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Protein

Secreted phosphoprotein 24

Gene

SPP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Could coordinate an aspect of bone turnover.By similarity

GO - Molecular functioni

  • endopeptidase inhibitor activity Source: ProtInc

GO - Biological processi

  • bone remodeling Source: InterPro
  • platelet degranulation Source: Reactome
  • skeletal system development Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Secreted phosphoprotein 24
Short name:
Spp-24
Alternative name(s):
Secreted phosphoprotein 2
Gene namesi
Name:SPP2
Synonyms:SPP24
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11256. SPP2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • platelet dense granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36086.

Polymorphism and mutation databases

BioMutaiSPP2.
DMDMi2498939.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Chaini30 – 211182Secreted phosphoprotein 24PRO_0000022403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi92 ↔ 103By similarity
Modified residuei96 – 961PhosphoserineCombined sources
Disulfide bondi116 ↔ 134By similarity
Modified residuei145 – 1451PhosphoserineBy similarity
Modified residuei146 – 1461PhosphoserineBy similarity
Modified residuei170 – 1701PhosphoserineBy similarity
Modified residuei173 – 1731PhosphoserineBy similarity
Modified residuei182 – 1821PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ13103.
PaxDbiQ13103.
PeptideAtlasiQ13103.
PRIDEiQ13103.

PTM databases

iPTMnetiQ13103.
PhosphoSiteiQ13103.

Expressioni

Tissue specificityi

Detected in liver and plasma.1 Publication

Developmental stagei

Found in fetal liver and kidney.1 Publication

Gene expression databases

BgeeiQ13103.
CleanExiHS_SPP2.
ExpressionAtlasiQ13103. baseline and differential.
GenevisibleiQ13103. HS.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000168148.

Structurei

3D structure databases

ProteinModelPortaliQ13103.
SMRiQ13103. Positions 33-135.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SPP2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IWPI. Eukaryota.
ENOG410Z1VS. LUCA.
GeneTreeiENSGT00390000009001.
HOGENOMiHOG000264228.
HOVERGENiHBG065800.
InParanoidiQ13103.
OMAiCAGFPVY.
OrthoDBiEOG754HQN.
PhylomeDBiQ13103.
TreeFamiTF335972.

Family and domain databases

InterProiIPR010892. Spp-24.
[Graphical view]
PfamiPF07448. Spp-24. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q13103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISRMEKMTM MMKILIMFAL GMNYWSCSGF PVYDYDPSSL RDALSASVVK
60 70 80 90 100
VNSQSLSPYL FRAFRSSLKR VEVLDENNLV MNLEFSIRET TCRKDSGEDP
110 120 130 140 150
ATCAFQRDYY VSTAVCRSTV KVSAQQVQGV HARCSWSSST SESYSSEEMI
160 170 180 190 200
FGDMLGSHKW RNNYLFGLIS DESISEQFYD RSLGIMRRVL PPGNRRYPNH
210
RHRARINTDF E
Length:211
Mass (Da):24,338
Last modified:November 1, 1997 - v1
Checksum:iAED049E63464E38D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241A → V in AAI06706 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381S → F.1 Publication
Corresponds to variant rs34347825 [ dbSNP | Ensembl ].
VAR_025698

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20530 mRNA. Translation: AAA87905.1.
AJ272265 Genomic DNA. Translation: CAB75571.1.
AJ308099 mRNA. Translation: CAC87050.1.
AC006037 Genomic DNA. Translation: AAX93090.1.
CH471063 Genomic DNA. Translation: EAW71070.1.
BC069401 mRNA. Translation: AAH69401.1.
BC106705 mRNA. Translation: AAI06706.1.
BC112438 mRNA. Translation: AAI12439.1.
CCDSiCCDS2511.1.
PIRiG01654.
RefSeqiNP_008875.1. NM_006944.2.
XP_005246159.1. XM_005246102.2.
XP_011510000.1. XM_011511698.1.
XP_011510001.1. XM_011511699.1.
XP_011510002.1. XM_011511700.1.
UniGeneiHs.444488.

Genome annotation databases

EnsembliENST00000168148; ENSP00000168148; ENSG00000072080.
ENST00000373368; ENSP00000362466; ENSG00000072080.
GeneIDi6694.
KEGGihsa:6694.
UCSCiuc002vvk.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20530 mRNA. Translation: AAA87905.1.
AJ272265 Genomic DNA. Translation: CAB75571.1.
AJ308099 mRNA. Translation: CAC87050.1.
AC006037 Genomic DNA. Translation: AAX93090.1.
CH471063 Genomic DNA. Translation: EAW71070.1.
BC069401 mRNA. Translation: AAH69401.1.
BC106705 mRNA. Translation: AAI06706.1.
BC112438 mRNA. Translation: AAI12439.1.
CCDSiCCDS2511.1.
PIRiG01654.
RefSeqiNP_008875.1. NM_006944.2.
XP_005246159.1. XM_005246102.2.
XP_011510000.1. XM_011511698.1.
XP_011510001.1. XM_011511699.1.
XP_011510002.1. XM_011511700.1.
UniGeneiHs.444488.

3D structure databases

ProteinModelPortaliQ13103.
SMRiQ13103. Positions 33-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000168148.

PTM databases

iPTMnetiQ13103.
PhosphoSiteiQ13103.

Polymorphism and mutation databases

BioMutaiSPP2.
DMDMi2498939.

Proteomic databases

EPDiQ13103.
PaxDbiQ13103.
PeptideAtlasiQ13103.
PRIDEiQ13103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000168148; ENSP00000168148; ENSG00000072080.
ENST00000373368; ENSP00000362466; ENSG00000072080.
GeneIDi6694.
KEGGihsa:6694.
UCSCiuc002vvk.2. human.

Organism-specific databases

CTDi6694.
GeneCardsiSPP2.
HGNCiHGNC:11256. SPP2.
MIMi602637. gene.
neXtProtiNX_Q13103.
PharmGKBiPA36086.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IWPI. Eukaryota.
ENOG410Z1VS. LUCA.
GeneTreeiENSGT00390000009001.
HOGENOMiHOG000264228.
HOVERGENiHBG065800.
InParanoidiQ13103.
OMAiCAGFPVY.
OrthoDBiEOG754HQN.
PhylomeDBiQ13103.
TreeFamiTF335972.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.

Miscellaneous databases

ChiTaRSiSPP2. human.
GenomeRNAii6694.
PROiQ13103.
SOURCEiSearch...

Gene expression databases

BgeeiQ13103.
CleanExiHS_SPP2.
ExpressionAtlasiQ13103. baseline and differential.
GenevisibleiQ13103. HS.

Family and domain databases

InterProiIPR010892. Spp-24.
[Graphical view]
PfamiPF07448. Spp-24. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and molecular cloning of human spp-24, a bone phosphoprotein related in sequence to the cystatin family of thiol protease inhibitors."
    Coulson L., Hu B., Price P.A.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone.
  2. "Characterization of the human secreted phosphoprotein 24 gene (SPP2) and comparison of the protein sequence in nine species."
    Bennett C.S., Khorram Khorshid H.R., Kitchen J.A., Arteta D., Dalgleish R.
    Matrix Biol. 22:641-651(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, VARIANT PHE-38.
    Tissue: Liver.
  3. "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].
  4. 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].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSPP24_HUMAN
AccessioniPrimary (citable) accession number: Q13103
Secondary accession number(s): A4QMV3, Q3B892, Q546M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 119 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.