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Protein

Inter-alpha-trypsin inhibitor heavy chain H1

Gene

ITIH1

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

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
Complete GO annotation...

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: UniProtKB
  2. extracellular region Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

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
Modified residuei129 – 1291Phosphoserine1 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

BgeeiP19827.
CleanExiHS_ITIH1.
ExpressionAtlasiP19827. baseline and differential.
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.
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.
GeneTreeiENSGT00550000074468.
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. AlignAdd to basket

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

        10         20         30         40         50
MDGAMGPRGL LLCMYLVSLL ILQAMPALGS ATGRSKSSEK RQAVDTAVDG
60 70 80 90 100
VFIRSLKVNC KVTSRFAHYV VTSQVVNTAN EAREVAFDLE IPKTAFISDF
110 120 130 140 150
AVTADGNAFI GDIKDKVTAW KQYRKAAISG ENAGLVRASG RTMEQFTIHL
160 170 180 190 200
TVNPQSKVTF QLTYEEVLKR NHMQYEIVIK VKPKQLVHHF EIDVDIFEPQ
210 220 230 240 250
GISKLDAQAS FLPKELAAQT IKKSFSGKKG HVLFRPTVSQ QQSCPTCSTS
260 270 280 290 300
LLNGHFKVTY DVSRDKICDL LVANNHFAHF FAPQNLTNMN KNVVFVIDIS
310 320 330 340 350
GSMRGQKVKQ TKEALLKILG DMQPGDYFDL VLFGTRVQSW KGSLVQASEA
360 370 380 390 400
NLQAAQDFVR GFSLDEATNL NGGLLRGIEI LNQVQESLPE LSNHASILIM
410 420 430 440 450
LTDGDPTEGV TDRSQILKNV RNAIRGRFPL YNLGFGHNVD FNFLEVMSME
460 470 480 490 500
NNGRAQRIYE DHDATQQLQG FYSQVAKPLL VDVDLQYPQD AVLALTQNHH
510 520 530 540 550
KQYYEGSEIV VAGRIADNKQ SSFKADVQAH GEGQEFSITC LVDEEEMKKL
560 570 580 590 600
LRERGHMLEN HVERLWAYLT IQELLAKRMK VDREERANLS SQALQMSLDY
610 620 630 640 650
GFVTPLTSMS IRGMADQDGL KPTIDKPSED SPPLEMLGPR RTFVLSALQP
660 670 680 690 700
SPTHSSSNTQ RLPDRVTGVD TDPHFIIHVP QKEDTLCFNI NEEPGVILSL
710 720 730 740 750
VQDPNTGFSV NGQLIGNKAR SPGQHDGTYF GRLGIANPAT DFQLEVTPQN
760 770 780 790 800
ITLNPGFGGP VFSWRDQAVL RQDGVVVTIN KKRNLVVSVD DGGTFEVVLH
810 820 830 840 850
RVWKGSSVHQ DFLGFYVLDS HRMSARTHGL LGQFFHPIGF EVSDIHPGSD
860 870 880 890 900
PTKPDATMVV RNRRLTVTRG LQKDYSKDPW HGAEVSCWFI HNNGAGLIDG
910
AYTDYIVPDI F
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP19827.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP19827.
UniCarbKBiP19827.

Proteomic databases

MaxQBiP19827.
PaxDbiP19827.
PeptideAtlasiP19827.
PRIDEiP19827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3697.
GeneCardsiGC03P052811.
HGNCiHGNC:6166. ITIH1.
HPAiHPA041639.
HPA042049.
MIMi147270. gene.
neXtProtiNX_P19827.
PharmGKBiPA29964.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2304.
GeneTreeiENSGT00550000074468.
HOGENOMiHOG000000680.
HOVERGENiHBG057734.
InParanoidiP19827.
OMAiMSMENNG.
OrthoDBiEOG7CRTP5.
PhylomeDBiP19827.
TreeFamiTF328982.

Miscellaneous databases

GeneWikiiITIH1.
GenomeRNAii3697.
NextBioi14491.
PROiP19827.
SOURCEiSearch...

Gene expression databases

BgeeiP19827.
CleanExiHS_ITIH1.
ExpressionAtlasiP19827. baseline and differential.
GenevestigatoriP19827.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. "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: March 4, 2015
This is version 155 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

Similar proteinsi

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