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P20702

- ITAX_HUMAN

UniProt

P20702 - ITAX_HUMAN

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Protein

Integrin alpha-X

Gene

ITGAX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. receptor activity Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cell adhesion Source: ProtInc
  3. extracellular matrix organization Source: Reactome
  4. heterotypic cell-cell adhesion Source: UniProtKB
  5. integrin-mediated signaling pathway Source: UniProtKB-KW
  6. leukocyte migration Source: Reactome
  7. organ morphogenesis Source: ProtInc
Complete GO annotation...

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. integrin complex Source: ProtInc
  3. membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

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

BgeeiP20702.
CleanExiHS_ITGAX.
ExpressionAtlasiP20702. baseline and differential.
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. 2 interactions.
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.
GeneTreeiENSGT00760000118782.
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

        10         20         30         40         50
MTRTRAALLL FTALATSLGF NLDTEELTAF RVDSAGFGDS VVQYANSWVV
60 70 80 90 100
VGAPQKITAA NQTGGLYQCG YSTGACEPIG LQVPPEAVNM SLGLSLASTT
110 120 130 140 150
SPSQLLACGP TVHHECGRNM YLTGLCFLLG PTQLTQRLPV SRQECPRQEQ
160 170 180 190 200
DIVFLIDGSG SISSRNFATM MNFVRAVISQ FQRPSTQFSL MQFSNKFQTH
210 220 230 240 250
FTFEEFRRSS NPLSLLASVH QLQGFTYTAT AIQNVVHRLF HASYGARRDA
260 270 280 290 300
AKILIVITDG KKEGDSLDYK DVIPMADAAG IIRYAIGVGL AFQNRNSWKE
310 320 330 340 350
LNDIASKPSQ EHIFKVEDFD ALKDIQNQLK EKIFAIEGTE TTSSSSFELE
360 370 380 390 400
MAQEGFSAVF TPDGPVLGAV GSFTWSGGAF LYPPNMSPTF INMSQENVDM
410 420 430 440 450
RDSYLGYSTE LALWKGVQSL VLGAPRYQHT GKAVIFTQVS RQWRMKAEVT
460 470 480 490 500
GTQIGSYFGA SLCSVDVDSD GSTDLVLIGA PHYYEQTRGG QVSVCPLPRG
510 520 530 540 550
WRRWWCDAVL YGEQGHPWGR FGAALTVLGD VNGDKLTDVV IGAPGEEENR
560 570 580 590 600
GAVYLFHGVL GPSISPSHSQ RIAGSQLSSR LQYFGQALSG GQDLTQDGLV
610 620 630 640 650
DLAVGARGQV LLLRTRPVLW VGVSMQFIPA EIPRSAFECR EQVVSEQTLV
660 670 680 690 700
QSNICLYIDK RSKNLLGSRD LQSSVTLDLA LDPGRLSPRA TFQETKNRSL
710 720 730 740 750
SRVRVLGLKA HCENFNLLLP SCVEDSVTPI TLRLNFTLVG KPLLAFRNLR
760 770 780 790 800
PMLAADAQRY FTASLPFEKN CGADHICQDN LGISFSFPGL KSLLVGSNLE
810 820 830 840 850
LNAEVMVWND GEDSYGTTIT FSHPAGLSYR YVAEGQKQGQ LRSLHLTCDS
860 870 880 890 900
APVGSQGTWS TSCRINHLIF RGGAQITFLA TFDVSPKAVL GDRLLLTANV
910 920 930 940 950
SSENNTPRTS KTTFQLELPV KYAVYTVVSS HEQFTKYLNF SESEEKESHV
960 970 980 990 1000
AMHRYQVNNL GQRDLPVSIN FWVPVELNQE AVWMDVEVSH PQNPSLRCSS
1010 1020 1030 1040 1050
EKIAPPASDF LAHIQKNPVL DCSIAGCLRF RCDVPSFSVQ EELDFTLKGN
1060 1070 1080 1090 1100
LSFGWVRQIL QKKVSVVSVA EITFDTSVYS QLPGQEAFMR AQTTTVLEKY
1110 1120 1130 1140 1150
KVHNPTPLIV GSSIGGLLLL ALITAVLYKV GFFKRQYKEM MEEANGQIAP
1160
ENGTQTPSPP SEK
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. 2 interactions.
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.
GeneTreei ENSGT00760000118782.
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

Bgeei P20702.
CleanExi HS_ITGAX.
ExpressionAtlasi P20702. baseline and differential.
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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 154 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