P19823 · ITIH2_HUMAN

  • Protein
    Inter-alpha-trypsin inhibitor heavy chain H2
  • Gene
    ITIH2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentblood microparticle
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentendoplasmic reticulum lumen
Cellular Componentextracellular exosome
Cellular Componentextracellular region
Molecular Functionendopeptidase inhibitor activity
Molecular Functionhyaluronic acid binding
Molecular Functionserine-type endopeptidase inhibitor activity
Biological Processhyaluronan metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inter-alpha-trypsin inhibitor heavy chain H2
  • Short names
    ITI heavy chain H2; ITI-HC2; Inter-alpha-inhibitor heavy chain 2
  • Alternative names
    • Inter-alpha-trypsin inhibitor complex component II
    • Serum-derived hyaluronan-associated protein (SHAP)

Gene names

    • Name
      ITIH2
    • Synonyms
      IGHEP2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P19823
  • Secondary accessions
    • Q14659
    • Q15484
    • Q5T986

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_055248263in dbSNP:rs7075296
Natural variantVAR_055249569in dbSNP:rs7084817
Natural variantVAR_055250674in dbSNP:rs3740217

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,146 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, propeptide, modified residue (large scale data), chain, modified residue, glycosylation, disulfide bond.

TypeIDPosition(s)SourceDescription
Signal1-18UniProt
PropeptidePRO_000001651719-54UniProt
Modified residue (large scale data)55PRIDEPhosphoserine
ChainPRO_000001651855-702UniProtInter-alpha-trypsin inhibitor heavy chain H2
Modified residue60UniProtPhosphoserine; by FAM20C
Modified residue (large scale data)60PRIDEPhosphoserine
GlycosylationCAR_000140118UniProtN-linked (GlcNAc...) (complex) asparagine
Disulfide bond261↔264UniProt
Modified residue282UniProt4-carboxyglutamate
Modified residue283UniProt4-carboxyglutamate
Glycosylation445UniProtN-linked (GlcNAc...) asparagine
Modified residue466UniProtPhosphoserine; by FAM20C
Disulfide bond650↔651UniProt
GlycosylationCAR_000214666UniProtO-linked (GalNAc...) threonine; partial
GlycosylationCAR_000215673UniProtO-linked (GalNAc...) serine
GlycosylationCAR_000216675UniProtO-linked (GalNAc...) threonine
GlycosylationCAR_000217691UniProtO-linked (GalNAc...) threonine
Modified residue702UniProtAspartate 1-(chondroitin 4-sulfate)-ester
PropeptidePRO_0000016519703-946UniProt
Modified residue886UniProtPhosphoserine; by FAM20C

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.
N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.
Phosphorylated by FAM20C in the extracellular medium.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Plasma.

Gene expression databases

Organism-specific databases

Interaction

Subunit

I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (HC) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of ITIH1/HC1, ITIH2/HC2 and bikunin.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain56-185VIT
Domain308-468VWFA
Region665-679O-glycosylated at three sites

Sequence similarities

Belongs to the ITIH family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    946
  • Mass (Da)
    106,463
  • Last updated
    2009-05-05 v2
  • Checksum
    BA626B146DDC2A5F
MKRLTCFFICFFLSEVSGFEIPINGLSEFVDYEDLVELAPGKFQLVAENRRYQRSLPGESEEMMEEVDQVTLYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEKTVGRALYAQARAKGKTAGLVRSSALDMENFRTEVNVLPGAKVQFELHYQEVKWRKLGSYEHRIYLQPGRLAKHLEVDVWVIEPQGLRFLHVPDTFEGHFDGVPVISKGQQKAHVSFKPTVAQQRICPNCRETAVDGELVVLYDVKREEKAGELEVFNGYFVHFFAPDNLDPIPKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQPSGGTNINEALLRAIFILNEANNLGLLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLSNENHGIAQRIYGNQDTSSQLKKFYNQVSTPLLRNVQFNYPHTSVTDVTQNNFHNYFGGSEIVVAGKFDPAKLDQIESVITATSANTQLVLETLAQMDDLQDFLSKDKHADPDFTRKLWAYLTINQLLAERSLAPTAAAKRRITRSILQMSLDHHIVTPLTSLVIENEAGDERMLADAPPQDPSCCSGALYYGSKVVPDSTPSWANPSPTPVISMLAQGSQVLESTPPPHVMRVENDPHFIIYLPKSQKNICFNIDSEPGKILNLVSDPESGIVVNGQLVGAKKPNNGKLSTYFGKLGFYFQSEDIKIEISTETITLSHGSSTFSLSWSDTAQVTNQRVQISVKKEKVVTITLDKEMSFSVLLHRVWKKHPVNVDFLGIYIPPTNKFSPKAHGLIGQFMQEPKIHIFNERPGKDPEKPEASMEVKGQKLIITRGLQKDYRTDLVFGTDVTCWFVHNSGKGFIDGHYKDYFVPQLYSFLKRP

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q5T985Q5T985_HUMANITIH2935
Q5T987Q5T987_HUMANITIH2237

Sequence caution

The sequence CAA30160.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict374in Ref. 6; AA sequence
Sequence conflict705in Ref. 3; AAA60558 and 4; AAA59195
Sequence conflict729in Ref. 3; AAA60558 and 4; AAA59195
Sequence conflict731in Ref. 3; AAA60558 and 4; AAA59195

Mass Spectrometry

Molecular mass is 76,508 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X07173
EMBL· GenBank· DDBJ
CAA30160.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AL158044
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
M18193
EMBL· GenBank· DDBJ
AAA60558.1
EMBL· GenBank· DDBJ
mRNA
M33033
EMBL· GenBank· DDBJ
AAA59195.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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