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P13612

- ITA4_HUMAN

UniProt

P13612 - ITA4_HUMAN

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Protein

Integrin alpha-4

Gene

ITGA4

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 – 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

GO - Biological processi

  1. B cell differentiation Source: BHF-UCL
  2. blood coagulation Source: Reactome
  3. blood vessel remodeling Source: Ensembl
  4. cell-matrix adhesion Source: UniProtKB
  5. cell-matrix adhesion involved in ameboidal cell migration Source: UniProtKB
  6. chorio-allantoic fusion Source: Ensembl
  7. endodermal cell differentiation Source: UniProtKB
  8. extracellular matrix organization Source: Reactome
  9. face development Source: Ensembl
  10. heart development Source: Ensembl
  11. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: Ensembl
  12. heterotypic cell-cell adhesion Source: UniProtKB
  13. integrin-mediated signaling pathway Source: UniProtKB-KW
  14. leukocyte cell-cell adhesion Source: BHF-UCL
  15. leukocyte migration Source: Reactome
  16. leukocyte tethering or rolling Source: UniProtKB
  17. negative regulation of protein homodimerization activity Source: UniProtKB
  18. receptor clustering Source: UniProtKB
  19. regulation of immune response Source: Reactome
  20. substrate adhesion-dependent cell spreading Source: UniProtKB
  21. T cell migration Source: Ensembl
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 – 977943ExtracellularSequence AnalysisAdd
BLAST
Transmembranei978 – 100124HelicalSequence AnalysisAdd
BLAST
Topological domaini1002 – 103231CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cell surface Source: UniProtKB
  3. external side of plasma membrane Source: Ensembl
  4. extracellular vesicular exosome Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. integrin alpha4-beta7 complex Source: UniProtKB
  7. membrane Source: UniProtKB
  8. 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 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

BgeeiP13612.
CleanExiHS_ITGA4.
ExpressionAtlasiP13612. baseline and differential.
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
PXNP490234EBI-703044,EBI-702209

Protein-protein interaction databases

BioGridi109883. 504 interactions.
DIPiDIP-34971N.
IntActiP13612. 9 interactions.
MINTiMINT-4098849.
STRINGi9606.ENSP00000380227.

Structurei

Secondary structure

1
1032
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 454Combined sources
Beta strandi54 – 618Combined sources
Beta strandi64 – 718Combined sources
Beta strandi87 – 959Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi141 – 1455Combined sources
Turni152 – 1565Combined sources
Beta strandi165 – 1684Combined sources
Helixi174 – 1763Combined sources
Beta strandi178 – 1803Combined sources
Turni193 – 1975Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi208 – 2158Combined sources
Helixi218 – 2214Combined sources
Beta strandi223 – 2297Combined sources
Turni230 – 2334Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi267 – 2726Combined sources
Helixi275 – 2773Combined sources
Beta strandi280 – 2867Combined sources
Beta strandi288 – 29811Combined sources
Beta strandi308 – 3136Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi322 – 3276Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi338 – 3447Combined sources
Beta strandi346 – 3494Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi381 – 3833Combined sources
Beta strandi386 – 3905Combined sources
Helixi393 – 3964Combined sources
Beta strandi398 – 4036Combined sources
Beta strandi415 – 4195Combined sources
Helixi420 – 4223Combined sources
Beta strandi429 – 43810Combined sources
Beta strandi440 – 4456Combined sources
Beta strandi447 – 4526Combined sources
Helixi453 – 4553Combined sources
Beta strandi457 – 4615Combined sources
Beta strandi466 – 4749Combined sources
Beta strandi495 – 50511Combined sources
Beta strandi511 – 52212Combined sources
Beta strandi532 – 5343Combined sources
Beta strandi536 – 5383Combined sources
Beta strandi542 – 55413Combined sources
Beta strandi556 – 5649Combined sources
Beta strandi575 – 5839Combined sources
Beta strandi610 – 6178Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V4PX-ray3.15A/C34-620[»]
3V4VX-ray3.10A/C34-620[»]
4HKCX-ray2.20B1003-1032[»]
ProteinModelPortaliP13612.
SMRiP13612. Positions 34-829.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118782.
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. 1 hit.
[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

        10         20         30         40         50
MAWEARREPG PRRAAVRETV MLLLCLGVPT GRPYNVDTES ALLYQGPHNT
60 70 80 90 100
LFGYSVVLHS HGANRWLLVG APTANWLANA SVINPGAIYR CRIGKNPGQT
110 120 130 140 150
CEQLQLGSPN GEPCGKTCLE ERDNQWLGVT LSRQPGENGS IVTCGHRWKN
160 170 180 190 200
IFYIKNENKL PTGGCYGVPP DLRTELSKRI APCYQDYVKK FGENFASCQA
210 220 230 240 250
GISSFYTKDL IVMGAPGSSY WTGSLFVYNI TTNKYKAFLD KQNQVKFGSY
260 270 280 290 300
LGYSVGAGHF RSQHTTEVVG GAPQHEQIGK AYIFSIDEKE LNILHEMKGK
310 320 330 340 350
KLGSYFGASV CAVDLNADGF SDLLVGAPMQ STIREEGRVF VYINSGSGAV
360 370 380 390 400
MNAMETNLVG SDKYAARFGE SIVNLGDIDN DGFEDVAIGA PQEDDLQGAI
410 420 430 440 450
YIYNGRADGI SSTFSQRIEG LQISKSLSMF GQSISGQIDA DNNGYVDVAV
460 470 480 490 500
GAFRSDSAVL LRTRPVVIVD ASLSHPESVN RTKFDCVENG WPSVCIDLTL
510 520 530 540 550
CFSYKGKEVP GYIVLFYNMS LDVNRKAESP PRFYFSSNGT SDVITGSIQV
560 570 580 590 600
SSREANCRTH QAFMRKDVRD ILTPIQIEAA YHLGPHVISK RSTEEFPPLQ
610 620 630 640 650
PILQQKKEKD IMKKTINFAR FCAHENCSAD LQVSAKIGFL KPHENKTYLA
660 670 680 690 700
VGSMKTLMLN VSLFNAGDDA YETTLHVKLP VGLYFIKILE LEEKQINCEV
710 720 730 740 750
TDNSGVVQLD CSIGYIYVDH LSRIDISFLL DVSSLSRAEE DLSITVHATC
760 770 780 790 800
ENEEEMDNLK HSRVTVAIPL KYEVKLTVHG FVNPTSFVYG SNDENEPETC
810 820 830 840 850
MVEKMNLTFH VINTGNSMAP NVSVEIMVPN SFSPQTDKLF NILDVQTTTG
860 870 880 890 900
ECHFENYQRV CALEQQKSAM QTLKGIVRFL SKTDKRLLYC IKADPHCLNF
910 920 930 940 950
LCNFGKMESG KEASVHIQLE GRPSILEMDE TSALKFEIRA TGFPEPNPRV
960 970 980 990 1000
IELNKDENVA HVLLEGLHHQ RPKRYFTIVI ISSSLLLGLI VLLLISYVMW
1010 1020 1030
KAGFFKRQYK SILQEENRRD SWSYINSKSN DD
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. Curated
The sequence CAA34852.1 differs from that shown. Reason: Frameshift at position 13. Curated

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:
EMBLi
GenBanki
DDBJi
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. [P13612-1]
PIRiS06046.
RefSeqiNP_000876.3. NM_000885.4. [P13612-1]
UniGeneiHs.440955.

Genome annotation databases

EnsembliENST00000339307; ENSP00000340149; ENSG00000115232. [P13612-2]
ENST00000397033; ENSP00000380227; ENSG00000115232. [P13612-1]
GeneIDi3676.
KEGGihsa:3676.
UCSCiuc002unu.3. human. [P13612-1]

Polymorphism databases

DMDMi311033436.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P13612-1 ]
PIRi S06046.
RefSeqi NP_000876.3. NM_000885.4. [P13612-1 ]
UniGenei Hs.440955.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109883. 504 interactions.
DIPi DIP-34971N.
IntActi P13612. 9 interactions.
MINTi MINT-4098849.
STRINGi 9606.ENSP00000380227.

Chemistry

BindingDBi P13612.
ChEMBLi CHEMBL1907599.
DrugBanki DB00108. Natalizumab.
DB06822. Tinzaparin.
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 . [P13612-2 ]
ENST00000397033 ; ENSP00000380227 ; ENSG00000115232 . [P13612-1 ]
GeneIDi 3676.
KEGGi hsa:3676.
UCSCi uc002unu.3. human. [P13612-1 ]

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.
GeneTreei ENSGT00760000118782.
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

Bgeei P13612.
CleanExi HS_ITGA4.
ExpressionAtlasi P13612. baseline and differential.
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. 1 hit.
[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] (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: November 26, 2014
This is version 159 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

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