Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q92854 (SEM4D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Semaphorin-4D
Alternative name(s):
A8
BB18
GR3
CD_antigen=CD100
Gene names
Name:SEMA4D
Synonyms:C9orf164, CD100, SEMAJ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.8 Ref.11

Subunit structure

Homodimer. Interacts with PLXNB2 By similarity. Binds PLXNB1. Ref.5 Ref.11

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.1 Ref.11.

Tissue specificity

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. Ref.1

Sequence similarities

Belongs to the semaphorin family.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 PSI domain.

Contains 1 Sema domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement Ref.1. Source: ProtInc

immune response

Traceable author statement Ref.1. Source: ProtInc

leukocyte aggregation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

negative regulation of alkaline phosphatase activity

Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL

negative regulation of apoptotic process

Traceable author statement Ref.1. Source: ProtInc

negative regulation of osteoblast differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL

ossification involved in bone maturation

Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL

positive regulation of Rho GTPase activity

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of collateral sprouting

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of cell projection organization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of dendrite morphogenesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

semaphorin-plexin signaling pathway

Inferred from mutant phenotype Ref.8Ref.11. Source: UniProtKB

semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentextracellular space

Inferred from sequence or structural similarity. Source: BHF-UCL

integral component of plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionreceptor activity

Inferred from direct assay PubMed 15613544. Source: HGNC

receptor binding

Inferred from direct assay Ref.11. Source: UniProtKB

semaphorin receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

transmembrane signaling receptor activity

Inferred from mutant phenotype Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92854-1)

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.
Isoform 2 (identifier: Q92854-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 862841Semaphorin-4D
PRO_0000032327

Regions

Topological domain22 – 734713Extracellular Potential
Transmembrane735 – 75521Helical; Potential
Topological domain756 – 862107Cytoplasmic Potential
Domain22 – 500479Sema
Domain502 – 55150PSI
Domain554 – 63683Ig-like C2-type

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Ref.9 Ref.11
Glycosylation741N-linked (GlcNAc...); atypical Ref.9
Glycosylation771N-linked (GlcNAc...) Ref.9 Ref.11
Glycosylation1391N-linked (GlcNAc...) Ref.11
Glycosylation1911N-linked (GlcNAc...) Ref.11
Glycosylation3291N-linked (GlcNAc...) Ref.11
Glycosylation3791N-linked (GlcNAc...) Ref.9
Glycosylation4191N-linked (GlcNAc...) Ref.7 Ref.9 Ref.11
Glycosylation6131N-linked (GlcNAc...) Potential
Glycosylation6321N-linked (GlcNAc...) Potential
Disulfide bond97 ↔ 108 Ref.10 Ref.11
Disulfide bond126 ↔ 135 Ref.10 Ref.11
Disulfide bond257 ↔ 370 Ref.10 Ref.11
Disulfide bond281 ↔ 326 Ref.10 Ref.11
Disulfide bond503 ↔ 520 Ref.10 Ref.11
Disulfide bond509 ↔ 553 Ref.10 Ref.11
Disulfide bond512 ↔ 529 Ref.10 Ref.11
Disulfide bond576 ↔ 624 Ref.10 Ref.11

Natural variations

Alternative sequence555 – 738184DKSKG…RLLMS → ASSPKPLPPPGSSSLSCLGH VGDRRLSSPWTPWPASGAGP DSSSRVSLLPPFLSDQAQHV HALGNFYLFCQATGPADIRF VWEKNGRALETCVPVQTHAL PDGRAHALSWLQDAIRESAE YRCSVLSSAGNKTSKVQVAV MRPEVTHQERWTRELSAWRA VAGEHDRMMQSWRKAWESCS KDTL in isoform 2.
VSP_039483
Alternative sequence739 – 862124Missing in isoform 2.
VSP_039484
Natural variant721A → T.
Corresponds to variant rs13284404 [ dbSNP | Ensembl ].
VAR_030293
Natural variant3271A → T.
Corresponds to variant rs11526468 [ dbSNP | Ensembl ].
VAR_057175

Experimental info

Mutagenesis100 – 1012KG → DT: Abolishes PLXNB1 binding.
Mutagenesis181 – 1822FL → ER: Abolishes PLXNB1 binding.
Mutagenesis2441F → N: Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with S-246. Ref.11
Mutagenesis2461F → S: Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with N-244. Ref.11
Mutagenesis3951K → E: Strongly reduces PLXNB1 binding. Ref.11
Sequence conflict5921G → D in AAH54500. Ref.3

Secondary structure

.................................................................................................................................. 862
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 7B18EFEA98789371

FASTA86296,150
        10         20         30         40         50         60 
MRMCTPIRGL LMALAVMFGT AMAFAPIPRI TWEHREVHLV QFHEPDIYNY SALLLSEDKD 

        70         80         90        100        110        120 
TLYIGAREAV FAVNALNISE KQHEVYWKVS EDKKAKCAEK GKSKQTECLN YIRVLQPLSA 

       130        140        150        160        170        180 
TSLYVCGTNA FQPACDHLNL TSFKFLGKNE DGKGRCPFDP AHSYTSVMVD GELYSGTSYN 

       190        200        210        220        230        240 
FLGSEPIISR NSSHSPLRTE YAIPWLNEPS FVFADVIRKS PDSPDGEDDR VYFFFTEVSV 

       250        260        270        280        290        300 
EYEFVFRVLI PRIARVCKGD QGGLRTLQKK WTSFLKARLI CSRPDSGLVF NVLRDVFVLR 

       310        320        330        340        350        360 
SPGLKVPVFY ALFTPQLNNV GLSAVCAYNL STAEEVFSHG KYMQSTTVEQ SHTKWVRYNG 

       370        380        390        400        410        420 
PVPKPRPGAC IDSEARAANY TSSLNLPDKT LQFVKDHPLM DDSVTPIDNR PRLIKKDVNY 

       430        440        450        460        470        480 
TQIVVDRTQA LDGTVYDVMF VSTDRGALHK AISLEHAVHI IEETQLFQDF EPVQTLLLSS 

       490        500        510        520        530        540 
KKGNRFVYAG SNSGVVQAPL AFCGKHGTCE DCVLARDPYC AWSPPTATCV ALHQTESPSR 

       550        560        570        580        590        600 
GLIQEMSGDA SVCPDKSKGS YRQHFFKHGG TAELKCSQKS NLARVFWKFQ NGVLKAESPK 

       610        620        630        640        650        660 
YGLMGRKNLL IFNLSEGDSG VYQCLSEERV KNKTVFQVVA KHVLEVKVVP KPVVAPTLSV 

       670        680        690        700        710        720 
VQTEGSRIAT KVLVASTQGS SPPTPAVQAT SSGAITLPPK PAPTGTSCEP KIVINTVPQL 

       730        740        750        760        770        780 
HSEKTMYLKS SDNRLLMSLF LFFFVLFLCL FFYNCYKGYL PRQCLKFRSA LLIGKKKPKS 

       790        800        810        820        830        840 
DFCDREQSLK ETLVEPGSFS QQNGEHPKPA LDTGYETEQD TITSKVPTDR EDSQRIDDLS 

       850        860 
ARDKPFDVKC ELKFADSDAD GD 

« Hide

Isoform 2 [UniParc].

Checksum: 93ED5D62D6A17ED1
Show »

FASTA73882,164

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Structural basis of semaphorin-plexin signalling."
Janssen B.J., Robinson R.A., Perez-Branguli F., Bell C.H., Mitchell K.J., Siebold C., Jones E.Y.
Nature 467:1118-1122(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001135759.1. NM_001142287.1.
NP_006369.3. NM_006378.3.
XP_005251711.1. XM_005251654.1.
UniGeneHs.494406.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OLZX-ray2.00A/B22-677[»]
3OL2X-ray2.99A22-677[»]
ProteinModelPortalQ92854.
SMRQ92854. Positions 24-648.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115766. 5 interactions.
DIPDIP-59221N.
IntActQ92854. 2 interactions.
STRING9606.ENSP00000343418.

PTM databases

PhosphoSiteQ92854.

Polymorphism databases

DMDM8134701.

Proteomic databases

PaxDbQ92854.
PeptideAtlasQ92854.
PRIDEQ92854.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339861; ENSP00000344923; ENSG00000187764. [Q92854-2]
ENST00000343780; ENSP00000343418; 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]
GeneID10507.
KEGGhsa:10507.
UCSCuc004aqo.1. human. [Q92854-1]
uc011ltm.1. human. [Q92854-2]

Organism-specific databases

CTD10507.
GeneCardsGC09M091975.
HGNCHGNC:10732. SEMA4D.
HPAHPA015662.
HPA023277.
MIM601866. gene.
neXtProtNX_Q92854.
PharmGKBPA35654.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326211.
HOGENOMHOG000111669.
HOVERGENHBG061627.
InParanoidQ8N8B0.
KOK06521.
OMAAWESCNQ.
OrthoDBEOG71K62C.
PhylomeDBQ92854.
TreeFamTF316102.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ92854.
BgeeQ92854.
CleanExHS_SEMA4D.
GenevestigatorQ92854.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProIPR007110. 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]
PANTHERPTHR11036. PTHR11036. 1 hit.
PfamPF00047. ig. 1 hit.
PF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
[Graphical view]
SUPFAMSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS51004. SEMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ92854.
GeneWikiSEMA4D.
GenomeRNAi10507.
NextBio39858.
PROQ92854.
SOURCESearch...

Entry information

Entry nameSEM4D_HUMAN
AccessionPrimary (citable) accession number: Q92854
Secondary accession number(s): B2RPM6, Q7Z5S4, Q8N8B0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries