_011873
Natural variant5851E → V in allele ITIH1*2. Ref.1 Ref.3 Ref.22
Corresponds to variant rs678 [ dbSNP | Ensembl ].
VAR_004019
Natural variant5951Q → R in allele ITIH1*2 and allele ITIH1*3. Ref.1 Ref.3 Ref.22
Corresponds to variant rs1042779 [ dbSNP | Ensembl ].
VAR_004020
Natural variant6951G → C.
Corresponds to variant rs1042904 [ dbSNP | Ensembl ].
VAR_011874
Natural variant8441D → E.
Corresponds to variant rs1042849 [ dbSNP | Ensembl ].
VAR_011875

Experimental info

Sequence conflict511V → T AA sequence Ref.8
Sequence conflict541R → A AA sequence Ref.8
Sequence conflict2661K → E in CAA45188. Ref.1
Sequence conflict5391T → A in BAH12794. Ref.3
Sequence conflict7981V → A in BAH12794. Ref.3

Sequences

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

Last modified July 15, 1998. Version 3.
Checksum: 8FE715FF223FC917

FASTA911101,389
        10         20         30         40         50         60 
MDGAMGPRGL LLCMYLVSLL ILQAMPALGS ATGRSKSSEK RQAVDTAVDG VFIRSLKVNC 

        70         80         90        100        110        120 
KVTSRFAHYV VTSQVVNTAN EAREVAFDLE IPKTAFISDF AVTADGNAFI GDIKDKVTAW 

       130        140        150        160        170        180 
KQYRKAAISG ENAGLVRASG RTMEQFTIHL TVNPQSKVTF QLTYEEVLKR NHMQYEIVIK 

       190        200        210        220        230        240 
VKPKQLVHHF EIDVDIFEPQ GISKLDAQAS FLPKELAAQT IKKSFSGKKG HVLFRPTVSQ 

       250        260        270        280        290        300 
QQSCPTCSTS LLNGHFKVTY DVSRDKICDL LVANNHFAHF FAPQNLTNMN KNVVFVIDIS 

       310        320        330        340        350        360 
GSMRGQKVKQ TKEALLKILG DMQPGDYFDL VLFGTRVQSW KGSLVQASEA NLQAAQDFVR 

       370        380        390        400        410        420 
GFSLDEATNL NGGLLRGIEI LNQVQESLPE LSNHASILIM LTDGDPTEGV TDRSQILKNV 

       430        440        450        460        470        480 
RNAIRGRFPL YNLGFGHNVD FNFLEVMSME NNGRAQRIYE DHDATQQLQG FYSQVAKPLL 

       490        500        510        520        530        540 
VDVDLQYPQD AVLALTQNHH KQYYEGSEIV VAGRIADNKQ SSFKADVQAH GEGQEFSITC 

       550        560        570        580        590        600 
LVDEEEMKKL LRERGHMLEN HVERLWAYLT IQELLAKRMK VDREERANLS SQALQMSLDY 

       610        620        630        640        650        660 
GFVTPLTSMS IRGMADQDGL KPTIDKPSED SPPLEMLGPR RTFVLSALQP SPTHSSSNTQ 

       670        680        690        700        710        720 
RLPDRVTGVD TDPHFIIHVP QKEDTLCFNI NEEPGVILSL VQDPNTGFSV NGQLIGNKAR 

       730        740        750        760        770        780 
SPGQHDGTYF GRLGIANPAT DFQLEVTPQN ITLNPGFGGP VFSWRDQAVL RQDGVVVTIN 

       790        800        810        820        830        840 
KKRNLVVSVD DGGTFEVVLH RVWKGSSVHQ DFLGFYVLDS HRMSARTHGL LGQFFHPIGF 

       850        860        870        880        890        900 
EVSDIHPGSD PTKPDATMVV RNRRLTVTRG LQKDYSKDPW HGAEVSCWFI HNNGAGLIDG 

       910 
AYTDYIVPDI F 

« Hide

Isoform 2 [UniParc].

Checksum: 9447D42CB083BC9F
Show »

FASTA76986,192
Isoform 3 [UniParc].

Checksum: EBB1BB3250D74DA7
Show »

FASTA62369,495

References

« Hide 'large scale' references
[1]"Human inter-alpha-trypsin inhibitor: full-length cDNA sequence of the heavy chain H1."
Diarra-Mehrpour M., Bourguignon J., Bost F., Sesboue R., Muschio F., Sarafan N., Martin J.-P.
Biochim. Biophys. Acta 1132:114-118(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-263; VAL-585 AND ARG-595.
Tissue: Blood and Liver.
[2]"Isolation and characterization of the human inter-alpha-trypsin inhibitor heavy-chain H1 gene."
Bost F., Bourguignon J., Martin J.-P., Sesboue R., Thiberville L., Diarra-Mehrpour M.
Eur. J. Biochem. 218:283-291(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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] (ISOFORMS 1; 2 AND 3), VARIANTS VAL-585 AND ARG-595.
Tissue: Liver and Thymus.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
[7]"The heavy chains of human plasma inter-alpha-trypsin inhibitor: their isolation, their identification by electrophoresis and partial sequencing. Differential reactivity with concanavalin A."
Malki N., Balduyck M., Maes P., Capon C., Mizon C., Han K.K., Tartar A., Fournet B., Mizon J.
Biol. Chem. Hoppe-Seyler 373:1009-1018(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-34; 117-119; 126-137; 318-329; 342-355 AND 478-501.
Tissue: Plasma.
[8]"Analysis of inter-alpha-trypsin inhibitor and a novel trypsin inhibitor, pre-alpha-trypsin inhibitor, from human plasma. Polypeptide chain stoichiometry and assembly by glycan."
Enghild J.J., Thoegersen I.B., Pizzo S.V., Salvesen G.
J. Biol. Chem. 264:15975-15981(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-54; 110-124; 333-347 AND 399-435.
Tissue: Plasma.
[9]"Two out of the three kinds of subunits of inter-alpha-trypsin inhibitor are structurally related."
Gebhard W., Schreitmueller T., Hochstrasser K., Wachter E.
Eur. J. Biochem. 181:571-576(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-911 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[10]"A serum-derived hyaluronan-associated protein (SHAP) is the heavy chain of the inter alpha-trypsin inhibitor."
Huang L., Yoneda M., Kimata K.
J. Biol. Chem. 268:26725-26730(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 177-211 AND 387-428, HYALURONAN BINDING.
Tissue: Serum.
[11]"Isolation and characterization of cDNAs encoding the heavy chain of human inter-alpha-trypsin inhibitor (I alpha TI): unambiguous evidence for multipolypeptide chain structure of I alpha TI."
Salier J.-P., Diarra-Mehrpour M., Sesboue R., Bourguignon J., Benarous R., Ohkubo I., Kurachi S., Kurachi K., Martin J.-P.
Proc. Natl. Acad. Sci. U.S.A. 84:8272-8276(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 399-723 (ISOFORM 1/2/3).
[12]"cDNA cloning of human inter-alpha-trypsin inhibitor discloses three different proteins."
Schreitmueller T., Hochstrasser K., Resinger P.W.M., Wachter E., Gebhard W.
Biol. Chem. Hoppe-Seyler 368:963-970(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 535-685 (ISOFORM 1/2/3).
[13]"Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor."
Morelle W., Capon C., Balduyck M., Sautiere P., Kouach M., Michalski C., Fournet B., Mizon J.
Eur. J. Biochem. 221:881-888(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 669-672, COVALENT LINKAGE WITH CHONDROITIN SULFATE.
Tissue: Plasma.
[14]"Tandem orientation of the inter-alpha-trypsin inhibitor heavy chain H1 and H3 genes."
Diarra-Mehrpour M., Bourguignon J., Sarafan N., Bost F., Sesbouee R., Muschio-Bonnet F., Martin J.-P.
Biochim. Biophys. Acta 1219:551-554(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 870-911.
[15]"Glycosylation pattern of human inter-alpha-inhibitor heavy chains."
Flahaut C., Capon C., Balduyck M., Ricart G., Sautiere P., Mizon J.
Biochem. J. 333:749-756(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-285 AND ASN-588, MASS SPECTROMETRY.
[16]"Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2."
Olsen E.H.N., Rahbek-Nielsen H., Thoegersen I.B., Roepstorff P., Enghild J.J.
Biochemistry 37:408-416(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT CYS-60; ASN-285; ASN-588 AND THR-653, DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"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-285.
[18]"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-588.
Tissue: Plasma.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-402 AND THR-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-750.
Tissue: Liver.
[21]"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-285.
[22]"Molecular basis of inter-alpha-trypsin inhibitor heavy chain H1 (ITIH1) polymorphism."
Ding M., Umetsu K., Yuasa I., Sato M., Harada A., Suzuki T.
Hum. Genet. 95:435-436(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-585 AND ARG-595.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63652 mRNA. Translation: CAA45188.1.
X69532 expand/collapse EMBL AC list , X69533, X69534, X69535, X69536, X69537, X69538, X69539, X69540, X69541, X69542, X69543, X69544, X69545, X69546, X69547 Genomic DNA. Translation: CAA49279.1.
AK292750 mRNA. Translation: BAF85439.1.
AK298455 mRNA. Translation: BAH12794.1.
AK303156 mRNA. Translation: BAH13906.1.
AK314198 mRNA. Translation: BAG36876.1.
AC006254 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65259.1.
BC069464 mRNA. Translation: AAH69464.1.
X16260 mRNA. Translation: CAA34346.1.
M18192 mRNA. Translation: AAA60557.1.
X75318 Genomic DNA. Translation: CAA53067.1.
CCDSCCDS2864.1. [P19827-1]
CCDS54594.1. [P19827-2]
CCDS54595.1. [P19827-3]
PIRA39967. S39527.
RefSeqNP_001159906.1. NM_001166434.2. [P19827-2]
NP_001159907.1. NM_001166435.2. [P19827-3]
NP_002206.2. NM_002215.3. [P19827-1]
UniGeneHs.420257.
Hs.76716.

3D structure databases

ProteinModelPortalP19827.
SMRP19827. Positions 290-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109903. 3 interactions.
IntActP19827. 2 interactions.
STRING9606.ENSP00000273283.

PTM databases

PhosphoSiteP19827.
UniCarbKBP19827.

Proteomic databases

MaxQBP19827.
PaxDbP19827.
PeptideAtlasP19827.
PRIDEP19827.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273283; ENSP00000273283; ENSG00000055957. [P19827-1]
ENST00000537050; ENSP00000443847; ENSG00000055957. [P19827-3]
ENST00000540715; ENSP00000443973; ENSG00000055957. [P19827-2]
GeneID3697.
KEGGhsa:3697.
UCSCuc003dfs.3. human. [P19827-1]

Organism-specific databases

CTD3697.
GeneCardsGC03P052811.
HGNCHGNC:6166. ITIH1.
HPAHPA041639.
HPA042049.
MIM147270. gene.
neXtProtNX_P19827.
PharmGKBPA29964.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2304.
HOGENOMHOG000000680.
HOVERGENHBG057734.
InParanoidP19827.
OMAMSMENNG.
OrthoDBEOG7CRTP5.
PhylomeDBP19827.
TreeFamTF328982.

Gene expression databases

ArrayExpressP19827.
BgeeP19827.
CleanExHS_ITIH1.
GenevestigatorP19827.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR010600. ITI_HC_C.
IPR013694. VIT.
IPR002035. VWF_A.
[Graphical view]
PfamPF06668. ITI_HC_C. 1 hit.
PF08487. VIT. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
SMARTSM00609. VIT. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
PROSITEPS51468. VIT. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiITIH1.
GenomeRNAi3697.
NextBio14491.
PROP19827.
SOURCESearch...

Entry information

Entry nameITIH1_HUMAN
AccessionPrimary (citable) accession number: P19827
Secondary accession number(s): A8K9N5 expand/collapse secondary AC list , B2RAH9, B7Z558, B7Z8C0, F5H165, F5H7Y8, P78455, Q01746, Q562G1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 150 of the entry and version 3 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

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 3

Human chromosome 3: entries, gene names and cross-references to MIM