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Q92854

- SEM4D_HUMAN

UniProt

Q92854 - SEM4D_HUMAN

Protein

Semaphorin-4D

Gene

SEMA4D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Cell surface receptor for PLXN1B and PLXNB2 that plays an important role in cell-cell signaling. Promotes reorganization of the actin cytoskeleton and plays a role in axonal growth cone guidance in the developing central nervous system. Regulates dendrite and axon branching and morphogenesis. Promotes the migration of cerebellar granule cells and of endothelial cells. Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro). Promotes signaling via SRC and PTK2B/PYK2, which then mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Interaction with PLXNB1 mediates activation of RHOA.4 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor activity Source: HGNC
    3. receptor binding Source: UniProtKB
    4. semaphorin receptor binding Source: UniProtKB
    5. transmembrane signaling receptor activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell adhesion Source: ProtInc
    3. immune response Source: ProtInc
    4. leukocyte aggregation Source: UniProtKB
    5. negative regulation of alkaline phosphatase activity Source: BHF-UCL
    6. negative regulation of apoptotic process Source: ProtInc
    7. negative regulation of cell adhesion Source: UniProtKB
    8. negative regulation of osteoblast differentiation Source: BHF-UCL
    9. negative regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    10. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    11. ossification involved in bone maturation Source: BHF-UCL
    12. positive regulation of cell migration Source: UniProtKB
    13. positive regulation of collateral sprouting Source: UniProtKB
    14. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    15. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    16. positive regulation of protein phosphorylation Source: UniProtKB
    17. positive regulation of Rho GTPase activity Source: UniProtKB
    18. regulation of cell projection organization Source: UniProtKB
    19. regulation of cell shape Source: UniProtKB
    20. regulation of dendrite morphogenesis Source: UniProtKB
    21. semaphorin-plexin signaling pathway Source: UniProtKB
    22. semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis Source: BHF-UCL

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_19200. Other semaphorin interactions.
    REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Semaphorin-4D
    Alternative name(s):
    A8
    BB18
    GR3
    CD_antigen: CD100
    Gene namesi
    Name:SEMA4D
    Synonyms:C9orf164, CD100, SEMAJ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:10732. SEMA4D.

    Subcellular locationi

    Cell membrane 2 Publications; Single-pass type I membrane protein 2 Publications

    GO - Cellular componenti

    1. extracellular space Source: BHF-UCL
    2. integral component of plasma membrane Source: UniProtKB
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1012KG → DT: Abolishes PLXNB1 binding.
    Mutagenesisi181 – 1822FL → ER: Abolishes PLXNB1 binding.
    Mutagenesisi244 – 2441F → N: Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with S-246. 1 Publication
    Mutagenesisi246 – 2461F → S: Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with N-244. 1 Publication
    Mutagenesisi395 – 3951K → E: Strongly reduces PLXNB1 binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA35654.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 862841Semaphorin-4DPRO_0000032327Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi49 – 491N-linked (GlcNAc...)2 Publications
    Glycosylationi74 – 741N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi77 – 771N-linked (GlcNAc...)2 Publications
    Disulfide bondi97 ↔ 108
    Disulfide bondi126 ↔ 135
    Glycosylationi139 – 1391N-linked (GlcNAc...)1 Publication
    Glycosylationi191 – 1911N-linked (GlcNAc...)1 Publication
    Disulfide bondi257 ↔ 370
    Disulfide bondi281 ↔ 326
    Glycosylationi329 – 3291N-linked (GlcNAc...)1 Publication
    Glycosylationi379 – 3791N-linked (GlcNAc...)1 Publication
    Glycosylationi419 – 4191N-linked (GlcNAc...)3 Publications
    Disulfide bondi503 ↔ 520
    Disulfide bondi509 ↔ 553
    Disulfide bondi512 ↔ 529
    Disulfide bondi576 ↔ 624
    Glycosylationi613 – 6131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi632 – 6321N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ92854.
    PaxDbiQ92854.
    PeptideAtlasiQ92854.
    PRIDEiQ92854.

    PTM databases

    PhosphoSiteiQ92854.

    Expressioni

    Tissue specificityi

    Strongly expressed in skeletal muscle, peripheral blood lymphocytes, spleen, and thymus and also expressed at lower levels in testes, brain, kidney, small intestine, prostate, heart, placenta, lung and pancreas, but not in colon and liver.1 Publication

    Gene expression databases

    ArrayExpressiQ92854.
    BgeeiQ92854.
    CleanExiHS_SEMA4D.
    GenevestigatoriQ92854.

    Organism-specific databases

    HPAiHPA015662.
    HPA023277.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with PLXNB2 By similarity. Binds PLXNB1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi115766. 5 interactions.
    DIPiDIP-59221N.
    IntActiQ92854. 2 interactions.
    STRINGi9606.ENSP00000343418.

    Structurei

    Secondary structure

    1
    862
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 324
    Turni34 – 363
    Beta strandi40 – 423
    Beta strandi52 – 554
    Beta strandi59 – 657
    Beta strandi67 – 748
    Beta strandi77 – 8610
    Helixi91 – 999
    Turni104 – 1074
    Beta strandi111 – 1177
    Beta strandi119 – 1279
    Turni129 – 1313
    Beta strandi134 – 1396
    Turni140 – 1434
    Turni153 – 1553
    Beta strandi164 – 1696
    Beta strandi172 – 1809
    Beta strandi185 – 1917
    Beta strandi193 – 1953
    Turni203 – 2053
    Beta strandi210 – 2178
    Beta strandi230 – 2389
    Beta strandi249 – 2579
    Beta strandi264 – 2674
    Beta strandi275 – 2795
    Helixi284 – 2863
    Beta strandi292 – 2998
    Beta strandi308 – 3147
    Beta strandi316 – 3183
    Beta strandi320 – 32910
    Helixi330 – 33910
    Beta strandi342 – 3465
    Turni349 – 3513
    Beta strandi354 – 3574
    Helixi373 – 3764
    Turni377 – 3793
    Helixi383 – 3853
    Helixi388 – 3969
    Beta strandi399 – 4046
    Helixi407 – 4093
    Beta strandi412 – 4176
    Beta strandi420 – 42910
    Beta strandi431 – 4333
    Beta strandi435 – 4439
    Beta strandi446 – 4538
    Beta strandi455 – 46511
    Beta strandi475 – 4784
    Beta strandi481 – 4844
    Beta strandi486 – 4905
    Beta strandi495 – 5006
    Helixi503 – 5053
    Helixi509 – 5146
    Beta strandi520 – 5234
    Turni524 – 5274
    Beta strandi528 – 5314
    Turni532 – 5343
    Helixi539 – 5413
    Helixi550 – 5523
    Beta strandi553 – 5553
    Beta strandi560 – 5678
    Beta strandi572 – 5743
    Beta strandi584 – 59310
    Beta strandi598 – 6025
    Turni604 – 6074
    Beta strandi609 – 6113
    Helixi616 – 6183
    Beta strandi620 – 62910
    Beta strandi631 – 64717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OLZX-ray2.00A/B22-677[»]
    3OL2X-ray2.99A22-677[»]
    ProteinModelPortaliQ92854.
    SMRiQ92854. Positions 24-648.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92854.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 734713ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini756 – 862107CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei735 – 75521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 500479SemaPROSITE-ProRule annotationAdd
    BLAST
    Domaini502 – 55150PSIAdd
    BLAST
    Domaini554 – 63683Ig-like C2-typeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the semaphorin family.Curated
    Contains 1 PSI domain.Curated
    Contains 1 Sema domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG326211.
    HOGENOMiHOG000111669.
    HOVERGENiHBG061627.
    InParanoidiQ8N8B0.
    KOiK06521.
    OMAiAWESCNQ.
    OrthoDBiEOG71K62C.
    PhylomeDBiQ92854.
    TreeFamiTF316102.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    IPR016201. Plexin-like_fold.
    IPR002165. Plexin_repeat.
    IPR001627. Semap_dom.
    IPR027231. Semaphorin.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PANTHERiPTHR11036. PTHR11036. 1 hit.
    PfamiPF00047. ig. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    SM00423. PSI. 1 hit.
    SM00630. Sema. 1 hit.
    [Graphical view]
    SUPFAMiSSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS51004. SEMA. 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: Q92854-1) [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

    MRMCTPIRGL LMALAVMFGT AMAFAPIPRI TWEHREVHLV QFHEPDIYNY    50
    SALLLSEDKD TLYIGAREAV FAVNALNISE KQHEVYWKVS EDKKAKCAEK 100
    GKSKQTECLN YIRVLQPLSA TSLYVCGTNA FQPACDHLNL TSFKFLGKNE 150
    DGKGRCPFDP AHSYTSVMVD GELYSGTSYN FLGSEPIISR NSSHSPLRTE 200
    YAIPWLNEPS FVFADVIRKS PDSPDGEDDR VYFFFTEVSV EYEFVFRVLI 250
    PRIARVCKGD QGGLRTLQKK WTSFLKARLI CSRPDSGLVF NVLRDVFVLR 300
    SPGLKVPVFY ALFTPQLNNV GLSAVCAYNL STAEEVFSHG KYMQSTTVEQ 350
    SHTKWVRYNG PVPKPRPGAC IDSEARAANY TSSLNLPDKT LQFVKDHPLM 400
    DDSVTPIDNR PRLIKKDVNY TQIVVDRTQA LDGTVYDVMF VSTDRGALHK 450
    AISLEHAVHI IEETQLFQDF EPVQTLLLSS KKGNRFVYAG SNSGVVQAPL 500
    AFCGKHGTCE DCVLARDPYC AWSPPTATCV ALHQTESPSR GLIQEMSGDA 550
    SVCPDKSKGS YRQHFFKHGG TAELKCSQKS NLARVFWKFQ NGVLKAESPK 600
    YGLMGRKNLL IFNLSEGDSG VYQCLSEERV KNKTVFQVVA KHVLEVKVVP 650
    KPVVAPTLSV VQTEGSRIAT KVLVASTQGS SPPTPAVQAT SSGAITLPPK 700
    PAPTGTSCEP KIVINTVPQL HSEKTMYLKS SDNRLLMSLF LFFFVLFLCL 750
    FFYNCYKGYL PRQCLKFRSA LLIGKKKPKS DFCDREQSLK ETLVEPGSFS 800
    QQNGEHPKPA LDTGYETEQD TITSKVPTDR EDSQRIDDLS ARDKPFDVKC 850
    ELKFADSDAD GD 862
    Length:862
    Mass (Da):96,150
    Last modified:February 1, 1997 - v1
    Checksum:i7B18EFEA98789371
    GO
    Isoform 2 (identifier: Q92854-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         555-738: DKSKGSYRQH...KSSDNRLLMS → ASSPKPLPPP...AWESCSKDTL
         739-862: Missing.

    Show »
    Length:738
    Mass (Da):82,164
    Checksum:i93ED5D62D6A17ED1
    GO

    Sequence cautioni

    The sequence AAI37516.1 differs from that shown. Reason: Cloning artifact.
    The sequence AAI37519.1 differs from that shown. Reason: Cloning artifact.
    The sequence BAC04938.1 differs from that shown. Reason: Cloning artifact.
    The sequence CAI95794.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti592 – 5921G → D in AAH54500. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721A → T.
    Corresponds to variant rs13284404 [ dbSNP | Ensembl ].
    VAR_030293
    Natural varianti327 – 3271A → T.
    Corresponds to variant rs11526468 [ dbSNP | Ensembl ].
    VAR_057175

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei555 – 738184DKSKG…RLLMS → ASSPKPLPPPGSSSLSCLGH VGDRRLSSPWTPWPASGAGP DSSSRVSLLPPFLSDQAQHV HALGNFYLFCQATGPADIRF VWEKNGRALETCVPVQTHAL PDGRAHALSWLQDAIRESAE YRCSVLSSAGNKTSKVQVAV MRPEVTHQERWTRELSAWRA VAGEHDRMMQSWRKAWESCS KDTL in isoform 2. CuratedVSP_039483Add
    BLAST
    Alternative sequencei739 – 862124Missing in isoform 2. CuratedVSP_039484Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U60800 mRNA. Translation: AAC50810.1.
    AL590233 Genomic DNA. Translation: CAI17379.2.
    AL929575 Genomic DNA. Translation: CAI43250.2.
    AL929575 Genomic DNA. Translation: CAI95794.1. Sequence problems.
    BC054500 mRNA. Translation: AAH54500.1.
    BC137515 mRNA. Translation: AAI37516.1. Sequence problems.
    BC137518 mRNA. Translation: AAI37519.1. Sequence problems.
    AK097056 mRNA. Translation: BAC04938.1. Sequence problems.
    CCDSiCCDS47991.1. [Q92854-2]
    CCDS6685.1. [Q92854-1]
    RefSeqiNP_001135759.1. NM_001142287.1. [Q92854-2]
    NP_006369.3. NM_006378.3. [Q92854-1]
    XP_005251711.1. XM_005251654.1. [Q92854-1]
    UniGeneiHs.494406.

    Genome annotation databases

    EnsembliENST00000339861; ENSP00000344923; ENSG00000187764. [Q92854-2]
    ENST00000356444; ENSP00000348822; ENSG00000187764. [Q92854-1]
    ENST00000420101; ENSP00000399948; ENSG00000187764.
    ENST00000420987; ENSP00000391733; ENSG00000187764. [Q92854-2]
    ENST00000422704; ENSP00000388768; ENSG00000187764. [Q92854-1]
    ENST00000438547; ENSP00000405102; ENSG00000187764. [Q92854-1]
    ENST00000450295; ENSP00000416523; ENSG00000187764. [Q92854-1]
    ENST00000455551; ENSP00000411981; ENSG00000187764. [Q92854-2]
    GeneIDi10507.
    KEGGihsa:10507.
    UCSCiuc004aqo.1. human. [Q92854-1]
    uc011ltm.1. human. [Q92854-2]

    Polymorphism databases

    DMDMi8134701.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U60800 mRNA. Translation: AAC50810.1 .
    AL590233 Genomic DNA. Translation: CAI17379.2 .
    AL929575 Genomic DNA. Translation: CAI43250.2 .
    AL929575 Genomic DNA. Translation: CAI95794.1 . Sequence problems.
    BC054500 mRNA. Translation: AAH54500.1 .
    BC137515 mRNA. Translation: AAI37516.1 . Sequence problems.
    BC137518 mRNA. Translation: AAI37519.1 . Sequence problems.
    AK097056 mRNA. Translation: BAC04938.1 . Sequence problems.
    CCDSi CCDS47991.1. [Q92854-2 ]
    CCDS6685.1. [Q92854-1 ]
    RefSeqi NP_001135759.1. NM_001142287.1. [Q92854-2 ]
    NP_006369.3. NM_006378.3. [Q92854-1 ]
    XP_005251711.1. XM_005251654.1. [Q92854-1 ]
    UniGenei Hs.494406.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OLZ X-ray 2.00 A/B 22-677 [» ]
    3OL2 X-ray 2.99 A 22-677 [» ]
    ProteinModelPortali Q92854.
    SMRi Q92854. Positions 24-648.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115766. 5 interactions.
    DIPi DIP-59221N.
    IntActi Q92854. 2 interactions.
    STRINGi 9606.ENSP00000343418.

    PTM databases

    PhosphoSitei Q92854.

    Polymorphism databases

    DMDMi 8134701.

    Proteomic databases

    MaxQBi Q92854.
    PaxDbi Q92854.
    PeptideAtlasi Q92854.
    PRIDEi Q92854.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339861 ; ENSP00000344923 ; ENSG00000187764 . [Q92854-2 ]
    ENST00000356444 ; ENSP00000348822 ; ENSG00000187764 . [Q92854-1 ]
    ENST00000420101 ; ENSP00000399948 ; ENSG00000187764 .
    ENST00000420987 ; ENSP00000391733 ; ENSG00000187764 . [Q92854-2 ]
    ENST00000422704 ; ENSP00000388768 ; ENSG00000187764 . [Q92854-1 ]
    ENST00000438547 ; ENSP00000405102 ; ENSG00000187764 . [Q92854-1 ]
    ENST00000450295 ; ENSP00000416523 ; ENSG00000187764 . [Q92854-1 ]
    ENST00000455551 ; ENSP00000411981 ; ENSG00000187764 . [Q92854-2 ]
    GeneIDi 10507.
    KEGGi hsa:10507.
    UCSCi uc004aqo.1. human. [Q92854-1 ]
    uc011ltm.1. human. [Q92854-2 ]

    Organism-specific databases

    CTDi 10507.
    GeneCardsi GC09M091975.
    HGNCi HGNC:10732. SEMA4D.
    HPAi HPA015662.
    HPA023277.
    MIMi 601866. gene.
    neXtProti NX_Q92854.
    PharmGKBi PA35654.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326211.
    HOGENOMi HOG000111669.
    HOVERGENi HBG061627.
    InParanoidi Q8N8B0.
    KOi K06521.
    OMAi AWESCNQ.
    OrthoDBi EOG71K62C.
    PhylomeDBi Q92854.
    TreeFami TF316102.

    Enzyme and pathway databases

    Reactomei REACT_19200. Other semaphorin interactions.
    REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.

    Miscellaneous databases

    EvolutionaryTracei Q92854.
    GeneWikii SEMA4D.
    GenomeRNAii 10507.
    NextBioi 39858.
    PROi Q92854.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92854.
    Bgeei Q92854.
    CleanExi HS_SEMA4D.
    Genevestigatori Q92854.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    IPR016201. Plexin-like_fold.
    IPR002165. Plexin_repeat.
    IPR001627. Semap_dom.
    IPR027231. Semaphorin.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    PANTHERi PTHR11036. PTHR11036. 1 hit.
    Pfami PF00047. ig. 1 hit.
    PF01437. PSI. 1 hit.
    PF01403. Sema. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    SM00423. PSI. 1 hit.
    SM00630. Sema. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101912. SSF101912. 1 hit.
    SSF103575. SSF103575. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS51004. SEMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human CD100, a novel leukocyte semaphorin that promotes B-cell aggregation and differentiation."
      Hall K.T., Boumsell L., Schultze J.L., Boussiotis V.A., Dorfman D.M., Cardoso A.A., Bensussan A., Nadler L.M., Freeman G.J.
      Proc. Natl. Acad. Sci. U.S.A. 93:11780-11785(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: T-cell.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 1), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain and Eye.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Small intestine.
    5. "Plexins are a large family of receptors for transmembrane, secreted and GPI-anchored semaphorins in vertebrates."
      Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L., Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M., Tessier-Lavigne M., Comoglio P.M.
      Cell 99:71-80(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLXNB1.
    6. "Semaphorin 4D/plexin-B1 induces endothelial cell migration through the activation of PYK2, Src, and the phosphatidylinositol 3-kinase-Akt pathway."
      Basile J.R., Afkhami T., Gutkind J.S.
      Mol. Cell. Biol. 25:6889-6898(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-419.
      Tissue: Platelet.
    8. "The semaphorin 4D-plexin-B signalling complex regulates dendritic and axonal complexity in developing neurons via diverse pathways."
      Vodrazka P., Korostylev A., Hirschberg A., Swiercz J.M., Worzfeld T., Deng S., Fazzari P., Tamagnone L., Offermanns S., Kuner R.
      Eur. J. Neurosci. 30:1193-1208(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "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-49; ASN-74; ASN-77; ASN-379 AND ASN-419.
      Tissue: Leukemic T-cell.
    10. "The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D."
      Love C.A., Harlos K., Mavaddat N., Davis S.J., Stuart D.I., Jones E.Y., Esnouf R.M.
      Nat. Struct. Biol. 10:843-848(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-684, DISULFIDE BONDS.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 22-677 IN COMPLEX WITH PLXNB1, SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 100-LYS-GLY-101; 181-PHE-LEU-182; PHE-244; PHE-246 AND LYS-395, GLYCOSYLATION AT ASN-49; ASN-77; ASN-139; ASN-191; ASN-329 AND ASN-419, DISULFIDE BONDS.

    Entry informationi

    Entry nameiSEM4D_HUMAN
    AccessioniPrimary (citable) accession number: Q92854
    Secondary accession number(s): B2RPM6, Q7Z5S4, Q8N8B0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 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, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 9
      Human chromosome 9: 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