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P13612

- ITA4_HUMAN

UniProt

P13612 - ITA4_HUMAN

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Protein
Integrin alpha-4
Gene
ITGA4, CD49D
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei591 – 5922Cleavage

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi314 – 3229 Reviewed prediction
Calcium bindingi377 – 3859 Reviewed prediction
Calcium bindingi439 – 4479 Reviewed prediction

GO - Molecular functioni

  1. cell adhesion molecule binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. B cell differentiation Source: BHF-UCL
  2. blood coagulation Source: Reactome
  3. blood vessel remodeling Source: Ensembl
  4. chorio-allantoic fusion Source: Ensembl
  5. extracellular matrix organization Source: Reactome
  6. face development Source: Ensembl
  7. heart development Source: Ensembl
  8. heterophilic cell-cell adhesion Source: Ensembl
  9. integrin-mediated signaling pathway Source: UniProtKB-KW
  10. leukocyte cell-cell adhesion Source: BHF-UCL
  11. leukocyte migration Source: Reactome
  12. negative regulation of protein homodimerization activity Source: UniProtKB
  13. regulation of immune response Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_13552. Integrin cell surface interactions.
SignaLinkiP13612.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha-4
Alternative name(s):
CD49 antigen-like family member D
Integrin alpha-IV
VLA-4 subunit alpha
CD_antigen: CD49d
Gene namesi
Name:ITGA4
Synonyms:CD49D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6140. ITGA4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 977943Extracellular Reviewed prediction
Add
BLAST
Transmembranei978 – 100124Helical; Reviewed prediction
Add
BLAST
Topological domaini1002 – 103231Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. external side of plasma membrane Source: Ensembl
  3. extracellular vesicular exosome Source: UniProtKB
  4. integrin complex Source: InterPro
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi590 – 5901K → Q: Abolishes almost completely cleavage. 1 Publication
Mutagenesisi591 – 5911R → L: Abolishes completely cleavage. 1 Publication
Mutagenesisi1021 – 10211S → A: Abolishes phosphorylation. 1 Publication
Mutagenesisi1021 – 10211S → D: Reduces PXN binding. 1 Publication
Mutagenesisi1024 – 10241Y → A: Disrupts PXN binding. 1 Publication

Organism-specific databases

PharmGKBiPA29940.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 Publication
Add
BLAST
Chaini34 – 1032999Integrin alpha-4
PRO_0000016244Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi91 ↔ 101 By similarity
Glycosylationi138 – 1381N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi144 ↔ 165 By similarity
Disulfide bondi183 ↔ 198 By similarity
Glycosylationi229 – 2291N-linked (GlcNAc...) Reviewed prediction
Glycosylationi480 – 4801N-linked (GlcNAc...)1 Publication
Disulfide bondi486 ↔ 495 By similarity
Disulfide bondi501 ↔ 557 By similarity
Glycosylationi518 – 5181N-linked (GlcNAc...)1 Publication
Glycosylationi538 – 5381N-linked (GlcNAc...)1 Publication
Disulfide bondi622 ↔ 627 By similarity
Glycosylationi626 – 6261N-linked (GlcNAc...) Reviewed prediction
Glycosylationi645 – 6451N-linked (GlcNAc...)1 Publication
Glycosylationi660 – 6601N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi698 ↔ 711 By similarity
Glycosylationi806 – 8061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi821 – 8211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi852 ↔ 890 By similarity
Disulfide bondi897 ↔ 902 By similarity
Modified residuei1021 – 10211Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation on Ser-1027 inhibits PXN binding.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP13612.
PaxDbiP13612.
PRIDEiP13612.

PTM databases

PhosphoSiteiP13612.

Expressioni

Gene expression databases

ArrayExpressiP13612.
BgeeiP13612.
CleanExiHS_ITGA4.
GenevestigatoriP13612.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The alpha subunit can sometimes be cleaved into two non-covalently associated fragments. Alpha-4 associates with either beta-1 or beta-7. Alpha-4 interacts with PXN, LPXN, and TGFB1I1/HIC5. Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan. Interacts with AMICA1; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling AMICA1 homodimerization.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB1P055563EBI-703044,EBI-703066
PXNP490233EBI-703044,EBI-702209
TGFB1I1O432942EBI-703044,EBI-1051449

Protein-protein interaction databases

BioGridi109883. 497 interactions.
DIPiDIP-34971N.
IntActiP13612. 10 interactions.
MINTiMINT-4098849.
STRINGi9606.ENSP00000380227.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 454
Beta strandi54 – 618
Beta strandi64 – 718
Beta strandi87 – 959
Beta strandi102 – 1043
Beta strandi127 – 1337
Beta strandi141 – 1455
Turni152 – 1565
Beta strandi165 – 1684
Helixi174 – 1763
Beta strandi178 – 1803
Turni193 – 1975
Beta strandi202 – 2065
Beta strandi208 – 2158
Helixi218 – 2214
Beta strandi223 – 2297
Turni230 – 2334
Beta strandi234 – 2374
Beta strandi253 – 2586
Beta strandi267 – 2726
Helixi275 – 2773
Beta strandi280 – 2867
Beta strandi288 – 29811
Beta strandi308 – 3136
Beta strandi318 – 3203
Beta strandi322 – 3276
Beta strandi332 – 3343
Beta strandi338 – 3447
Beta strandi346 – 3494
Beta strandi351 – 3533
Beta strandi381 – 3833
Beta strandi386 – 3905
Helixi393 – 3964
Beta strandi398 – 4036
Beta strandi415 – 4195
Helixi420 – 4223
Beta strandi429 – 43810
Beta strandi440 – 4456
Beta strandi447 – 4526
Helixi453 – 4553
Beta strandi457 – 4615
Beta strandi466 – 4749
Beta strandi495 – 50511
Beta strandi511 – 52212
Beta strandi532 – 5343
Beta strandi536 – 5383
Beta strandi542 – 55413
Beta strandi556 – 5649
Beta strandi575 – 5839
Beta strandi610 – 6178

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V4PX-ray3.15A/C34-620[»]
3V4VX-ray3.10A/C34-620[»]
4HKCX-ray2.20B1003-1032[»]
ProteinModelPortaliP13612.
SMRiP13612. Positions 34-829, 976-1015.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati35 – 10066FG-GAP 1
Add
BLAST
Repeati110 – 17768FG-GAP 2
Add
BLAST
Repeati185 – 23753FG-GAP 3
Add
BLAST
Repeati238 – 29356FG-GAP 4
Add
BLAST
Repeati294 – 35158FG-GAP 5
Add
BLAST
Repeati355 – 41258FG-GAP 6
Add
BLAST
Repeati416 – 47863FG-GAP 7
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi606 – 61611SG1
Add
BLAST
Motifi1003 – 10075GFFKR motif

Domaini

The SG1 motif is involved in binding to chondroitin sulfate glycosaminoglycan and cell adhesion.1 Publication

Sequence similaritiesi

Contains 7 FG-GAP repeats.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG324320.
HOGENOMiHOG000088626.
HOVERGENiHBG004538.
InParanoidiP13612.
KOiK06483.
OMAiNRRDSWS.
OrthoDBiEOG7MSMN4.
PhylomeDBiP13612.
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.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13612-1 [UniParc]FASTAAdd to Basket

« Hide

MAWEARREPG PRRAAVRETV MLLLCLGVPT GRPYNVDTES ALLYQGPHNT     50
LFGYSVVLHS HGANRWLLVG APTANWLANA SVINPGAIYR CRIGKNPGQT 100
CEQLQLGSPN GEPCGKTCLE ERDNQWLGVT LSRQPGENGS IVTCGHRWKN 150
IFYIKNENKL PTGGCYGVPP DLRTELSKRI APCYQDYVKK FGENFASCQA 200
GISSFYTKDL IVMGAPGSSY WTGSLFVYNI TTNKYKAFLD KQNQVKFGSY 250
LGYSVGAGHF RSQHTTEVVG GAPQHEQIGK AYIFSIDEKE LNILHEMKGK 300
KLGSYFGASV CAVDLNADGF SDLLVGAPMQ STIREEGRVF VYINSGSGAV 350
MNAMETNLVG SDKYAARFGE SIVNLGDIDN DGFEDVAIGA PQEDDLQGAI 400
YIYNGRADGI SSTFSQRIEG LQISKSLSMF GQSISGQIDA DNNGYVDVAV 450
GAFRSDSAVL LRTRPVVIVD ASLSHPESVN RTKFDCVENG WPSVCIDLTL 500
CFSYKGKEVP GYIVLFYNMS LDVNRKAESP PRFYFSSNGT SDVITGSIQV 550
SSREANCRTH QAFMRKDVRD ILTPIQIEAA YHLGPHVISK RSTEEFPPLQ 600
PILQQKKEKD IMKKTINFAR FCAHENCSAD LQVSAKIGFL KPHENKTYLA 650
VGSMKTLMLN VSLFNAGDDA YETTLHVKLP VGLYFIKILE LEEKQINCEV 700
TDNSGVVQLD CSIGYIYVDH LSRIDISFLL DVSSLSRAEE DLSITVHATC 750
ENEEEMDNLK HSRVTVAIPL KYEVKLTVHG FVNPTSFVYG SNDENEPETC 800
MVEKMNLTFH VINTGNSMAP NVSVEIMVPN SFSPQTDKLF NILDVQTTTG 850
ECHFENYQRV CALEQQKSAM QTLKGIVRFL SKTDKRLLYC IKADPHCLNF 900
LCNFGKMESG KEASVHIQLE GRPSILEMDE TSALKFEIRA TGFPEPNPRV 950
IELNKDENVA HVLLEGLHHQ RPKRYFTIVI ISSSLLLGLI VLLLISYVMW 1000
KAGFFKRQYK SILQEENRRD SWSYINSKSN DD 1032
Length:1,032
Mass (Da):114,900
Last modified:November 2, 2010 - v3
Checksum:i73EC1204DE78CD35
GO

Sequence cautioni

The sequence AAB59613.1 differs from that shown. Reason: Frameshift at position 13.
The sequence CAA34852.1 differs from that shown. Reason: Frameshift at position 13.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti634 – 6341S → T.
Corresponds to variant rs35322532 [ dbSNP | Ensembl ].
VAR_047423
Natural varianti824 – 8241V → A.
Corresponds to variant rs1143675 [ dbSNP | Ensembl ].
VAR_047424
Natural varianti878 – 8781R → Q.2 Publications
Corresponds to variant rs1143676 [ dbSNP | Ensembl ].
VAR_003978

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16983 mRNA. Translation: CAA34852.1. Frameshift.
L12002 mRNA. Translation: AAB59613.1. Frameshift.
AC020595 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX10985.1.
CH471058 Genomic DNA. Translation: EAX10987.1.
CCDSiCCDS42788.1.
PIRiS06046.
RefSeqiNP_000876.3. NM_000885.4.
UniGeneiHs.440955.

Genome annotation databases

EnsembliENST00000397033; ENSP00000380227; ENSG00000115232.
GeneIDi3676.
KEGGihsa:3676.
UCSCiuc002unu.3. human.

Polymorphism databases

DMDMi311033436.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16983 mRNA. Translation: CAA34852.1 . Frameshift.
L12002 mRNA. Translation: AAB59613.1 . Frameshift.
AC020595 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX10985.1 .
CH471058 Genomic DNA. Translation: EAX10987.1 .
CCDSi CCDS42788.1.
PIRi S06046.
RefSeqi NP_000876.3. NM_000885.4.
UniGenei Hs.440955.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3V4P X-ray 3.15 A/C 34-620 [» ]
3V4V X-ray 3.10 A/C 34-620 [» ]
4HKC X-ray 2.20 B 1003-1032 [» ]
ProteinModelPortali P13612.
SMRi P13612. Positions 34-829, 976-1015.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109883. 497 interactions.
DIPi DIP-34971N.
IntActi P13612. 10 interactions.
MINTi MINT-4098849.
STRINGi 9606.ENSP00000380227.

Chemistry

BindingDBi P13612.
ChEMBLi CHEMBL1907599.
DrugBanki DB00108. Natalizumab.
GuidetoPHARMACOLOGYi 2443.

PTM databases

PhosphoSitei P13612.

Polymorphism databases

DMDMi 311033436.

Proteomic databases

MaxQBi P13612.
PaxDbi P13612.
PRIDEi P13612.

Protocols and materials databases

DNASUi 3676.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000397033 ; ENSP00000380227 ; ENSG00000115232 .
GeneIDi 3676.
KEGGi hsa:3676.
UCSCi uc002unu.3. human.

Organism-specific databases

CTDi 3676.
GeneCardsi GC02P182285.
HGNCi HGNC:6140. ITGA4.
MIMi 192975. gene.
neXtProti NX_P13612.
PharmGKBi PA29940.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324320.
HOGENOMi HOG000088626.
HOVERGENi HBG004538.
InParanoidi P13612.
KOi K06483.
OMAi NRRDSWS.
OrthoDBi EOG7MSMN4.
PhylomeDBi P13612.
TreeFami TF105391.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_13552. Integrin cell surface interactions.
SignaLinki P13612.

Miscellaneous databases

ChiTaRSi ITGA4. human.
GeneWikii CD49d.
GenomeRNAii 3676.
NextBioi 14391.
PROi P13612.
SOURCEi Search...

Gene expression databases

ArrayExpressi P13612.
Bgeei P13612.
CleanExi HS_ITGA4.
Genevestigatori P13612.

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.
[Graphical view ]
Pfami PF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view ]
PRINTSi PR01185. INTEGRINA.
SMARTi SM00191. Int_alpha. 5 hits.
[Graphical view ]
PROSITEi PS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of the alpha 4 subunit of VLA-4: homology to other integrins and a possible cell-cell adhesion function."
    Takada Y., Elices M.J., Crouse C., Hemler M.E.
    EMBO J. 8:1361-1368(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A single mRNA encodes the alpha 150 and alpha 80/70 forms of the alpha subunit of VLA4."
    Rubio M., Nueda A., Vara A., Corbi-Lopez A.L.
    Eur. J. Immunol. 22:1099-1102(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Identification of two variants of the human integrin alpha 4 subunit."
    Szabo M.C., McIntyre B.W.
    Mol. Immunol. 32:1453-1454(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-878.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-878.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-87.
  7. "The very late antigen family of heterodimers is part of a superfamily of molecules involved in adhesion and embryogenesis."
    Takada Y., Strominger J.L., Hemler M.E.
    Proc. Natl. Acad. Sci. U.S.A. 84:3239-3243(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-47.
  8. "Functional and structural analysis of VLA-4 integrin alpha 4 subunit cleavage."
    Teixido J., Parker C.M., Kassner P.D., Hemler M.E.
    J. Biol. Chem. 267:1786-1791(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 592-601, PROTEOLYTIC PROCESSING, MUTAGENESIS OF LYS-590 AND ARG-591.
  9. "A role of chondroitin sulfate glycosaminoglycan binding site in alpha4beta1 integrin-mediated melanoma cell adhesion."
    Iida J., Meijne A.M.L., Oegema T.R. Jr., Yednock T.A., Kovach N.L., Furcht L.T., McCarthy J.B.
    J. Biol. Chem. 273:5955-5962(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, INTERACTION WITH CSPG4.
  10. "Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses."
    Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., Ginsberg M.H.
    Nature 402:676-681(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PXN; LPXN AND TGFB1I1, MUTAGENESIS OF TYR-1024.
  11. "Phosphorylation of the integrin alpha 4 cytoplasmic domain regulates paxillin binding."
    Han J., Liu S., Rose D.M., Schlaepfer D.D., McDonald H., Ginsberg M.H.
    J. Biol. Chem. 276:40903-40909(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1021, MUTAGENESIS OF SER-1021.
  12. "JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by alpha4beta1 integrin activation."
    Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S.
    J. Cell Biol. 183:1159-1173(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LEUKOCYTE TO ENDOTHELIAL CELLS ADHESION, INTERACTION WITH AMICA1.
  13. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-480; ASN-518; ASN-538 AND ASN-645.
    Tissue: Leukemic T-cell.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1021, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiITA4_HUMAN
AccessioniPrimary (citable) accession number: P13612
Secondary accession number(s): D3DPG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 2, 2010
Last modified: September 3, 2014
This is version 156 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 2
    Human chromosome 2: 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

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