Q14624 · ITIH4_HUMAN
- ProteinInter-alpha-trypsin inhibitor heavy chain H4
- GeneITIH4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids930 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Peptides derived from the proline-rich potentially active peptide (PRO_0000016542) may be biomarkers for a variety of disease states including breast cancer (PubMed:21137033).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 688-689 | Cleavage; by kallikrein | ||||
Sequence: RR |
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 | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Cellular Component | platelet dense granule lumen | |
Molecular Function | endopeptidase inhibitor activity | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Biological Process | acute-phase response | |
Biological Process | hyaluronan metabolic process | |
Biological Process | response to cytokine |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInter-alpha-trypsin inhibitor heavy chain H4
- Short namesITI heavy chain H4; ITI-HC4; Inter-alpha-inhibitor heavy chain 4
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14624
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_027869 | 85 | in dbSNP:rs13072536 | |||
Sequence: I → N | ||||||
Natural variant | VAR_013836 | 86 | ||||
Sequence: I → N | ||||||
Natural variant | VAR_027870 | 669 | in dbSNP:rs2276814 | |||
Sequence: Q → L | ||||||
Natural variant | VAR_027871 | 698 | in dbSNP:rs4687657 | |||
Sequence: P → T | ||||||
Natural variant | VAR_027872 | 714 | in dbSNP:rs2256734 | |||
Sequence: M → I | ||||||
Natural variant | VAR_027873 | 791 | in dbSNP:rs2535621 | |||
Sequence: L → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,003 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, chain, glycosylation, modified residue (large scale data), propeptide, disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-28 | UniProt | |||||
Sequence: MKPPRPVRTCSKVLVLLSLLAIHQTTTA | |||||||
Chain | PRO_0000016541 | 29-661 | UniProt | 70 kDa inter-alpha-trypsin inhibitor heavy chain H4 | |||
Sequence: EKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRANTVQEATFQMELPKKAFITNFSMIIDGMTYPGIIKEKAEAQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEELLKRRLGVYELLLKVRPQQLVKHLQMDIHIFEPQGISFLETESTFMTNQLVDALTTWQNKTKAHIRFKPTLSQQQKSPEQQETVLDGNLIIRYDVDRAISGGSIQIENGYFVHYFAPEGLTTMPKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNKARSFAAGIQALGGTNINDAMLMAVQLLDSSNQEERLPEGSVSLIILLTDGDPTVGETNPRSIQNNVREAVSGRYSLFCLGFGFDVSYAFLEKLALDNGGLARRIHEDSDSALQLQDFYQEVANPLLTAVTFEYPSNAVEEVTQNNFRLLFKGSEMVVAGKLQDRGPDVLTATVSGKLPTQNITFQTESSVAEQEAEFQSPKYIFHNFMERLWAYLTIQQLLEQTVSASDADQQALRNQALNLSLAYSFVTPLTSMVVTKPDDQEQSQVAEKPMEGESRNRNVHSGSTFFKYYLQGAKIPKPEASFSPRRGWNRQAGAAGSRMNFR | |||||||
Glycosylation | 81 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 207 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 274 | UniProt | N-linked (GlcNAc...) asparagine; atypical | ||||
Sequence: N | |||||||
Glycosylation | 517 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 577 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 622 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Propeptide | PRO_0000016542 | 662-688 | UniProt | Potentially active peptide | |||
Sequence: PGVLSSRQLGLPGPPDVPDHAAYHPFR | |||||||
Chain | PRO_0000016543 | 689-930 | UniProt | 35 kDa inter-alpha-trypsin inhibitor heavy chain H4 | |||
Sequence: RLAILPASAPPATSNPDPAVSRVMNMKIEETTMTTQTPAPIQAPSAILPLPGQSVERLCVDPRHRQGPVNLLSDPEQGVEVTGQYEREKAGFSWIEVTFKNPLVWVHASPEHVVVTRNRRSSAYKWKETLFSVMPGLKMTMDKTGLLLLSDPDKVTIGLLFWDGRGEGLRLLLRDTDRFSSHVGGTLGQFYQEVLWGSPAASDDGRRTLRVQGNDHSATRERRLDYQEGPPGVEISCWSVEL | |||||||
Glycosylation | 719 | UniProt | O-linked (GalNAc...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 720 | UniProt | O-linked (GalNAc...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 722 | UniProt | O-linked (GalNAc...) threonine | ||||
Sequence: T | |||||||
Disulfide bond | 747↔925 | UniProt | |||||
Sequence: CVDPRHRQGPVNLLSDPEQGVEVTGQYEREKAGFSWIEVTFKNPLVWVHASPEHVVVTRNRRSSAYKWKETLFSVMPGLKMTMDKTGLLLLSDPDKVTIGLLFWDGRGEGLRLLLRDTDRFSSHVGGTLGQFYQEVLWGSPAASDDGRRTLRVQGNDHSATRERRLDYQEGPPGVEISC | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-148 | VIT | ||||
Sequence: EKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRANTVQEATFQMELPKKAFITNFSMIIDGMTYPGIIKEKAEAQAQYSAAVAKGKSAGLVKATGRNMEQFQVSVSVAPNAKITFELVYEE | ||||||
Domain | 272-432 | VWFA | ||||
Sequence: PKNVVFVIDKSGSMSGRKIQQTREALIKILDDLSPRDQFNLIVFSTEATQWRPSLVPASAENVNKARSFAAGIQALGGTNINDAMLMAVQLLDSSNQEERLPEGSVSLIILLTDGDPTVGETNPRSIQNNVREAVSGRYSLFCLGFGFDVSYAFLEKLALD | ||||||
Region | 595-618 | Disordered | ||||
Sequence: KPDDQEQSQVAEKPMEGESRNRNV | ||||||
Compositional bias | 600-614 | Basic and acidic residues | ||||
Sequence: EQSQVAEKPMEGESR | ||||||
Region | 658-688 | Proline-rich (PRR) potential bioactive peptide | ||||
Sequence: MNFRPGVLSSRQLGLPGPPDVPDHAAYHPFR | ||||||
Region | 719-725 | O-glycosylated at three sites | ||||
Sequence: TTMTTQT |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 4 isoforms produced by Alternative splicing.
Q14624-1
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.
- Name1
- Length930
- Mass (Da)103,357
- Last updated2009-05-05 v4
- Checksum847A9A5CB886C5A4
Q14624-2
- Name2
Q14624-3
- Name3
- Differences from canonical
- 621-650: Missing
Q14624-4
- Name4
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 85 | in Ref. 3; AAD05198 | ||||
Sequence: I → K | ||||||
Sequence conflict | 114 | in Ref. 2; BAA07602 | ||||
Sequence: S → N | ||||||
Sequence conflict | 207 | in Ref. 8; AA sequence | ||||
Sequence: N → F | ||||||
Sequence conflict | 221 | in Ref. 8; AA sequence | ||||
Sequence: Q → E | ||||||
Sequence conflict | 307 | in Ref. 8; AA sequence | ||||
Sequence: R → V | ||||||
Sequence conflict | 322 | in Ref. 8; AA sequence | ||||
Sequence: W → Y | ||||||
Sequence conflict | 370 | in Ref. 6; BAH12781 | ||||
Sequence: E → G | ||||||
Compositional bias | 600-614 | Basic and acidic residues | ||||
Sequence: EQSQVAEKPMEGESR | ||||||
Alternative sequence | VSP_002761 | 621-650 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002762 | 727 | in isoform 2 | |||
Sequence: A → ACPSCSRSRAPAVPA | ||||||
Alternative sequence | VSP_044764 | 727-765 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 816-817 | in Ref. 8; AA sequence | ||||
Sequence: ET → QR | ||||||
Alternative sequence | VSP_044765 | 851-866 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 905 | in Ref. 3; no nucleotide entry | ||||
Sequence: S → F | ||||||
Sequence conflict | 927 | in Ref. 3; no nucleotide entry | ||||
Sequence: S → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D38535 EMBL· GenBank· DDBJ | BAA07536.1 EMBL· GenBank· DDBJ | mRNA | ||
D38595 EMBL· GenBank· DDBJ | BAA07602.1 EMBL· GenBank· DDBJ | mRNA | ||
U43163 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U42015 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U42016 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43155 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43156 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43157 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43158 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43159 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43160 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43161 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43162 EMBL· GenBank· DDBJ | AAD05198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK298412 EMBL· GenBank· DDBJ | BAH12781.1 EMBL· GenBank· DDBJ | mRNA | ||
AC006254 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC099667 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF119856 EMBL· GenBank· DDBJ | AAF69610.1 EMBL· GenBank· DDBJ | mRNA |