Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9BUD6

- SPON2_HUMAN

UniProt

Q9BUD6 - SPON2_HUMAN

(max 400 entries)x

Your basket is currently empty.

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

Protein

Spondin-2

Gene

SPON2

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

Functioni

Cell adhesion protein that promotes adhesion and outgrowth of hippocampal embryonic neurons. Binds directly to bacteria and their components and functions as an opsonin for macrophage phagocytosis of bacteria. Essential in the initiation of the innate immune response and represents a unique pattern-recognition molecule in the ECM for microbial pathogens (By similarity). Binds bacterial lipopolysaccharide (LPS).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Divalent metal cationSequence Analysis
Metal bindingi122 – 1221Divalent metal cationSequence Analysis
Metal bindingi141 – 1411Divalent metal cationCurated
Sitei141 – 1411Important for metal ion-dependent interaction with integrinCurated
Metal bindingi160 – 1601Calcium
Metal bindingi188 – 1881Calcium
Metal bindingi192 – 1921Calcium; via carbonyl oxygen

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. axon guidance Source: ProtInc
  2. cell adhesion Source: UniProtKB-KW
  3. innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Spondin-2
Alternative name(s):
Differentially expressed in cancerous and non-cancerous lung cells 1
Short name:
DIL-1
Mindin
Gene namesi
Name:SPON2
Synonyms:DIL1
ORF Names:UNQ435/PRO866
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11253. SPON2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221E → A: Strongly reduced metal-dependent interaction with integrin; when associated with A-141. 1 Publication
Mutagenesisi141 – 1411E → A: Strongly reduced metal-dependent interaction with integrin; when associated with A-122. 1 Publication

Organism-specific databases

PharmGKBiPA36083.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 331305Spondin-2PRO_0000035870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 1711 PublicationPROSITE-ProRule annotation
Glycosylationi283 – 2831C-linked (Man)

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9BUD6.
PaxDbiQ9BUD6.
PRIDEiQ9BUD6.

PTM databases

PhosphoSiteiQ9BUD6.

Expressioni

Tissue specificityi

Expressed in normal lung tissue but not in lung carcinoma cell lines.1 Publication

Gene expression databases

BgeeiQ9BUD6.
CleanExiHS_SPON2.
ExpressionAtlasiQ9BUD6. baseline and differential.
GenevestigatoriQ9BUD6.

Organism-specific databases

HPAiHPA040170.
HPA043890.

Interactioni

Subunit structurei

Monomer. Interacts with integrin.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000290902.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 499
Turni53 – 553
Beta strandi63 – 653
Beta strandi67 – 7711
Helixi92 – 1009
Helixi104 – 11714
Beta strandi120 – 1267
Beta strandi129 – 1313
Beta strandi135 – 1439
Beta strandi148 – 15710
Beta strandi159 – 16911
Beta strandi178 – 1847
Beta strandi190 – 1923
Beta strandi215 – 2184
Beta strandi230 – 2323
Beta strandi236 – 2438

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D34X-ray1.80A/B27-249[»]
ProteinModelPortaliQ9BUD6.
SMRiQ9BUD6. Positions 34-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BUD6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 221191SpondinPROSITE-ProRule annotationAdd
BLAST
Domaini277 – 33155TSP type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 spondin domain.PROSITE-ProRule annotation
Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG279286.
GeneTreeiENSGT00740000115000.
HOGENOMiHOG000114626.
HOVERGENiHBG052919.
InParanoidiQ9BUD6.
OrthoDBiEOG71CFK9.
PhylomeDBiQ9BUD6.
TreeFamiTF326913.

Family and domain databases

InterProiIPR009465. Spondin_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF06468. Spond_N. 1 hit.
[Graphical view]
SMARTiSM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiPS51020. SPONDIN. 1 hit.
PS50092. TSP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BUD6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MENPSPAAAL GKALCALLLA TLGAAGQPLG GESICSARAL AKYSITFTGK
60 70 80 90 100
WSQTAFPKQY PLFRPPAQWS SLLGAAHSSD YSMWRKNQYV SNGLRDFAER
110 120 130 140 150
GEAWALMKEI EAAGEALQSV HEVFSAPAVP SGTGQTSAEL EVQRRHSLVS
160 170 180 190 200
FVVRIVPSPD WFVGVDSLDL CDGDRWREQA ALDLYPYDAG TDSGFTFSSP
210 220 230 240 250
NFATIPQDTV TEITSSSPSH PANSFYYPRL KALPPIARVT LVRLRQSPRA
260 270 280 290 300
FIPPAPVLPS RDNEIVDSAS VPETPLDCEV SLWSSWGLCG GHCGRLGTKS
310 320 330
RTRYVRVQPA NNGSPCPELE EEAECVPDNC V
Length:331
Mass (Da):35,846
Last modified:November 30, 2010 - v3
Checksum:i8AF827142D921705
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381R → G.
Corresponds to variant rs6836335 [ dbSNP | Ensembl ].
VAR_055149
Natural varianti40 – 401L → P.5 Publications
Corresponds to variant rs922697 [ dbSNP | Ensembl ].
VAR_019701
Natural varianti122 – 1221E → A.4 Publications
Corresponds to variant rs11247975 [ dbSNP | Ensembl ].
VAR_019702
Natural varianti242 – 2421V → L.4 Publications
Corresponds to variant rs2279279 [ dbSNP | Ensembl ].
VAR_019703

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB027466 mRNA. Translation: BAA85892.1.
AY358948 mRNA. Translation: AAQ89307.1.
AK074618 mRNA. Translation: BAC11092.1.
AK074770 mRNA. Translation: BAC11196.1.
AC092535 Genomic DNA. Translation: AAY40988.1.
CH471131 Genomic DNA. Translation: EAW82604.1.
CH471131 Genomic DNA. Translation: EAW82606.1.
BC002707 mRNA. Translation: AAH02707.1.
BC036341 mRNA. Translation: AAH36341.1.
CCDSiCCDS3347.1.
RefSeqiNP_001121797.1. NM_001128325.2.
NP_001185950.1. NM_001199021.1.
NP_036577.1. NM_012445.3.
UniGeneiHs.302963.
Hs.635350.
Hs.736956.

Genome annotation databases

EnsembliENST00000290902; ENSP00000290902; ENSG00000159674.
ENST00000431380; ENSP00000394832; ENSG00000159674.
ENST00000617421; ENSP00000483599; ENSG00000159674.
GeneIDi10417.
KEGGihsa:10417.
UCSCiuc003gco.4. human.

Polymorphism databases

DMDMi313104285.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB027466 mRNA. Translation: BAA85892.1 .
AY358948 mRNA. Translation: AAQ89307.1 .
AK074618 mRNA. Translation: BAC11092.1 .
AK074770 mRNA. Translation: BAC11196.1 .
AC092535 Genomic DNA. Translation: AAY40988.1 .
CH471131 Genomic DNA. Translation: EAW82604.1 .
CH471131 Genomic DNA. Translation: EAW82606.1 .
BC002707 mRNA. Translation: AAH02707.1 .
BC036341 mRNA. Translation: AAH36341.1 .
CCDSi CCDS3347.1.
RefSeqi NP_001121797.1. NM_001128325.2.
NP_001185950.1. NM_001199021.1.
NP_036577.1. NM_012445.3.
UniGenei Hs.302963.
Hs.635350.
Hs.736956.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3D34 X-ray 1.80 A/B 27-249 [» ]
ProteinModelPortali Q9BUD6.
SMRi Q9BUD6. Positions 34-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000290902.

PTM databases

PhosphoSitei Q9BUD6.

Polymorphism databases

DMDMi 313104285.

Proteomic databases

MaxQBi Q9BUD6.
PaxDbi Q9BUD6.
PRIDEi Q9BUD6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290902 ; ENSP00000290902 ; ENSG00000159674 .
ENST00000431380 ; ENSP00000394832 ; ENSG00000159674 .
ENST00000617421 ; ENSP00000483599 ; ENSG00000159674 .
GeneIDi 10417.
KEGGi hsa:10417.
UCSCi uc003gco.4. human.

Organism-specific databases

CTDi 10417.
GeneCardsi GC04M001150.
HGNCi HGNC:11253. SPON2.
HPAi HPA040170.
HPA043890.
MIMi 605918. gene.
neXtProti NX_Q9BUD6.
PharmGKBi PA36083.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279286.
GeneTreei ENSGT00740000115000.
HOGENOMi HOG000114626.
HOVERGENi HBG052919.
InParanoidi Q9BUD6.
OrthoDBi EOG71CFK9.
PhylomeDBi Q9BUD6.
TreeFami TF326913.

Enzyme and pathway databases

Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

EvolutionaryTracei Q9BUD6.
GenomeRNAii 10417.
NextBioi 35490182.
PROi Q9BUD6.
SOURCEi Search...

Gene expression databases

Bgeei Q9BUD6.
CleanExi HS_SPON2.
ExpressionAtlasi Q9BUD6. baseline and differential.
Genevestigatori Q9BUD6.

Family and domain databases

InterProi IPR009465. Spondin_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF06468. Spond_N. 1 hit.
[Graphical view ]
SMARTi SM00209. TSP1. 1 hit.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 1 hit.
PROSITEi PS51020. SPONDIN. 1 hit.
PS50092. TSP1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display."
    Manda R., Kohno T., Matsuno Y., Takenoshita S., Kuwano H., Yokota J.
    Genomics 61:5-14(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS PRO-40 AND ALA-122.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PRO-40 AND LEU-242.
  3. "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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PRO-40; ALA-122 AND LEU-242.
  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], VARIANT ALA-122.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS PRO-40; ALA-122 AND LEU-242.
  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], VARIANTS PRO-40 AND LEU-242.
    Tissue: Colon and Placenta.
  7. "Structure of the F-spondin domain of mindin, an integrin ligand and pattern recognition molecule."
    Li Y., Cao C., Jia W., Yu L., Mo M., Wang Q., Huang Y., Lim J.-M., Ishihara M., Wells L., Azadi P., Robinson H., He Y.-W., Zhang L., Mariuzza R.A.
    EMBO J. 28:286-297(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-249 IN COMPLEX WITH METAL IONS, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, GLYCOSYLATION AT TRP-283, INTERACTION WITH INTEGRIN AND BACTERIAL LIPOPOLYSACCHARIDE, MUTAGENESIS OF GLU-122 AND GLU-141, DISULFIDE BOND.

Entry informationi

Entry nameiSPON2_HUMAN
AccessioniPrimary (citable) accession number: Q9BUD6
Secondary accession number(s): D3DVN9, Q4W5N4, Q9ULW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 109 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 chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3