Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13612

- ITA4_HUMAN

UniProt

P13612 - ITA4_HUMAN

Protein

Integrin alpha-4

Gene

ITGA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (02 Nov 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 3229Sequence Analysis
    Calcium bindingi377 – 3859Sequence Analysis
    Calcium bindingi439 – 4479Sequence Analysis

    GO - Molecular functioni

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

    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

    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

    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. membrane Source: UniProtKB
    6. plasma membrane Source: UniProtKB

    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 PublicationAdd
    BLAST
    Chaini34 – 1032999Integrin alpha-4PRO_0000016244Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Phosphorylation on Ser-1027 inhibits PXN binding.2 Publications

    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

    1
    1032
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 977943ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1002 – 103231CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei978 – 100124HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

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

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi606 – 61611SG1Add
    BLAST
    Motifi1003 – 10075GFFKR motif

    Domaini

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

    Sequence similaritiesi

    Belongs to the integrin alpha chain family.Curated
    Contains 7 FG-GAP repeats.Curated

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P13612-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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
    Isoform 2 (identifier: P13612-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         186-195: DYVKKFGENF → GSISKYRART
         196-1032: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:195
    Mass (Da):21,536
    Checksum:iD8F8CBE554E5DE6B
    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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei186 – 19510DYVKKFGENF → GSISKYRART in isoform 2. 1 PublicationVSP_056612
    Alternative sequencei196 – 1032837Missing in isoform 2. 1 PublicationVSP_056613Add
    BLAST

    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.
    BC055419 mRNA. Translation: AAH55419.1.
    CCDSiCCDS42788.1.
    PIRiS06046.
    RefSeqiNP_000876.3. NM_000885.4.
    UniGeneiHs.440955.

    Genome annotation databases

    EnsembliENST00000339307; ENSP00000340149; ENSG00000115232.
    ENST00000397033; ENSP00000380227; ENSG00000115232.
    GeneIDi3676.
    KEGGihsa:3676.
    UCSCiuc002unu.3. human.

    Polymorphism databases

    DMDMi311033436.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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 .
    BC055419 mRNA. Translation: AAH55419.1 .
    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...
    MobiDBi 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 ENST00000339307 ; ENSP00000340149 ; ENSG00000115232 .
    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

    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] (ISOFORM 1).
    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] (ISOFORM 1).
    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] (ISOFORM 1), 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. "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] (ISOFORM 2).
      Tissue: Prostate.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-87 (ISOFORM 1).
    8. "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.
    9. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. "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.
    15. "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, Q7Z4L6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 157 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