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Q92854

- SEM4D_HUMAN

UniProt

Q92854 - SEM4D_HUMAN

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Protein

Semaphorin-4D

Gene

SEMA4D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. receptor activity Source: HGNC
  2. receptor binding Source: UniProtKB
  3. semaphorin receptor binding Source: UniProtKB
  4. 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 734713ExtracellularSequence AnalysisAdd
BLAST
Transmembranei735 – 75521HelicalSequence AnalysisAdd
BLAST
Topological domaini756 – 862107CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1012KG → DT: Abolishes PLXNB1 binding. 1 Publication
Mutagenesisi181 – 1822FL → ER: Abolishes PLXNB1 binding. 1 Publication
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

BgeeiQ92854.
CleanExiHS_SEMA4D.
ExpressionAtlasiQ92854. baseline and differential.
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 – 324Combined sources
Turni34 – 363Combined sources
Beta strandi40 – 423Combined sources
Beta strandi52 – 554Combined sources
Beta strandi59 – 657Combined sources
Beta strandi67 – 748Combined sources
Beta strandi77 – 8610Combined sources
Helixi91 – 999Combined sources
Turni104 – 1074Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi119 – 1279Combined sources
Turni129 – 1313Combined sources
Beta strandi134 – 1396Combined sources
Turni140 – 1434Combined sources
Turni153 – 1553Combined sources
Beta strandi164 – 1696Combined sources
Beta strandi172 – 1809Combined sources
Beta strandi185 – 1917Combined sources
Beta strandi193 – 1953Combined sources
Turni203 – 2053Combined sources
Beta strandi210 – 2178Combined sources
Beta strandi230 – 2389Combined sources
Beta strandi249 – 2579Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi275 – 2795Combined sources
Helixi284 – 2863Combined sources
Beta strandi292 – 2998Combined sources
Beta strandi308 – 3147Combined sources
Beta strandi316 – 3183Combined sources
Beta strandi320 – 32910Combined sources
Helixi330 – 33910Combined sources
Beta strandi342 – 3465Combined sources
Turni349 – 3513Combined sources
Beta strandi354 – 3574Combined sources
Helixi373 – 3764Combined sources
Turni377 – 3793Combined sources
Helixi383 – 3853Combined sources
Helixi388 – 3969Combined sources
Beta strandi399 – 4046Combined sources
Helixi407 – 4093Combined sources
Beta strandi412 – 4176Combined sources
Beta strandi420 – 42910Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi435 – 4439Combined sources
Beta strandi446 – 4538Combined sources
Beta strandi455 – 46511Combined sources
Beta strandi475 – 4784Combined sources
Beta strandi481 – 4844Combined sources
Beta strandi486 – 4905Combined sources
Beta strandi495 – 5006Combined sources
Helixi503 – 5053Combined sources
Helixi509 – 5146Combined sources
Beta strandi520 – 5234Combined sources
Turni524 – 5274Combined sources
Beta strandi528 – 5314Combined sources
Turni532 – 5343Combined sources
Helixi539 – 5413Combined sources
Helixi550 – 5523Combined sources
Beta strandi553 – 5553Combined sources
Beta strandi560 – 5678Combined sources
Beta strandi572 – 5743Combined sources
Beta strandi584 – 59310Combined sources
Beta strandi598 – 6025Combined sources
Turni604 – 6074Combined sources
Beta strandi609 – 6113Combined sources
Helixi616 – 6183Combined sources
Beta strandi620 – 62910Combined sources
Beta strandi631 – 64717Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ92854.

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.
GeneTreeiENSGT00760000118854.
HOGENOMiHOG000111669.
HOVERGENiHBG061627.
InParanoidiQ92854.
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

        10         20         30         40         50
MRMCTPIRGL LMALAVMFGT AMAFAPIPRI TWEHREVHLV QFHEPDIYNY
60 70 80 90 100
SALLLSEDKD TLYIGAREAV FAVNALNISE KQHEVYWKVS EDKKAKCAEK
110 120 130 140 150
GKSKQTECLN YIRVLQPLSA TSLYVCGTNA FQPACDHLNL TSFKFLGKNE
160 170 180 190 200
DGKGRCPFDP AHSYTSVMVD GELYSGTSYN FLGSEPIISR NSSHSPLRTE
210 220 230 240 250
YAIPWLNEPS FVFADVIRKS PDSPDGEDDR VYFFFTEVSV EYEFVFRVLI
260 270 280 290 300
PRIARVCKGD QGGLRTLQKK WTSFLKARLI CSRPDSGLVF NVLRDVFVLR
310 320 330 340 350
SPGLKVPVFY ALFTPQLNNV GLSAVCAYNL STAEEVFSHG KYMQSTTVEQ
360 370 380 390 400
SHTKWVRYNG PVPKPRPGAC IDSEARAANY TSSLNLPDKT LQFVKDHPLM
410 420 430 440 450
DDSVTPIDNR PRLIKKDVNY TQIVVDRTQA LDGTVYDVMF VSTDRGALHK
460 470 480 490 500
AISLEHAVHI IEETQLFQDF EPVQTLLLSS KKGNRFVYAG SNSGVVQAPL
510 520 530 540 550
AFCGKHGTCE DCVLARDPYC AWSPPTATCV ALHQTESPSR GLIQEMSGDA
560 570 580 590 600
SVCPDKSKGS YRQHFFKHGG TAELKCSQKS NLARVFWKFQ NGVLKAESPK
610 620 630 640 650
YGLMGRKNLL IFNLSEGDSG VYQCLSEERV KNKTVFQVVA KHVLEVKVVP
660 670 680 690 700
KPVVAPTLSV VQTEGSRIAT KVLVASTQGS SPPTPAVQAT SSGAITLPPK
710 720 730 740 750
PAPTGTSCEP KIVINTVPQL HSEKTMYLKS SDNRLLMSLF LFFFVLFLCL
760 770 780 790 800
FFYNCYKGYL PRQCLKFRSA LLIGKKKPKS DFCDREQSLK ETLVEPGSFS
810 820 830 840 850
QQNGEHPKPA LDTGYETEQD TITSKVPTDR EDSQRIDDLS ARDKPFDVKC
860
ELKFADSDAD GD
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.Curated
The sequence AAI37519.1 differs from that shown. Reason: Cloning artifact.Curated
The sequence BAC04938.1 differs from that shown. Reason: Cloning artifact.Curated
The sequence CAI95794.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00760000118854.
HOGENOMi HOG000111669.
HOVERGENi HBG061627.
InParanoidi Q92854.
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

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

Gene expression databases

Bgeei Q92854.
CleanExi HS_SEMA4D.
ExpressionAtlasi Q92854. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 154 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