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P20702

- ITAX_HUMAN

UniProt

P20702 - ITAX_HUMAN

Protein

Integrin alpha-X

Gene

ITGAX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (01 May 2007)
      Previous versions | rss
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    Functioni

    Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi157 – 1571Magnesium
    Metal bindingi159 – 1591Magnesium
    Metal bindingi161 – 1611Magnesium
    Metal bindingi259 – 2591Magnesium
    Metal bindingi466 – 4661Calcium 2
    Metal bindingi468 – 4681Calcium 2
    Metal bindingi470 – 4701Calcium 2
    Metal bindingi472 – 4721Calcium 2; via carbonyl oxygen
    Metal bindingi532 – 5321Calcium 3
    Metal bindingi534 – 5341Calcium 3
    Metal bindingi536 – 5361Calcium 3; via carbonyl oxygen
    Metal bindingi593 – 5931Calcium 1
    Metal bindingi595 – 5951Calcium 1
    Metal bindingi597 – 5971Calcium 1
    Metal bindingi599 – 5991Calcium 1; via carbonyl oxygen
    Metal bindingi601 – 6011Calcium 1

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi466 – 4749
    Calcium bindingi530 – 5389
    Calcium bindingi593 – 6019

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: BHF-UCL
    3. receptor activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell adhesion Source: ProtInc
    3. defense response to virus Source: Ensembl
    4. extracellular matrix organization Source: Reactome
    5. integrin-mediated signaling pathway Source: UniProtKB-KW
    6. leukocyte migration Source: Reactome
    7. organ morphogenesis Source: ProtInc

    Keywords - Molecular functioni

    Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
    REACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.
    SignaLinkiP20702.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin alpha-X
    Alternative name(s):
    CD11 antigen-like family member C
    Leu M5
    Leukocyte adhesion glycoprotein p150,95 alpha chain
    Leukocyte adhesion receptor p150,95
    CD_antigen: CD11c
    Gene namesi
    Name:ITGAX
    Synonyms:CD11C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:6152. ITGAX.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. external side of plasma membrane Source: Ensembl
    3. integrin complex Source: ProtInc
    4. membrane Source: UniProtKB
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29952.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 11631144Integrin alpha-XPRO_0000016294Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi61 – 611N-linked (GlcNAc...)1 Publication
    Disulfide bondi69 ↔ 761 Publication
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi108 ↔ 1261 Publication
    Disulfide bondi116 ↔ 1451 Publication
    Glycosylationi392 – 3921N-linked (GlcNAc...)1 Publication
    Disulfide bondi495 ↔ 5061 Publication
    Disulfide bondi639 ↔ 7221 Publication
    Disulfide bondi655 ↔ 7121 Publication
    Glycosylationi697 – 6971N-linked (GlcNAc...)1 Publication
    Glycosylationi735 – 7351N-linked (GlcNAc...)1 Publication
    Disulfide bondi771 ↔ 7771 Publication
    Disulfide bondi848 ↔ 8631 Publication
    Glycosylationi899 – 8991N-linked (GlcNAc...)2 Publications
    Glycosylationi939 – 9391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi998 ↔ 10221 Publication
    Disulfide bondi1027 ↔ 10321 Publication
    Glycosylationi1050 – 10501N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP20702.
    PRIDEiP20702.

    PTM databases

    PhosphoSiteiP20702.

    Expressioni

    Tissue specificityi

    Predominantly expressed in monocytes and granulocytes.

    Gene expression databases

    ArrayExpressiP20702.
    BgeeiP20702.
    CleanExiHS_ITGAX.
    GenevestigatoriP20702.

    Organism-specific databases

    HPAiCAB004458.
    HPA004723.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. Alpha-X associates with beta-2.1 Publication

    Protein-protein interaction databases

    BioGridi109893. 1 interaction.
    DIPiDIP-59369N.
    IntActiP20702. 1 interaction.
    STRINGi9606.ENSP00000268296.

    Structurei

    Secondary structure

    1
    1163
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 263
    Beta strandi28 – 314
    Turni35 – 384
    Beta strandi39 – 446
    Turni45 – 473
    Beta strandi48 – 5912
    Beta strandi62 – 698
    Turni71 – 733
    Beta strandi75 – 784
    Beta strandi85 – 873
    Beta strandi94 – 996
    Turni100 – 1034
    Beta strandi104 – 11613
    Beta strandi119 – 12911
    Beta strandi131 – 1333
    Beta strandi136 – 1416
    Beta strandi150 – 1578
    Helixi164 – 17815
    Turni183 – 1853
    Beta strandi186 – 20116
    Helixi203 – 2086
    Helixi212 – 2165
    Helixi228 – 2369
    Turni237 – 2404
    Helixi242 – 2443
    Beta strandi250 – 26011
    Helixi269 – 27810
    Beta strandi282 – 2898
    Helixi290 – 2934
    Helixi298 – 3047
    Beta strandi307 – 3093
    Helixi310 – 3123
    Beta strandi313 – 3186
    Helixi319 – 3257
    Helixi326 – 3349
    Helixi336 – 3383
    Turni341 – 3433
    Beta strandi348 – 3514
    Beta strandi354 – 3618
    Beta strandi364 – 3696
    Helixi372 – 3754
    Beta strandi379 – 3813
    Beta strandi384 – 3863
    Beta strandi389 – 3913
    Helixi398 – 4003
    Beta strandi407 – 42418
    Helixi427 – 4293
    Beta strandi432 – 4398
    Beta strandi442 – 4509
    Beta strandi460 – 4656
    Beta strandi470 – 4723
    Beta strandi475 – 48410
    Beta strandi489 – 4968
    Beta strandi508 – 5103
    Beta strandi514 – 5218
    Beta strandi523 – 5297
    Beta strandi531 – 5355
    Beta strandi538 – 5436
    Helixi546 – 5494
    Beta strandi551 – 5566
    Turni560 – 5623
    Beta strandi569 – 5735
    Helixi574 – 5774
    Beta strandi586 – 5927
    Beta strandi595 – 5995
    Beta strandi601 – 6066
    Beta strandi609 – 6157
    Beta strandi618 – 63215
    Turni634 – 6363
    Beta strandi641 – 6433
    Beta strandi648 – 66114
    Turni662 – 6643
    Turni668 – 6703
    Beta strandi673 – 68210
    Beta strandi685 – 6873
    Turni693 – 6953
    Beta strandi696 – 70611
    Beta strandi708 – 71912
    Beta strandi730 – 74011
    Turni744 – 7474
    Beta strandi760 – 7656
    Beta strandi772 – 7743
    Beta strandi782 – 7865
    Beta strandi791 – 7955
    Beta strandi800 – 8089
    Beta strandi814 – 82411
    Beta strandi827 – 8293
    Beta strandi838 – 8414
    Beta strandi847 – 8537
    Turni854 – 8574
    Beta strandi858 – 87013
    Beta strandi875 – 88410
    Beta strandi892 – 90110
    Beta strandi908 – 9103
    Beta strandi914 – 92411
    Beta strandi926 – 9305
    Beta strandi932 – 9343
    Beta strandi937 – 9415
    Beta strandi948 – 95912
    Beta strandi961 – 9633
    Beta strandi965 – 97713
    Beta strandi980 – 98910
    Beta strandi991 – 9933
    Beta strandi999 – 10035
    Helixi1010 – 10167
    Beta strandi1019 – 10213
    Turni1022 – 10243
    Beta strandi1025 – 103713
    Beta strandi1042 – 105312
    Helixi1054 – 10585
    Beta strandi1062 – 107312
    Turni1076 – 10783
    Beta strandi1079 – 10813
    Helixi1086 – 10894
    Beta strandi1090 – 110011
    Helixi1133 – 114412
    Beta strandi1147 – 11493
    Turni1150 – 11545
    Turni1160 – 11623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N3YX-ray1.65A147-338[»]
    2LUVNMR-A1129-1163[»]
    3K6SX-ray3.50A/C/E/G20-1103[»]
    3K71X-ray3.95A/C/E/G20-1103[»]
    3K72X-ray3.70A/C20-1103[»]
    4NEHX-ray2.75A20-1101[»]
    4NENX-ray2.90A20-1101[»]
    ProteinModelPortaliP20702.
    SMRiP20702. Positions 20-1101, 1129-1163.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20702.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 11071088ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1129 – 116335CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1108 – 112821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati23 – 7856FG-GAP 1Add
    BLAST
    Repeati79 – 13860FG-GAP 2Add
    BLAST
    Domaini165 – 339175VWFAPROSITE-ProRule annotationAdd
    BLAST
    Repeati340 – 39152FG-GAP 3Add
    BLAST
    Repeati392 – 44554FG-GAP 4Add
    BLAST
    Repeati446 – 50459FG-GAP 5Add
    BLAST
    Repeati507 – 56559FG-GAP 6Add
    BLAST
    Repeati570 – 63061FG-GAP 7Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1131 – 11355GFFKR motif

    Domaini

    The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.

    Sequence similaritiesi

    Belongs to the integrin alpha chain family.Curated
    Contains 7 FG-GAP repeats.Curated
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG301393.
    HOGENOMiHOG000113114.
    HOVERGENiHBG100530.
    InParanoidiP20702.
    KOiK06462.
    OrthoDBiEOG7353W1.
    PhylomeDBiP20702.
    TreeFamiTF105391.

    Family and domain databases

    InterProiIPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01839. FG-GAP. 1 hit.
    PF00357. Integrin_alpha. 1 hit.
    PF08441. Integrin_alpha2. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    PRINTSiPR01185. INTEGRINA.
    SMARTiSM00191. Int_alpha. 5 hits.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    PROSITEiPS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P20702-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRTRAALLL FTALATSLGF NLDTEELTAF RVDSAGFGDS VVQYANSWVV     50
    VGAPQKITAA NQTGGLYQCG YSTGACEPIG LQVPPEAVNM SLGLSLASTT 100
    SPSQLLACGP TVHHECGRNM YLTGLCFLLG PTQLTQRLPV SRQECPRQEQ 150
    DIVFLIDGSG SISSRNFATM MNFVRAVISQ FQRPSTQFSL MQFSNKFQTH 200
    FTFEEFRRSS NPLSLLASVH QLQGFTYTAT AIQNVVHRLF HASYGARRDA 250
    AKILIVITDG KKEGDSLDYK DVIPMADAAG IIRYAIGVGL AFQNRNSWKE 300
    LNDIASKPSQ EHIFKVEDFD ALKDIQNQLK EKIFAIEGTE TTSSSSFELE 350
    MAQEGFSAVF TPDGPVLGAV GSFTWSGGAF LYPPNMSPTF INMSQENVDM 400
    RDSYLGYSTE LALWKGVQSL VLGAPRYQHT GKAVIFTQVS RQWRMKAEVT 450
    GTQIGSYFGA SLCSVDVDSD GSTDLVLIGA PHYYEQTRGG QVSVCPLPRG 500
    WRRWWCDAVL YGEQGHPWGR FGAALTVLGD VNGDKLTDVV IGAPGEEENR 550
    GAVYLFHGVL GPSISPSHSQ RIAGSQLSSR LQYFGQALSG GQDLTQDGLV 600
    DLAVGARGQV LLLRTRPVLW VGVSMQFIPA EIPRSAFECR EQVVSEQTLV 650
    QSNICLYIDK RSKNLLGSRD LQSSVTLDLA LDPGRLSPRA TFQETKNRSL 700
    SRVRVLGLKA HCENFNLLLP SCVEDSVTPI TLRLNFTLVG KPLLAFRNLR 750
    PMLAADAQRY FTASLPFEKN CGADHICQDN LGISFSFPGL KSLLVGSNLE 800
    LNAEVMVWND GEDSYGTTIT FSHPAGLSYR YVAEGQKQGQ LRSLHLTCDS 850
    APVGSQGTWS TSCRINHLIF RGGAQITFLA TFDVSPKAVL GDRLLLTANV 900
    SSENNTPRTS KTTFQLELPV KYAVYTVVSS HEQFTKYLNF SESEEKESHV 950
    AMHRYQVNNL GQRDLPVSIN FWVPVELNQE AVWMDVEVSH PQNPSLRCSS 1000
    EKIAPPASDF LAHIQKNPVL DCSIAGCLRF RCDVPSFSVQ EELDFTLKGN 1050
    LSFGWVRQIL QKKVSVVSVA EITFDTSVYS QLPGQEAFMR AQTTTVLEKY 1100
    KVHNPTPLIV GSSIGGLLLL ALITAVLYKV GFFKRQYKEM MEEANGQIAP 1150
    ENGTQTPSPP SEK 1163
    Length:1,163
    Mass (Da):127,829
    Last modified:May 1, 2007 - v3
    Checksum:i8947288C43E76BE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti209 – 2091S → T in AAA59180. (PubMed:3327687)Curated
    Sequence conflicti209 – 2091S → T in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti266 – 2661S → T in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti327 – 3271N → T in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti330 – 3301K → R in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti335 – 3351A → P in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti460 – 4601A → P in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti469 – 4691S → T in AAA59180. (PubMed:3327687)Curated
    Sequence conflicti480 – 4801A → P in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti490 – 4901G → A in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti756 – 7561D → L in AAA59180. (PubMed:3327687)Curated
    Sequence conflicti819 – 8191I → V in AAH38237. (PubMed:15489334)Curated
    Sequence conflicti990 – 9901H → L in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti1005 – 10051P → G in AAA51620. (PubMed:2303426)Curated
    Sequence conflicti1161 – 11633SEK → TPHYPQDNV in AAH38237. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481W → R.
    Corresponds to variant rs2230424 [ dbSNP | Ensembl ].
    VAR_018672
    Natural varianti201 – 2011F → L.1 Publication
    Corresponds to variant rs1574566 [ dbSNP | Ensembl ].
    VAR_049632
    Natural varianti251 – 2511A → T.2 Publications
    Corresponds to variant rs2230428 [ dbSNP | Ensembl ].
    VAR_031925
    Natural varianti517 – 5171P → R.
    Corresponds to variant rs2230429 [ dbSNP | Ensembl ].
    VAR_031926
    Natural varianti547 – 5471E → K.1 Publication
    Corresponds to variant rs17853815 [ dbSNP | Ensembl ].
    VAR_031927
    Natural varianti564 – 5641I → V.
    Corresponds to variant rs2230430 [ dbSNP | Ensembl ].
    VAR_059363
    Natural varianti971 – 9711F → L.
    Corresponds to variant rs2230427 [ dbSNP | Ensembl ].
    VAR_031928
    Natural varianti1012 – 10121A → V.1 Publication
    Corresponds to variant rs181404376 [ dbSNP | Ensembl ].
    VAR_066662

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81695 mRNA. Translation: AAA59180.1.
    M29165 mRNA. No translation available.
    M29487
    , M29482, M29483, M29484, M29485, M29486 Genomic DNA. Translation: AAA51620.1. Sequence problems.
    BC038237 mRNA. Translation: AAH38237.1.
    CCDSiCCDS10711.1.
    PIRiA36584. RWHU1C.
    RefSeqiNP_000878.2. NM_000887.4.
    NP_001273304.1. NM_001286375.1.
    UniGeneiHs.248472.

    Genome annotation databases

    EnsembliENST00000268296; ENSP00000268296; ENSG00000140678.
    GeneIDi3687.
    KEGGihsa:3687.
    UCSCiuc002ebu.1. human.

    Polymorphism databases

    DMDMi146345441.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81695 mRNA. Translation: AAA59180.1 .
    M29165 mRNA. No translation available.
    M29487
    , M29482 , M29483 , M29484 , M29485 , M29486 Genomic DNA. Translation: AAA51620.1 . Sequence problems.
    BC038237 mRNA. Translation: AAH38237.1 .
    CCDSi CCDS10711.1.
    PIRi A36584. RWHU1C.
    RefSeqi NP_000878.2. NM_000887.4.
    NP_001273304.1. NM_001286375.1.
    UniGenei Hs.248472.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N3Y X-ray 1.65 A 147-338 [» ]
    2LUV NMR - A 1129-1163 [» ]
    3K6S X-ray 3.50 A/C/E/G 20-1103 [» ]
    3K71 X-ray 3.95 A/C/E/G 20-1103 [» ]
    3K72 X-ray 3.70 A/C 20-1103 [» ]
    4NEH X-ray 2.75 A 20-1101 [» ]
    4NEN X-ray 2.90 A 20-1101 [» ]
    ProteinModelPortali P20702.
    SMRi P20702. Positions 20-1101, 1129-1163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109893. 1 interaction.
    DIPi DIP-59369N.
    IntActi P20702. 1 interaction.
    STRINGi 9606.ENSP00000268296.

    PTM databases

    PhosphoSitei P20702.

    Polymorphism databases

    DMDMi 146345441.

    Proteomic databases

    PaxDbi P20702.
    PRIDEi P20702.

    Protocols and materials databases

    DNASUi 3687.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268296 ; ENSP00000268296 ; ENSG00000140678 .
    GeneIDi 3687.
    KEGGi hsa:3687.
    UCSCi uc002ebu.1. human.

    Organism-specific databases

    CTDi 3687.
    GeneCardsi GC16P031366.
    H-InvDB HIX0012988.
    HGNCi HGNC:6152. ITGAX.
    HPAi CAB004458.
    HPA004723.
    MIMi 151510. gene.
    neXtProti NX_P20702.
    PharmGKBi PA29952.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301393.
    HOGENOMi HOG000113114.
    HOVERGENi HBG100530.
    InParanoidi P20702.
    KOi K06462.
    OrthoDBi EOG7353W1.
    PhylomeDBi P20702.
    TreeFami TF105391.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.
    REACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.
    SignaLinki P20702.

    Miscellaneous databases

    ChiTaRSi ITGAX. human.
    EvolutionaryTracei P20702.
    GeneWikii CD11c.
    GenomeRNAii 3687.
    NextBioi 14429.
    PROi P20702.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20702.
    Bgeei P20702.
    CleanExi HS_ITGAX.
    Genevestigatori P20702.

    Family and domain databases

    InterProi IPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01839. FG-GAP. 1 hit.
    PF00357. Integrin_alpha. 1 hit.
    PF08441. Integrin_alpha2. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    PRINTSi PR01185. INTEGRINA.
    SMARTi SM00191. Int_alpha. 5 hits.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    PROSITEi PS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
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    Publicationsi

    1. "cDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein, p150,95."
      Corbi A.L., Miller L.J., O'Connor K., Larson R.S., Springer T.A.
      EMBO J. 6:4023-4028(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-251.
    2. "Genomic structure of an integrin alpha subunit, the leukocyte p150,95 molecule."
      Corbi A.L., Garcia-Aguilar J., Springer T.A.
      J. Biol. Chem. 265:2782-2788(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-201 AND THR-251.
    3. Erratum
      Corbi A.L., Garcia-Aguilar J., Springer T.A.
      J. Biol. Chem. 265:12750-12751(1990)
    4. "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], VARIANT LYS-547.
      Tissue: Blood.
    5. "Purification and alpha subunit N-terminal sequences of human Mac-1 and p150,95 leukocyte adhesion proteins."
      Miller L.J., Wiebe M., Springer T.A.
      J. Immunol. 138:2381-2383(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-43.
    6. "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-899.
      Tissue: Liver.
    7. "Structure of an integrin with an alphaI domain, complement receptor type 4."
      Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A.
      EMBO J. 29:666-679(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 20-1103 IN COMPLEX WITH ITGB2, GLYCOSYLATION AT ASN-61; ASN-392; ASN-697; ASN-735 AND ASN-899, DISULFIDE BONDS, METAL-BINDING SITES, SUBUNIT.
    8. "Structure and binding interface of the cytosolic tails of alphaXbeta2 integrin."
      Chua G.L., Tang X.Y., Patra A.T., Tan S.M., Bhattacharjya S.
      PLoS ONE 7:E41924-E41924(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1129-1163.
    9. Cited for: VARIANT VAL-1012.

    Entry informationi

    Entry nameiITAX_HUMAN
    AccessioniPrimary (citable) accession number: P20702
    Secondary accession number(s): Q8IVA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 153 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3