| Tag | Content |
|---|
| CPLM ID | CPLM-012062 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Dentin matrix acidic phosphoprotein 1 |
Protein Synonyms/Alias | DMP-1; Dentin matrix protein 1 |
Gene Name | DMP1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 124 | DDSGPGPKDRQEGGN | ubiquitination | [1] |
|
Reference | [1] Global identification of modular cullin-RING ligase substrates. Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ. Cell. 2011 Oct 14;147(2):459-74. [ PMID: 21963094] |
Functional Description | May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite. |
Sequence Annotation | MOTIF 364 366 Cell attachment site (Potential).
CARBOHYD 25 25 N-linked (GlcNAc...) (Potential).
CARBOHYD 285 285 N-linked (GlcNAc...) (Potential).
CARBOHYD 324 324 N-linked (GlcNAc...) (Potential).
CARBOHYD 345 345 N-linked (GlcNAc...) (Potential).
CARBOHYD 351 351 N-linked (GlcNAc...) (Potential).
CARBOHYD 413 413 N-linked (GlcNAc...) (Potential).
CARBOHYD 426 426 N-linked (GlcNAc...) (Potential).
CARBOHYD 467 467 N-linked (GlcNAc...) (Potential). |
Keyword | Alternative splicing; Biomineralization; Complete proteome; Cytoplasm; Extracellular matrix; Glycoprotein; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Secreted; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 513 AA |
Protein Sequence | MKISILLMFL WGLSCALPVT RYQNNESEDS EEWKGHLAQA PTPPLESSES SEGSKVSSEE 60
QANEDPSDST QSEEGLGSDD HQYIYRLAGG FSRSTGKGGD DKDDDEDDSG DDTFGDDDSG 120
PGPKDRQEGG NSRLGSDEDS DDTIQASEES APQGQDSAQD TTSESRELDN EDRVDSKPEG 180
GDSTQESESE EHWVGGGSDG ESSHGDGSEL DDEGMQSDDP ESIRSERGNS RMNSAGMKSK 240
ESGENSEQAN TQDSGGSQLL EHPSRKIFRK SRISEEDDRS ELDDNNTMEE VKSDSTENSN 300
SRDTGLSQPR RDSKGDSQED SKENLSQEES QNVDGPSSES SQEANLSSQE NSSESQEEVV 360
SESRGDNPDP TTSYVEDQED SDSSEEDSSH TLSHSKSESR EEQADSESSE SLNFSEESPE 420
SPEDENSSSQ EGLQSHSSSA ESQSEESHSE EDDSDSQDSS RSKEDSNSTE SKSSSEEDGQ 480
LKNIEIESRK LTVDAYHNKP IGDQDDNDCQ DGY 513 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005730; C:nucleolus; IDA:HPA. GO:0005578; C:proteinaceous extracellular matrix; TAS:ProtInc. GO:0005509; F:calcium ion binding; TAS:ProtInc. GO:0050840; F:extracellular matrix binding; IEA:Compara. GO:0005178; F:integrin binding; TAS:ProtInc. GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW. GO:0030198; P:extracellular matrix organization; IEA:Compara. GO:0001503; P:ossification; TAS:ProtInc. GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |