P19823 · ITIH2_HUMAN
- ProteinInter-alpha-trypsin inhibitor heavy chain H2
- GeneITIH2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids946 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | blood microparticle | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Molecular Function | endopeptidase inhibitor activity | |
Molecular Function | hyaluronic acid binding | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Biological Process | hyaluronan metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInter-alpha-trypsin inhibitor heavy chain H2
- Short namesITI heavy chain H2; ITI-HC2; Inter-alpha-inhibitor heavy chain 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP19823
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055248 | 263 | in dbSNP:rs7075296 | |||
Sequence: N → S | ||||||
Natural variant | VAR_055249 | 569 | in dbSNP:rs7084817 | |||
Sequence: L → V | ||||||
Natural variant | VAR_055250 | 674 | in dbSNP:rs3740217 | |||
Sequence: P → A |
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.
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.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-18 | UniProt | |||||
Sequence: MKRLTCFFICFFLSEVSG | |||||||
Propeptide | PRO_0000016517 | 19-54 | UniProt | ||||
Sequence: FEIPINGLSEFVDYEDLVELAPGKFQLVAENRRYQR | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000016518 | 55-702 | UniProt | Inter-alpha-trypsin inhibitor heavy chain H2 | |||
Sequence: SLPGESEEMMEEVDQVTLYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEKTVGRALYAQARAKGKTAGLVRSSALDMENFRTEVNVLPGAKVQFELHYQEVKWRKLGSYEHRIYLQPGRLAKHLEVDVWVIEPQGLRFLHVPDTFEGHFDGVPVISKGQQKAHVSFKPTVAQQRICPNCRETAVDGELVVLYDVKREEKAGELEVFNGYFVHFFAPDNLDPIPKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQPSGGTNINEALLRAIFILNEANNLGLLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLSNENHGIAQRIYGNQDTSSQLKKFYNQVSTPLLRNVQFNYPHTSVTDVTQNNFHNYFGGSEIVVAGKFDPAKLDQIESVITATSANTQLVLETLAQMDDLQDFLSKDKHADPDFTRKLWAYLTINQLLAERSLAPTAAAKRRITRSILQMSLDHHIVTPLTSLVIENEAGDERMLADAPPQDPSCCSGALYYGSKVVPDSTPSWANPSPTPVISMLAQGSQVLESTPPPHVMRVEND | |||||||
Modified residue | 60 | UniProt | Phosphoserine; by FAM20C | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | CAR_000140 | 118 | UniProt | N-linked (GlcNAc...) (complex) asparagine | |||
Sequence: N | |||||||
Disulfide bond | 261↔264 | UniProt | |||||
Sequence: CPNC | |||||||
Modified residue | 282 | UniProt | 4-carboxyglutamate | ||||
Sequence: E | |||||||
Modified residue | 283 | UniProt | 4-carboxyglutamate | ||||
Sequence: E | |||||||
Glycosylation | 445 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 466 | UniProt | Phosphoserine; by FAM20C | ||||
Sequence: S | |||||||
Disulfide bond | 650↔651 | UniProt | |||||
Sequence: CC | |||||||
Glycosylation | CAR_000214 | 666 | UniProt | O-linked (GalNAc...) threonine; partial | |||
Sequence: T | |||||||
Glycosylation | CAR_000215 | 673 | UniProt | O-linked (GalNAc...) serine | |||
Sequence: S | |||||||
Glycosylation | CAR_000216 | 675 | UniProt | O-linked (GalNAc...) threonine | |||
Sequence: T | |||||||
Glycosylation | CAR_000217 | 691 | UniProt | O-linked (GalNAc...) threonine | |||
Sequence: T | |||||||
Modified residue | 702 | UniProt | Aspartate 1-(chondroitin 4-sulfate)-ester | ||||
Sequence: D | |||||||
Propeptide | PRO_0000016519 | 703-946 | UniProt | ||||
Sequence: PHFIIYLPKSQKNICFNIDSEPGKILNLVSDPESGIVVNGQLVGAKKPNNGKLSTYFGKLGFYFQSEDIKIEISTETITLSHGSSTFSLSWSDTAQVTNQRVQISVKKEKVVTITLDKEMSFSVLLHRVWKKHPVNVDFLGIYIPPTNKFSPKAHGLIGQFMQEPKIHIFNERPGKDPEKPEASMEVKGQKLIITRGLQKDYRTDLVFGTDVTCWFVHNSGKGFIDGHYKDYFVPQLYSFLKRP | |||||||
Modified residue | 886 | UniProt | Phosphoserine; by FAM20C | ||||
Sequence: S |
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
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 56-185 | VIT | ||||
Sequence: LPGESEEMMEEVDQVTLYSYKVQSTITSRMATTMIQSKVVNNSPQPQNVVFDVQIPKGAFISNFSMTVDGKTFRSSIKEKTVGRALYAQARAKGKTAGLVRSSALDMENFRTEVNVLPGAKVQFELHYQE | ||||||
Domain | 308-468 | VWFA | ||||
Sequence: PKNILFVIDVSGSMWGVKMKQTVEAMKTILDDLRAEDHFSVIDFNQNIRTWRNDLISATKTQVADAKRYIEKIQPSGGTNINEALLRAIFILNEANNLGLLDPNSVSLIILVSDGDPTVGELKLSKIQKNVKENIQDNISLFSLGMGFDVDYDFLKRLSNE | ||||||
Region | 665-679 | O-glycosylated at three sites | ||||
Sequence: STPSWANPSPTPVIS |
Sequence similarities
Belongs to the ITIH family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length946
- Mass (Da)106,463
- Last updated2009-05-05 v2
- ChecksumBA626B146DDC2A5F
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 374 | in Ref. 6; AA sequence | ||||
Sequence: K → L | ||||||
Sequence conflict | 705 | in Ref. 3; AAA60558 and 4; AAA59195 | ||||
Sequence: F → S | ||||||
Sequence conflict | 729 | in Ref. 3; AAA60558 and 4; AAA59195 | ||||
Sequence: N → D | ||||||
Sequence conflict | 731 | in Ref. 3; AAA60558 and 4; AAA59195 | ||||
Sequence: V → A |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |