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Protein

Inter-alpha-trypsin inhibitor heavy chain H2

Gene

ITIH2

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.

GO - Molecular functioni

  • endopeptidase inhibitor activity Source: ProtInc
  • serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  • hyaluronan metabolic process Source: InterPro
  • negative regulation of endopeptidase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Inter-alpha-trypsin inhibitor heavy chain H2
Short name:
ITI heavy chain H2
Short name:
ITI-HC2
Short name:
Inter-alpha-inhibitor heavy chain 2
Alternative name(s):
Inter-alpha-trypsin inhibitor complex component II
Serum-derived hyaluronan-associated protein
Short name:
SHAP
Gene namesi
Name:ITIH2
Synonyms:IGHEP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:6167. ITIH2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29965.

Polymorphism and mutation databases

BioMutaiITIH2.
DMDMi229462889.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 5436PRO_0000016517Add
BLAST
Chaini55 – 702648Inter-alpha-trypsin inhibitor heavy chain H2PRO_0000016518Add
BLAST
Propeptidei703 – 946244PRO_0000016519Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphoserine; by FAM20CCombined sources1 Publication
Glycosylationi96 – 961N-linked (GlcNAc...)1 Publication
Glycosylationi118 – 1181N-linked (GlcNAc...) (complex)5 PublicationsCAR_000140
Disulfide bondi261 ↔ 2641 Publication
Modified residuei282 – 28214-carboxyglutamate1 Publication
Modified residuei283 – 28314-carboxyglutamate1 Publication
Glycosylationi445 – 4451N-linked (GlcNAc...)1 Publication
Modified residuei466 – 4661Phosphoserine; by FAM20C1 Publication
Disulfide bondi650 ↔ 6511 Publication
Glycosylationi666 – 6661O-linked (GalNAc...); partial2 PublicationsCAR_000214
Glycosylationi673 – 6731O-linked (GalNAc...)2 PublicationsCAR_000215
Glycosylationi675 – 6751O-linked (GalNAc...)2 PublicationsCAR_000216
Glycosylationi691 – 6911O-linked (GalNAc...)3 PublicationsCAR_000217
Modified residuei702 – 7021Aspartate 1-(chondroitin 4-sulfate)-ester
Modified residuei886 – 8861Phosphoserine; by FAM20C1 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.By similarity
N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.7 Publications
Phosphorylated by FAM20C in the extracellular medium.1 Publication

Keywords - PTMi

Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

MaxQBiP19823.
PaxDbiP19823.
PRIDEiP19823.

PTM databases

iPTMnetiP19823.
PhosphoSiteiP19823.
UniCarbKBiP19823.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP19823.
CleanExiHS_ITIH2.
ExpressionAtlasiP19823. baseline and differential.
GenevisibleiP19823. HS.

Organism-specific databases

HPAiHPA059150.

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

BioGridi109904. 15 interactions.
IntActiP19823. 1 interaction.
MINTiMINT-1415907.
STRINGi9606.ENSP00000351190.

Structurei

3D structure databases

ProteinModelPortaliP19823.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 185130VITPROSITE-ProRule annotationAdd
BLAST
Domaini308 – 468161VWFAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni665 – 67915O-glycosylated at three sitesAdd
BLAST

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

eggNOGiENOG410IEJB. Eukaryota.
COG2304. LUCA.
GeneTreeiENSGT00550000074468.
HOVERGENiHBG057734.
InParanoidiP19823.
KOiK19015.
OMAiVPQLYSF.
OrthoDBiEOG7CRTP5.
PhylomeDBiP19823.
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]

Sequencei

Sequence statusi: Complete.

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

P19823-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRLTCFFIC FFLSEVSGFE IPINGLSEFV DYEDLVELAP GKFQLVAENR
60 70 80 90 100
RYQRSLPGES EEMMEEVDQV TLYSYKVQST ITSRMATTMI QSKVVNNSPQ
110 120 130 140 150
PQNVVFDVQI PKGAFISNFS MTVDGKTFRS SIKEKTVGRA LYAQARAKGK
160 170 180 190 200
TAGLVRSSAL DMENFRTEVN VLPGAKVQFE LHYQEVKWRK LGSYEHRIYL
210 220 230 240 250
QPGRLAKHLE VDVWVIEPQG LRFLHVPDTF EGHFDGVPVI SKGQQKAHVS
260 270 280 290 300
FKPTVAQQRI CPNCRETAVD GELVVLYDVK REEKAGELEV FNGYFVHFFA
310 320 330 340 350
PDNLDPIPKN ILFVIDVSGS MWGVKMKQTV EAMKTILDDL RAEDHFSVID
360 370 380 390 400
FNQNIRTWRN DLISATKTQV ADAKRYIEKI QPSGGTNINE ALLRAIFILN
410 420 430 440 450
EANNLGLLDP NSVSLIILVS DGDPTVGELK LSKIQKNVKE NIQDNISLFS
460 470 480 490 500
LGMGFDVDYD FLKRLSNENH GIAQRIYGNQ DTSSQLKKFY NQVSTPLLRN
510 520 530 540 550
VQFNYPHTSV TDVTQNNFHN YFGGSEIVVA GKFDPAKLDQ IESVITATSA
560 570 580 590 600
NTQLVLETLA QMDDLQDFLS KDKHADPDFT RKLWAYLTIN QLLAERSLAP
610 620 630 640 650
TAAAKRRITR SILQMSLDHH IVTPLTSLVI ENEAGDERML ADAPPQDPSC
660 670 680 690 700
CSGALYYGSK VVPDSTPSWA NPSPTPVISM LAQGSQVLES TPPPHVMRVE
710 720 730 740 750
NDPHFIIYLP KSQKNICFNI DSEPGKILNL VSDPESGIVV NGQLVGAKKP
760 770 780 790 800
NNGKLSTYFG KLGFYFQSED IKIEISTETI TLSHGSSTFS LSWSDTAQVT
810 820 830 840 850
NQRVQISVKK EKVVTITLDK EMSFSVLLHR VWKKHPVNVD FLGIYIPPTN
860 870 880 890 900
KFSPKAHGLI GQFMQEPKIH IFNERPGKDP EKPEASMEVK GQKLIITRGL
910 920 930 940
QKDYRTDLVF GTDVTCWFVH NSGKGFIDGH YKDYFVPQLY SFLKRP
Length:946
Mass (Da):106,463
Last modified:May 5, 2009 - v2
Checksum:iBA626B146DDC2A5F
GO

Sequence cautioni

The sequence CAA30160.1 differs from that shown. Reason: Frameshift at positions 363 and 373. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti374 – 3741K → L AA sequence (PubMed:2476436).Curated
Sequence conflicti705 – 7051F → S in AAA60558 (PubMed:2446322).Curated
Sequence conflicti705 – 7051F → S in AAA59195 (PubMed:2462430).Curated
Sequence conflicti729 – 7291N → D in AAA60558 (PubMed:2446322).Curated
Sequence conflicti729 – 7291N → D in AAA59195 (PubMed:2462430).Curated
Sequence conflicti731 – 7311V → A in AAA60558 (PubMed:2446322).Curated
Sequence conflicti731 – 7311V → A in AAA59195 (PubMed:2462430).Curated

Mass spectrometryi

Molecular mass is 76508 Da from positions 55 - 702. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti263 – 2631N → S.1 Publication
Corresponds to variant rs7075296 [ dbSNP | Ensembl ].
VAR_055248
Natural varianti569 – 5691L → V.
Corresponds to variant rs7084817 [ dbSNP | Ensembl ].
VAR_055249
Natural varianti674 – 6741P → A.1 Publication
Corresponds to variant rs3740217 [ dbSNP | Ensembl ].
VAR_055250

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07173 mRNA. Translation: CAA30160.1. Frameshift.
AL158044 Genomic DNA. Translation: CAI12957.1.
M18193 mRNA. Translation: AAA60558.1.
M33033 mRNA. Translation: AAA59195.1.
CCDSiCCDS31141.1.
PIRiS00346. IYHU2.
RefSeqiNP_002207.2. NM_002216.2.
UniGeneiHs.75285.

Genome annotation databases

EnsembliENST00000358415; ENSP00000351190; ENSG00000151655.
GeneIDi3698.
KEGGihsa:3698.
UCSCiuc001ijs.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07173 mRNA. Translation: CAA30160.1. Frameshift.
AL158044 Genomic DNA. Translation: CAI12957.1.
M18193 mRNA. Translation: AAA60558.1.
M33033 mRNA. Translation: AAA59195.1.
CCDSiCCDS31141.1.
PIRiS00346. IYHU2.
RefSeqiNP_002207.2. NM_002216.2.
UniGeneiHs.75285.

3D structure databases

ProteinModelPortaliP19823.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109904. 15 interactions.
IntActiP19823. 1 interaction.
MINTiMINT-1415907.
STRINGi9606.ENSP00000351190.

PTM databases

iPTMnetiP19823.
PhosphoSiteiP19823.
UniCarbKBiP19823.

Polymorphism and mutation databases

BioMutaiITIH2.
DMDMi229462889.

Proteomic databases

MaxQBiP19823.
PaxDbiP19823.
PRIDEiP19823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358415; ENSP00000351190; ENSG00000151655.
GeneIDi3698.
KEGGihsa:3698.
UCSCiuc001ijs.4. human.

Organism-specific databases

CTDi3698.
GeneCardsiITIH2.
H-InvDBHIX0035419.
HGNCiHGNC:6167. ITIH2.
HPAiHPA059150.
MIMi146640. gene.
neXtProtiNX_P19823.
PharmGKBiPA29965.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEJB. Eukaryota.
COG2304. LUCA.
GeneTreeiENSGT00550000074468.
HOVERGENiHBG057734.
InParanoidiP19823.
KOiK19015.
OMAiVPQLYSF.
OrthoDBiEOG7CRTP5.
PhylomeDBiP19823.
TreeFamiTF328982.

Miscellaneous databases

GeneWikiiITIH2.
GenomeRNAii3698.
PROiP19823.
SOURCEiSearch...

Gene expression databases

BgeeiP19823.
CleanExiHS_ITIH2.
ExpressionAtlasiP19823. baseline and differential.
GenevisibleiP19823. HS.

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. "Complementary DNA and derived amino acid sequence of the precursor of one of the three protein components of the inter-alpha-trypsin inhibitor complex."
    Gebhard W., Schreitmueller T., Hochstrasser K., Wachter E.
    FEBS Lett. 229:63-67(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GAMMA-CARBOXYGLUTAMATION AT GLU-282 AND GLU-283, VARIANT SER-263.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 384-865.
  4. "Human inter-alpha-trypsin inhibitor. Isolation and characterization of heavy (H) chain cDNA clones coding for a 383 amino-acid sequence of the H chain."
    Salier J.-P., Diarra-Mehrpour M., Sesboue R., Bourguignon J., Martin J.-P.
    Biol. Chem. Hoppe-Seyler 369:15-18(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 384-766, VARIANT ALA-674.
  5. "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: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  6. "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 55-74; 116-127; 224-246; 295-307 AND 365-385.
  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 55-64.
    Tissue: Plasma.
  8. "Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-alpha-inhibitor-related proteinase inhibitor heavy chain 2/bikunin."
    Enghild J.J., Salvesen G., Thoegersen I.B., Valnickova Z., Pizzo S.V., Hefta S.A.
    J. Biol. Chem. 268:8711-8716(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 55-64 AND 681-702, CROSS-LINK STRUCTURE, GLYCOSYLATION AT THR-691.
  9. "TSG-6, an arthritis-associated hyaluronan binding protein, forms a stable complex with the serum protein inter-alpha-inhibitor."
    Wisniewski H.-G., Burgess W.H., Oppenheim J.D., Vilcek J.
    Biochemistry 33:7423-7429(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 55-64, INTERACTION WITH TNFAIP6.
  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 67-101, HYALURONAN BINDING.
    Tissue: Serum.
  11. "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 699-702, COVALENT LINKAGE WITH CHONDROITIN SULFATE.
    Tissue: Plasma.
  12. "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-118; THR-666; SER-673; THR-675 AND THR-691, MASS SPECTROMETRY.
  13. "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 ASN-118; THR-666; SER-673; THR-675 AND THR-691, DISULFIDE BONDS.
  14. "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-118.
  15. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96; ASN-118 AND ASN-445.
    Tissue: Plasma.
  16. "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-118.
    Tissue: Liver.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  19. "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-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. Cited for: PHOSPHORYLATION AT SER-60; SER-466 AND SER-886.

Entry informationi

Entry nameiITIH2_HUMAN
AccessioniPrimary (citable) accession number: P19823
Secondary accession number(s): Q14659, Q15484, Q5T986
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 5, 2009
Last modified: June 8, 2016
This is version 157 of the entry and version 2 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 10
    Human chromosome 10: 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

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 one 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.