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P19827

- ITIH1_HUMAN

UniProt

P19827 - ITIH1_HUMAN

Protein

Inter-alpha-trypsin inhibitor heavy chain H1

Gene

ITIH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. calcium ion binding Source: ProtInc
    2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. hyaluronan metabolic process Source: InterPro

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ITIH1
    Synonyms:IGHEP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6166. ITIH1.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29964.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Propeptidei28 – 3471 PublicationPRO_0000016506
    Chaini35 – 672638Inter-alpha-trypsin inhibitor heavy chain H1PRO_0000016507Add
    BLAST
    Propeptidei673 – 911239PRO_0000016508Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi60 – 601S-linked (Hex...)1 Publication
    Disulfide bondi244 ↔ 2471 Publication
    Disulfide bondi268 ↔ 5401 Publication
    Glycosylationi285 – 2851N-linked (GlcNAc...) (complex)4 PublicationsCAR_000138
    Modified residuei402 – 4021Phosphothreonine1 Publication
    Modified residuei407 – 4071Phosphothreonine1 Publication
    Glycosylationi588 – 5881N-linked (GlcNAc...) (complex)3 PublicationsCAR_000139
    Glycosylationi653 – 6531O-linked (GalNAc...)1 PublicationCAR_000213
    Modified residuei672 – 6721Aspartate 1-(chondroitin 4-sulfate)-ester
    Glycosylationi750 – 7501N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    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.6 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

    Proteomic databases

    MaxQBiP19827.
    PaxDbiP19827.
    PeptideAtlasiP19827.
    PRIDEiP19827.

    PTM databases

    PhosphoSiteiP19827.
    UniCarbKBiP19827.

    Expressioni

    Gene expression databases

    ArrayExpressiP19827.
    BgeeiP19827.
    CleanExiHS_ITIH1.
    GenevestigatoriP19827.

    Organism-specific databases

    HPAiHPA041639.
    HPA042049.

    Interactioni

    Subunit structurei

    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.

    Protein-protein interaction databases

    BioGridi109903. 3 interactions.
    IntActiP19827. 2 interactions.
    STRINGi9606.ENSP00000273283.

    Structurei

    3D structure databases

    ProteinModelPortaliP19827.
    SMRiP19827. Positions 290-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 166130VITPROSITE-ProRule annotationAdd
    BLAST
    Domaini290 – 450161VWFAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni387 – 911525Hyaluronan-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi181 – 1844Phagocytosis uptake signalSequence Analysis

    Sequence similaritiesi

    Belongs to the ITIH family.Curated
    Contains 1 VIT domain.PROSITE-ProRule annotation
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2304.
    HOGENOMiHOG000000680.
    HOVERGENiHBG057734.
    InParanoidiP19827.
    OMAiMSMENNG.
    OrthoDBiEOG7CRTP5.
    PhylomeDBiP19827.
    TreeFamiTF328982.

    Family and domain databases

    Gene3Di3.40.50.410. 1 hit.
    InterProiIPR010600. ITI_HC_C.
    IPR013694. VIT.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF06668. ITI_HC_C. 1 hit.
    PF08487. VIT. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    SMARTiSM00609. VIT. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    PROSITEiPS51468. VIT. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19827-1) [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

    MDGAMGPRGL LLCMYLVSLL ILQAMPALGS ATGRSKSSEK RQAVDTAVDG    50
    VFIRSLKVNC KVTSRFAHYV VTSQVVNTAN EAREVAFDLE IPKTAFISDF 100
    AVTADGNAFI GDIKDKVTAW KQYRKAAISG ENAGLVRASG RTMEQFTIHL 150
    TVNPQSKVTF QLTYEEVLKR NHMQYEIVIK VKPKQLVHHF EIDVDIFEPQ 200
    GISKLDAQAS FLPKELAAQT IKKSFSGKKG HVLFRPTVSQ QQSCPTCSTS 250
    LLNGHFKVTY DVSRDKICDL LVANNHFAHF FAPQNLTNMN KNVVFVIDIS 300
    GSMRGQKVKQ TKEALLKILG DMQPGDYFDL VLFGTRVQSW KGSLVQASEA 350
    NLQAAQDFVR GFSLDEATNL NGGLLRGIEI LNQVQESLPE LSNHASILIM 400
    LTDGDPTEGV TDRSQILKNV RNAIRGRFPL YNLGFGHNVD FNFLEVMSME 450
    NNGRAQRIYE DHDATQQLQG FYSQVAKPLL VDVDLQYPQD AVLALTQNHH 500
    KQYYEGSEIV VAGRIADNKQ SSFKADVQAH GEGQEFSITC LVDEEEMKKL 550
    LRERGHMLEN HVERLWAYLT IQELLAKRMK VDREERANLS SQALQMSLDY 600
    GFVTPLTSMS IRGMADQDGL KPTIDKPSED SPPLEMLGPR RTFVLSALQP 650
    SPTHSSSNTQ RLPDRVTGVD TDPHFIIHVP QKEDTLCFNI NEEPGVILSL 700
    VQDPNTGFSV NGQLIGNKAR SPGQHDGTYF GRLGIANPAT DFQLEVTPQN 750
    ITLNPGFGGP VFSWRDQAVL RQDGVVVTIN KKRNLVVSVD DGGTFEVVLH 800
    RVWKGSSVHQ DFLGFYVLDS HRMSARTHGL LGQFFHPIGF EVSDIHPGSD 850
    PTKPDATMVV RNRRLTVTRG LQKDYSKDPW HGAEVSCWFI HNNGAGLIDG 900
    AYTDYIVPDI F 911
    Length:911
    Mass (Da):101,389
    Last modified:July 15, 1998 - v3
    Checksum:i8FE715FF223FC917
    GO
    Isoform 2 (identifier: P19827-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-142: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:769
    Mass (Da):86,192
    Checksum:i9447D42CB083BC9F
    GO
    Isoform 3 (identifier: P19827-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-288: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:623
    Mass (Da):69,495
    Checksum:iEBB1BB3250D74DA7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511V → T AA sequence (PubMed:2476436)Curated
    Sequence conflicti54 – 541R → A AA sequence (PubMed:2476436)Curated
    Sequence conflicti266 – 2661K → E in CAA45188. (PubMed:1380832)Curated
    Sequence conflicti539 – 5391T → A in BAH12794. (PubMed:14702039)Curated
    Sequence conflicti798 – 7981V → A in BAH12794. (PubMed:14702039)Curated

    Mass spectrometryi

    Molecular mass is 76258 Da from positions 28 - 672. Determined by MALDI. 1 Publication

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti263 – 2631S → T.1 Publication
    Corresponds to variant rs1042777 [ dbSNP | Ensembl ].
    VAR_011873
    Natural varianti585 – 5851E → V in allele ITIH1*2. 3 Publications
    Corresponds to variant rs678 [ dbSNP | Ensembl ].
    VAR_004019
    Natural varianti595 – 5951Q → R in allele ITIH1*2 and allele ITIH1*3. 3 Publications
    Corresponds to variant rs1042779 [ dbSNP | Ensembl ].
    VAR_004020
    Natural varianti695 – 6951G → C.
    Corresponds to variant rs1042904 [ dbSNP | Ensembl ].
    VAR_011874
    Natural varianti844 – 8441D → E.
    Corresponds to variant rs1042849 [ dbSNP | Ensembl ].
    VAR_011875

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 288288Missing in isoform 3. 1 PublicationVSP_045419Add
    BLAST
    Alternative sequencei1 – 142142Missing in isoform 2. 1 PublicationVSP_045420Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63652 mRNA. Translation: CAA45188.1.
    X69532
    , 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.
    CCDSiCCDS2864.1. [P19827-1]
    CCDS54594.1. [P19827-2]
    CCDS54595.1. [P19827-3]
    PIRiS39527. A39967.
    RefSeqiNP_001159906.1. NM_001166434.2. [P19827-2]
    NP_001159907.1. NM_001166435.2. [P19827-3]
    NP_002206.2. NM_002215.3. [P19827-1]
    UniGeneiHs.420257.
    Hs.76716.

    Genome annotation databases

    EnsembliENST00000273283; ENSP00000273283; ENSG00000055957. [P19827-1]
    ENST00000537050; ENSP00000443847; ENSG00000055957. [P19827-3]
    GeneIDi3697.
    KEGGihsa:3697.
    UCSCiuc003dfs.3. human. [P19827-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63652 mRNA. Translation: CAA45188.1 .
    X69532
    , 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 .
    CCDSi CCDS2864.1. [P19827-1 ]
    CCDS54594.1. [P19827-2 ]
    CCDS54595.1. [P19827-3 ]
    PIRi S39527. A39967.
    RefSeqi NP_001159906.1. NM_001166434.2. [P19827-2 ]
    NP_001159907.1. NM_001166435.2. [P19827-3 ]
    NP_002206.2. NM_002215.3. [P19827-1 ]
    UniGenei Hs.420257.
    Hs.76716.

    3D structure databases

    ProteinModelPortali P19827.
    SMRi P19827. Positions 290-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109903. 3 interactions.
    IntActi P19827. 2 interactions.
    STRINGi 9606.ENSP00000273283.

    PTM databases

    PhosphoSitei P19827.
    UniCarbKBi P19827.

    Proteomic databases

    MaxQBi P19827.
    PaxDbi P19827.
    PeptideAtlasi P19827.
    PRIDEi P19827.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273283 ; ENSP00000273283 ; ENSG00000055957 . [P19827-1 ]
    ENST00000537050 ; ENSP00000443847 ; ENSG00000055957 . [P19827-3 ]
    GeneIDi 3697.
    KEGGi hsa:3697.
    UCSCi uc003dfs.3. human. [P19827-1 ]

    Organism-specific databases

    CTDi 3697.
    GeneCardsi GC03P052811.
    HGNCi HGNC:6166. ITIH1.
    HPAi HPA041639.
    HPA042049.
    MIMi 147270. gene.
    neXtProti NX_P19827.
    PharmGKBi PA29964.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2304.
    HOGENOMi HOG000000680.
    HOVERGENi HBG057734.
    InParanoidi P19827.
    OMAi MSMENNG.
    OrthoDBi EOG7CRTP5.
    PhylomeDBi P19827.
    TreeFami TF328982.

    Miscellaneous databases

    GeneWikii ITIH1.
    GenomeRNAii 3697.
    NextBioi 14491.
    PROi P19827.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19827.
    Bgeei P19827.
    CleanExi HS_ITIH1.
    Genevestigatori P19827.

    Family and domain databases

    Gene3Di 3.40.50.410. 1 hit.
    InterProi IPR010600. ITI_HC_C.
    IPR013694. VIT.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF06668. ITI_HC_C. 1 hit.
    PF08487. VIT. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    SMARTi SM00609. VIT. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    PROSITEi PS51468. VIT. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiITIH1_HUMAN
    AccessioniPrimary (citable) accession number: P19827
    Secondary accession number(s): A8K9N5
    , B2RAH9, B7Z558, B7Z8C0, F5H165, F5H7Y8, P78455, Q01746, Q562G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 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 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3