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Q61711

- SIAL_MOUSE

UniProt

Q61711 - SIAL_MOUSE

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Protein

Bone sialoprotein 2

Gene

Ibsp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment (By similarity).By similarity

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
  2. cell adhesion Source: UniProt
  3. cellular response to growth factor stimulus Source: MGI
  4. extracellular matrix organization Source: MGI
  5. osteoblast differentiation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Biomineralization, Cell adhesion

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Bone sialoprotein 2
Alternative name(s):
Bone sialoprotein II
Short name:
BSP II
Cell-binding sialoprotein
Integrin-binding sialoprotein
Gene namesi
Name:Ibsp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:96389. Ibsp.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProt
  2. membrane Source: Ensembl
  3. membrane-bounded vesicle Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616By similarityAdd
BLAST
Chaini17 – 324308Bone sialoprotein 2PRO_0000020331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei75 – 751PhosphoserineBy similarity
Modified residuei76 – 761PhosphoserineBy similarity
Modified residuei95 – 951PhosphoserineBy similarity
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
Modified residuei155 – 1551PhosphoserineBy similarity
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
Modified residuei320 – 3201SulfotyrosineBy similarity
Modified residuei321 – 3211SulfotyrosineBy similarity

Post-translational modificationi

N-glycosylated; glycans consist of sialylated and core-fucosylated bi-, tri- and tetraantennary chains.By similarity
Sulfated on either Tyr-320 or Tyr-321.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

PRIDEiQ61711.

PTM databases

PhosphoSiteiQ61711.

Expressioni

Gene expression databases

BgeeiQ61711.
CleanExiMM_IBSP.
GenevestigatoriQ61711.

Interactioni

Protein-protein interaction databases

IntActiQ61711. 1 interaction.
MINTiMINT-8283231.
STRINGi10090.ENSMUSP00000031246.

Structurei

3D structure databases

ProteinModelPortaliQ61711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi293 – 2953Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 179112Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi77 – 848Poly-Glu
Compositional biasi157 – 17216Poly-GluAdd
BLAST

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG238366.
GeneTreeiENSGT00390000002485.
HOGENOMiHOG000234824.
HOVERGENiHBG007981.
InParanoidiQ61711.
KOiK06253.
OMAiAYEDEYS.
OrthoDBiEOG7NW6BX.
TreeFamiTF338678.

Family and domain databases

InterProiIPR008412. BSP_II.
[Graphical view]
PANTHERiPTHR10345. PTHR10345. 1 hit.
PfamiPF05432. BSP_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q61711-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTALILLSI LGMACAFSMK NFHRRIKAED SEENGVFKYR PRYFLYKHAY
60 70 80 90 100
FYPPLKRFPV QGGSDSSEEN GDGDSSEEEG EEEETSNEEE NNEDSEGNED
110 120 130 140 150
QEAEAENSTL STLSGVTASY GAETTPQAQT FELAALQLPK KAGDAESRAP
160 170 180 190 200
KVKESDEEEE EEEEEEENEN EEAEVDENEL AVNGTSTNST EVDGGNGSSG
210 220 230 240 250
GDNGEEAEAE EASVTEAGAE GTTGGRELTS VGTQTAVLLN GFQQTTPPPE
260 270 280 290 300
AYGTTSPPIR KSSTVEYGGE YEQTGNEYNN EYEVYDNENG EPRGDTYRAY
310 320
EDEYSYYKGH GYEGYEGQNY YYHQ
Length:324
Mass (Da):35,734
Last modified:July 27, 2011 - v2
Checksum:iD0CD12EA82D27773
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731G → C in AAA37326. 1 PublicationCurated
Sequence conflicti108 – 1081S → A in AAA21726. (PubMed:8180469)Curated
Sequence conflicti108 – 1081S → A in AAA37326. 1 PublicationCurated
Sequence conflicti259 – 2591I → V in AAA37326. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20232 mRNA. Translation: AAA21726.1.
L23801 mRNA. Translation: AAA37326.1.
AK132371 mRNA. Translation: BAE21132.1.
BC045143 mRNA. Translation: AAH45143.1.
CH466529 Genomic DNA. Translation: EDL20226.1.
CCDSiCCDS19485.1.
PIRiI49768.
RefSeqiNP_032344.2. NM_008318.3.
UniGeneiMm.4987.

Genome annotation databases

EnsembliENSMUST00000031246; ENSMUSP00000031246; ENSMUSG00000029306.
GeneIDi15891.
KEGGimmu:15891.
UCSCiuc008ykg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20232 mRNA. Translation: AAA21726.1 .
L23801 mRNA. Translation: AAA37326.1 .
AK132371 mRNA. Translation: BAE21132.1 .
BC045143 mRNA. Translation: AAH45143.1 .
CH466529 Genomic DNA. Translation: EDL20226.1 .
CCDSi CCDS19485.1.
PIRi I49768.
RefSeqi NP_032344.2. NM_008318.3.
UniGenei Mm.4987.

3D structure databases

ProteinModelPortali Q61711.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q61711. 1 interaction.
MINTi MINT-8283231.
STRINGi 10090.ENSMUSP00000031246.

PTM databases

PhosphoSitei Q61711.

Proteomic databases

PRIDEi Q61711.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031246 ; ENSMUSP00000031246 ; ENSMUSG00000029306 .
GeneIDi 15891.
KEGGi mmu:15891.
UCSCi uc008ykg.2. mouse.

Organism-specific databases

CTDi 3381.
MGIi MGI:96389. Ibsp.

Phylogenomic databases

eggNOGi NOG238366.
GeneTreei ENSGT00390000002485.
HOGENOMi HOG000234824.
HOVERGENi HBG007981.
InParanoidi Q61711.
KOi K06253.
OMAi AYEDEYS.
OrthoDBi EOG7NW6BX.
TreeFami TF338678.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

NextBioi 288596.
PROi Q61711.
SOURCEi Search...

Gene expression databases

Bgeei Q61711.
CleanExi MM_IBSP.
Genevestigatori Q61711.

Family and domain databases

InterProi IPR008412. BSP_II.
[Graphical view ]
PANTHERi PTHR10345. PTHR10345. 1 hit.
Pfami PF05432. BSP_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Murine bone sialoprotein (BSP): cDNA cloning, mRNA expression, and genetic mapping."
    Young M.F., Ibaraki K., Kerr J.M., Lyu M.S., Kozak C.A.
    Mamm. Genome 5:108-111(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence of mouse bone sialoprotein II (BSP) cDNA."
    Wuyts W., Tylzanowski P., Merregaert J.
    Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Olfactory epithelium.

Entry informationi

Entry nameiSIAL_MOUSE
AccessioniPrimary (citable) accession number: Q61711
Secondary accession number(s): Q61363, Q80VR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

It is possible that the segments of clustered carboxyl groups mediate the strong binding to hydroxyapatite.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3