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Protein

Integrin alpha-X

Gene

ITGAX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi157Magnesium1
Metal bindingi159Magnesium1
Metal bindingi161Magnesium1
Metal bindingi259Magnesium1
Metal bindingi466Calcium 21
Metal bindingi468Calcium 21
Metal bindingi470Calcium 21
Metal bindingi472Calcium 2; via carbonyl oxygen1
Metal bindingi532Calcium 31
Metal bindingi534Calcium 31
Metal bindingi536Calcium 3; via carbonyl oxygen1
Metal bindingi593Calcium 11
Metal bindingi595Calcium 11
Metal bindingi597Calcium 11
Metal bindingi599Calcium 1; via carbonyl oxygen1
Metal bindingi601Calcium 11

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi466 – 4749
Calcium bindingi530 – 5389
Calcium bindingi593 – 6019

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • receptor activity Source: ProtInc

GO - Biological processi

  • animal organ morphogenesis Source: ProtInc
  • cell adhesion Source: ProtInc
  • extracellular matrix organization Source: Reactome
  • heterotypic cell-cell adhesion Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB-KW
  • leukocyte migration Source: Reactome
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000140678-MONOMER.
ReactomeiR-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiP20702.
SIGNORiP20702.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:6152. ITGAX.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 1107ExtracellularSequence analysisAdd BLAST1088
Transmembranei1108 – 1128HelicalSequence analysisAdd BLAST21
Topological domaini1129 – 1163CytoplasmicSequence analysisAdd BLAST35

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • integrin complex Source: ProtInc
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi3687.
OpenTargetsiENSG00000140678.
PharmGKBiPA29952.

Polymorphism and mutation databases

BioMutaiITGAX.
DMDMi146345441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000001629420 – 1163Integrin alpha-XAdd BLAST1144

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi61N-linked (GlcNAc...)1 Publication1
Disulfide bondi69 ↔ 761 Publication
Glycosylationi89N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi108 ↔ 1261 Publication
Disulfide bondi116 ↔ 1451 Publication
Glycosylationi392N-linked (GlcNAc...)1 Publication1
Disulfide bondi495 ↔ 5061 Publication
Disulfide bondi639 ↔ 7221 Publication
Disulfide bondi655 ↔ 7121 Publication
Glycosylationi697N-linked (GlcNAc...)1 Publication1
Glycosylationi735N-linked (GlcNAc...)1 Publication1
Disulfide bondi771 ↔ 7771 Publication
Disulfide bondi848 ↔ 8631 Publication
Glycosylationi899N-linked (GlcNAc...)2 Publications1
Glycosylationi939N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi998 ↔ 10221 Publication
Disulfide bondi1027 ↔ 10321 Publication
Glycosylationi1050N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP20702.
PaxDbiP20702.
PeptideAtlasiP20702.
PRIDEiP20702.

PTM databases

iPTMnetiP20702.
PhosphoSitePlusiP20702.

Expressioni

Tissue specificityi

Predominantly expressed in monocytes and granulocytes.

Gene expression databases

BgeeiENSG00000140678.
CleanExiHS_ITGAX.
ExpressionAtlasiP20702. baseline and differential.
GenevisibleiP20702. HS.

Organism-specific databases

HPAiCAB004458.
CAB072871.
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 interactor.
DIPiDIP-59369N.
IntActiP20702. 2 interactors.
STRINGi9606.ENSP00000268296.

Structurei

Secondary structure

11163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 26Combined sources3
Beta strandi28 – 31Combined sources4
Turni35 – 38Combined sources4
Beta strandi39 – 44Combined sources6
Turni45 – 47Combined sources3
Beta strandi48 – 59Combined sources12
Beta strandi62 – 69Combined sources8
Turni71 – 73Combined sources3
Beta strandi75 – 78Combined sources4
Beta strandi87 – 89Combined sources3
Beta strandi94 – 99Combined sources6
Turni100 – 103Combined sources4
Beta strandi104 – 116Combined sources13
Beta strandi119 – 129Combined sources11
Beta strandi131 – 133Combined sources3
Beta strandi136 – 141Combined sources6
Beta strandi150 – 157Combined sources8
Helixi164 – 178Combined sources15
Turni183 – 185Combined sources3
Beta strandi186 – 201Combined sources16
Helixi203 – 208Combined sources6
Helixi212 – 216Combined sources5
Helixi228 – 236Combined sources9
Turni237 – 240Combined sources4
Helixi242 – 244Combined sources3
Beta strandi250 – 260Combined sources11
Helixi269 – 278Combined sources10
Beta strandi282 – 289Combined sources8
Helixi290 – 293Combined sources4
Helixi298 – 304Combined sources7
Beta strandi307 – 309Combined sources3
Helixi310 – 312Combined sources3
Beta strandi313 – 318Combined sources6
Helixi319 – 325Combined sources7
Helixi326 – 334Combined sources9
Helixi336 – 338Combined sources3
Turni341 – 343Combined sources3
Beta strandi348 – 351Combined sources4
Beta strandi354 – 361Combined sources8
Beta strandi364 – 369Combined sources6
Helixi372 – 375Combined sources4
Beta strandi379 – 381Combined sources3
Beta strandi384 – 386Combined sources3
Beta strandi389 – 391Combined sources3
Helixi398 – 400Combined sources3
Beta strandi407 – 424Combined sources18
Helixi427 – 429Combined sources3
Beta strandi432 – 439Combined sources8
Beta strandi442 – 450Combined sources9
Beta strandi460 – 465Combined sources6
Beta strandi470 – 472Combined sources3
Beta strandi475 – 484Combined sources10
Beta strandi489 – 496Combined sources8
Beta strandi508 – 510Combined sources3
Beta strandi514 – 521Combined sources8
Beta strandi523 – 529Combined sources7
Beta strandi531 – 535Combined sources5
Beta strandi538 – 543Combined sources6
Helixi546 – 549Combined sources4
Beta strandi551 – 556Combined sources6
Turni560 – 562Combined sources3
Beta strandi569 – 573Combined sources5
Helixi574 – 577Combined sources4
Beta strandi586 – 592Combined sources7
Beta strandi595 – 599Combined sources5
Beta strandi601 – 606Combined sources6
Beta strandi609 – 615Combined sources7
Beta strandi618 – 632Combined sources15
Turni634 – 636Combined sources3
Beta strandi641 – 643Combined sources3
Beta strandi648 – 661Combined sources14
Turni662 – 664Combined sources3
Turni668 – 670Combined sources3
Beta strandi673 – 682Combined sources10
Beta strandi685 – 687Combined sources3
Turni693 – 695Combined sources3
Beta strandi696 – 706Combined sources11
Beta strandi708 – 719Combined sources12
Beta strandi726 – 728Combined sources3
Beta strandi730 – 740Combined sources11
Turni744 – 747Combined sources4
Beta strandi760 – 765Combined sources6
Beta strandi772 – 774Combined sources3
Beta strandi782 – 786Combined sources5
Beta strandi791 – 795Combined sources5
Beta strandi800 – 808Combined sources9
Beta strandi814 – 824Combined sources11
Beta strandi827 – 829Combined sources3
Beta strandi838 – 841Combined sources4
Beta strandi847 – 853Combined sources7
Turni854 – 857Combined sources4
Beta strandi858 – 870Combined sources13
Beta strandi875 – 884Combined sources10
Beta strandi892 – 901Combined sources10
Beta strandi908 – 910Combined sources3
Beta strandi914 – 924Combined sources11
Beta strandi926 – 930Combined sources5
Beta strandi932 – 934Combined sources3
Beta strandi937 – 941Combined sources5
Beta strandi948 – 959Combined sources12
Beta strandi961 – 963Combined sources3
Beta strandi965 – 977Combined sources13
Beta strandi980 – 989Combined sources10
Beta strandi991 – 993Combined sources3
Beta strandi999 – 1003Combined sources5
Helixi1010 – 1016Combined sources7
Beta strandi1019 – 1021Combined sources3
Turni1022 – 1024Combined sources3
Beta strandi1025 – 1037Combined sources13
Beta strandi1042 – 1053Combined sources12
Helixi1054 – 1058Combined sources5
Beta strandi1062 – 1073Combined sources12
Turni1076 – 1078Combined sources3
Beta strandi1079 – 1081Combined sources3
Helixi1086 – 1089Combined sources4
Beta strandi1090 – 1100Combined sources11
Helixi1133 – 1144Combined sources12
Beta strandi1147 – 1149Combined sources3
Turni1150 – 1154Combined sources5
Turni1160 – 1162Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5ES4X-ray3.30A/C/E/G20-1103[»]
ProteinModelPortaliP20702.
SMRiP20702.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20702.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati23 – 78FG-GAP 1PROSITE-ProRule annotationAdd BLAST56
Repeati79 – 138FG-GAP 2PROSITE-ProRule annotationAdd BLAST60
Domaini165 – 339VWFAPROSITE-ProRule annotationAdd BLAST175
Repeati340 – 391FG-GAP 3PROSITE-ProRule annotationAdd BLAST52
Repeati392 – 443FG-GAP 4PROSITE-ProRule annotationAdd BLAST52
Repeati444 – 504FG-GAP 5PROSITE-ProRule annotationAdd BLAST61
Repeati507 – 565FG-GAP 6PROSITE-ProRule annotationAdd BLAST59
Repeati570 – 630FG-GAP 7PROSITE-ProRule annotationAdd BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1131 – 1135GFFKR motif5

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.PROSITE-ProRule annotation
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPBA. Eukaryota.
ENOG410ZFBE. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000113114.
HOVERGENiHBG100530.
InParanoidiP20702.
KOiK06462.
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.
IPR032695. Integrin_dom.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
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.
SSF69179. SSF69179. 3 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti209S → T in AAA59180 (PubMed:3327687).Curated1
Sequence conflicti209S → T in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti266S → T in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti327N → T in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti330K → R in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti335A → P in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti460A → P in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti469S → T in AAA59180 (PubMed:3327687).Curated1
Sequence conflicti480A → P in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti490G → A in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti756D → L in AAA59180 (PubMed:3327687).Curated1
Sequence conflicti819I → V in AAH38237 (PubMed:15489334).Curated1
Sequence conflicti990H → L in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti1005P → G in AAA51620 (PubMed:2303426).Curated1
Sequence conflicti1161 – 1163SEK → TPHYPQDNV in AAH38237 (PubMed:15489334).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01867248W → R.Corresponds to variant rs2230424dbSNPEnsembl.1
Natural variantiVAR_049632201F → L.1 PublicationCorresponds to variant rs1574566dbSNPEnsembl.1
Natural variantiVAR_031925251A → T.2 PublicationsCorresponds to variant rs2230428dbSNPEnsembl.1
Natural variantiVAR_031926517P → R.Corresponds to variant rs2230429dbSNPEnsembl.1
Natural variantiVAR_031927547E → K.1 PublicationCorresponds to variant rs17853815dbSNPEnsembl.1
Natural variantiVAR_059363564I → V.Corresponds to variant rs189592567dbSNPEnsembl.1
Natural variantiVAR_031928971F → L.Corresponds to variant rs2230427dbSNPEnsembl.1
Natural variantiVAR_0666621012A → V.1 PublicationCorresponds to variant rs181404376dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5ES4X-ray3.30A/C/E/G20-1103[»]
ProteinModelPortaliP20702.
SMRiP20702.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109893. 1 interactor.
DIPiDIP-59369N.
IntActiP20702. 2 interactors.
STRINGi9606.ENSP00000268296.

PTM databases

iPTMnetiP20702.
PhosphoSitePlusiP20702.

Polymorphism and mutation databases

BioMutaiITGAX.
DMDMi146345441.

Proteomic databases

EPDiP20702.
PaxDbiP20702.
PeptideAtlasiP20702.
PRIDEiP20702.

Protocols and materials databases

DNASUi3687.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268296; ENSP00000268296; ENSG00000140678.
GeneIDi3687.
KEGGihsa:3687.
UCSCiuc002ebu.2. human.

Organism-specific databases

CTDi3687.
DisGeNETi3687.
GeneCardsiITGAX.
H-InvDBHIX0012988.
HGNCiHGNC:6152. ITGAX.
HPAiCAB004458.
CAB072871.
HPA004723.
MIMi151510. gene.
neXtProtiNX_P20702.
OpenTargetsiENSG00000140678.
PharmGKBiPA29952.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPBA. Eukaryota.
ENOG410ZFBE. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000113114.
HOVERGENiHBG100530.
InParanoidiP20702.
KOiK06462.
PhylomeDBiP20702.
TreeFamiTF105391.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000140678-MONOMER.
ReactomeiR-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiP20702.
SIGNORiP20702.

Miscellaneous databases

ChiTaRSiITGAX. human.
EvolutionaryTraceiP20702.
GeneWikiiCD11c.
GenomeRNAii3687.
PROiP20702.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000140678.
CleanExiHS_ITGAX.
ExpressionAtlasiP20702. baseline and differential.
GenevisibleiP20702. HS.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
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.
SSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 169 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

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.