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Protein

Basic salivary proline-rich protein 1

Gene

PRB1

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

Names & Taxonomyi

Protein namesi
Recommended name:
Basic salivary proline-rich protein 1
Short name:
Salivary proline-rich protein
Cleaved into the following 3 chains:
Gene namesi
Name:PRB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:9337. PRB1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33699.

Polymorphism and mutation databases

BioMutaiPRB1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 392376Basic salivary proline-rich protein 1PRO_0000022129Add
BLAST
Chaini17 – 9175Proline-rich peptide II-2PRO_0000372441Add
BLAST
Chaini275 – 392118Basic peptide IB-6PRO_0000022130Add
BLAST
Chaini337 – 39256Peptide P-HPRO_0000022131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Pyrrolidone carboxylic acid2 Publications
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei40 – 401Phosphoserine; alternate1 Publication
Glycosylationi40 – 401O-linked (Hex); alternate1 Publication
Glycosylationi87 – 871O-linked (HexNAc...); prevalent in head and neck cancer patients1 Publication
Modified residuei92 – 921Phosphoserine1 Publication
Modified residuei150 – 1501Phosphoserine; alternate1 Publication
Glycosylationi150 – 1501O-linked (Hex); alternate1 Publication
Glycosylationi330 – 3301O-linked (HexNAc...); 5 times prevalence in head and neck cancers

Post-translational modificationi

O-glycosylated.1 Publication
Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa in the P3 position is mostly lysine. The endoprotease may be of microbial origin.1 Publication
Pyroglutamate formation occurs on terminal Gln residues of cleaved peptides. Besides on the N-terminal of mature PBR1, pyroglutamate formation found on at least Gln-58.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP04280.
TopDownProteomicsiP04280.

PTM databases

iPTMnetiP04280.
PhosphoSiteiP04280.

Expressioni

Gene expression databases

CleanExiHS_PRB1.

Interactioni

Protein-protein interaction databases

BioGridi111534. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP04280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati53 – 72201Add
BLAST
Repeati73 – 92202Add
BLAST
Repeati93 – 112203Add
BLAST
Repeati114 – 133204Add
BLAST
Repeati134 – 153205Add
BLAST
Repeati154 – 173206Add
BLAST
Repeati175 – 194207Add
BLAST
Repeati195 – 214208Add
BLAST
Repeati215 – 234209Add
BLAST
Repeati236 – 2552010Add
BLAST
Repeati256 – 2752011Add
BLAST
Repeati276 – 2952012Add
BLAST
Repeati297 – 3162013Add
BLAST
Repeati317 – 3362014Add
BLAST
Repeati338 – 3572015Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 35730515 X 20 AA approximate tandem repeats of P-P-G-K-P-Q-G-P-P-[PAQ]-Q-[GE]-[GD]-[NKS]-[KSQRN]-[PRQS]-[QS] [GPS]-[PQAR]-[PSR]Add
BLAST

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

InParanoidiP04280.
KOiK13911.

Family and domain databases

InterProiIPR026086. Pro-rich.
[Graphical view]
PANTHERiPTHR23203. PTHR23203. 1 hit.
PfamiPF15240. Pro-rich. 3 hits.
[Graphical view]
SMARTiSM01412. Pro-rich. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P04280-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLILLSVAL LALSSAQNLN EDVSQEESPS LIAGNPQGPS PQGGNKPQGP
60 70 80 90 100
PPPPGKPQGP PPQGGNKPQG PPPPGKPQGP PPQGDKSRSP RSPPGKPQGP
110 120 130 140 150
PPQGGNQPQG PPPPPGKPQG PPPQGGNKPQ GPPPPGKPQG PPPQGDKSQS
160 170 180 190 200
PRSPPGKPQG PPPQGGNQPQ GPPPPPGKPQ GPPPQGGNKP QGPPPPGKPQ
210 220 230 240 250
GPPPQGDKSQ SPRSPPGKPQ GPPPQGGNQP QGPPPPPGKP QGPPQQGGNR
260 270 280 290 300
PQGPPPPGKP QGPPPQGDKS RSPQSPPGKP QGPPPQGGNQ PQGPPPPPGK
310 320 330 340 350
PQGPPPQGGN KPQGPPPPGK PQGPPAQGGS KSQSARAPPG KPQGPPQQEG
360 370 380 390
NNPQGPPPPA GGNPQQPQAP PAGQPQGPPR PPQGGRPSRP PQ
Length:392
Mass (Da):38,546
Last modified:September 13, 2004 - v2
Checksum:iB3F4C5A01F335CB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 3316NLNED…PSLIA → SCVGFYSVFLFSLCPL in AAA36502 (PubMed:6089212).CuratedAdd
BLAST
Sequence conflicti40 – 401S → P in AAA36502 (PubMed:6089212).Curated
Sequence conflicti85 – 862DK → GKR in AAA36502 (PubMed:6089212).Curated
Sequence conflicti128 – 1281K → R in CAA30395 (PubMed:2851479).Curated
Sequence conflicti216 – 2172PG → R in AAA36502 (PubMed:6089212).Curated
Sequence conflicti271 – 2711R → Q in AAB27288 (PubMed:8317492).Curated
Sequence conflicti274 – 2741Q → R in CAA30395 (PubMed:2851479).Curated
Sequence conflicti278 – 2781G → R in CAA30395 (PubMed:2851479).Curated
Sequence conflicti307 – 3071Q → T in AAA36503 (PubMed:6089212).Curated
Sequence conflicti326 – 3261A → P in AAB27289 (PubMed:8317492).Curated
Sequence conflicti330 – 3301S → C in AAA36503 (PubMed:6089212).Curated
Sequence conflicti337 – 3371A → S in AAA13341 (PubMed:8422499).Curated
Sequence conflicti337 – 3371A → S in CAA30395 (PubMed:2851479).Curated
Sequence conflicti337 – 3371A → S AA sequence (PubMed:6671974).Curated
Sequence conflicti385 – 3862GR → DK in AAA36503 (PubMed:6089212).Curated

Polymorphismi

The number of repeats is polymorphic and varies among different alleles. The sequence shown is that of allele L (long). There are allele M (medium) and allele S (short) which contain 12 and 9 approximate tandem repeats repectively.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 15361Missing in allele M.
VAR_019693Add
BLAST
Natural varianti106 – 319214Missing .1 Publication
VAR_005562Add
BLAST
Natural varianti106 – 299194Missing .
VAR_005561Add
BLAST
Natural varianti134 – 255122Missing in allele S.
VAR_019694Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03204 mRNA. Translation: AAA60185.1.
K03205 mRNA. Translation: AAA60186.1.
K03206 mRNA. Translation: AAA60187.1.
S52986 Genomic DNA. Translation: AAA13341.2.
M97220 Genomic DNA. Translation: AAB05816.1.
K02575 Genomic DNA. Translation: AAA36502.1.
K02576 Genomic DNA. Translation: AAA36503.1.
X07516 Genomic DNA. Translation: CAA30394.2.
X07517 Genomic DNA. Translation: CAA30395.2.
S62928 Genomic DNA. Translation: AAB27288.2.
S62941 Genomic DNA. Translation: AAB27289.1.
PIRiB40750. PIHUB6.
C38355.
D40750.
RefSeqiNP_005030.2. NM_005039.3.
NP_955385.1. NM_199353.2.
NP_955386.1. NM_199354.2.
UniGeneiHs.631726.

Genome annotation databases

GeneIDi5542.
KEGGihsa:5542.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03204 mRNA. Translation: AAA60185.1.
K03205 mRNA. Translation: AAA60186.1.
K03206 mRNA. Translation: AAA60187.1.
S52986 Genomic DNA. Translation: AAA13341.2.
M97220 Genomic DNA. Translation: AAB05816.1.
K02575 Genomic DNA. Translation: AAA36502.1.
K02576 Genomic DNA. Translation: AAA36503.1.
X07516 Genomic DNA. Translation: CAA30394.2.
X07517 Genomic DNA. Translation: CAA30395.2.
S62928 Genomic DNA. Translation: AAB27288.2.
S62941 Genomic DNA. Translation: AAB27289.1.
PIRiB40750. PIHUB6.
C38355.
D40750.
RefSeqiNP_005030.2. NM_005039.3.
NP_955385.1. NM_199353.2.
NP_955386.1. NM_199354.2.
UniGeneiHs.631726.

3D structure databases

ProteinModelPortaliP04280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111534. 3 interactions.

PTM databases

iPTMnetiP04280.
PhosphoSiteiP04280.

Polymorphism and mutation databases

BioMutaiPRB1.

Proteomic databases

PRIDEiP04280.
TopDownProteomicsiP04280.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5542.
KEGGihsa:5542.

Organism-specific databases

CTDi5542.
GeneCardsiPRB1.
HGNCiHGNC:9337. PRB1.
MIMi180989. gene.
neXtProtiNX_P04280.
PharmGKBiPA33699.
GenAtlasiSearch...

Phylogenomic databases

InParanoidiP04280.
KOiK13911.

Miscellaneous databases

GeneWikiiPRB1.
GenomeRNAii5542.
PROiP04280.
SOURCEiSearch...

Gene expression databases

CleanExiHS_PRB1.

Family and domain databases

InterProiIPR026086. Pro-rich.
[Graphical view]
PANTHERiPTHR23203. PTHR23203. 1 hit.
PfamiPF15240. Pro-rich. 3 hits.
[Graphical view]
SMARTiSM01412. Pro-rich. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Differential RNA splicing and post-translational cleavages in the human salivary proline-rich protein gene system."
    Maeda N., Kim H.-S., Azen E.A., Smithies O.
    J. Biol. Chem. 260:11123-11130(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE M).
  2. "The structure and evolution of the human salivary proline-rich protein gene family."
    Kim H.-S., Lyons K.M., Saitoh E., Azen E.A., Smithies O., Maeda N.
    Mamm. Genome 4:3-14(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE M).
  3. "Basic proline-rich proteins from human parotid saliva: relationships of the covalent structures of ten proteins from a single individual."
    Kauffman D.L., Bennick A., Blum M., Keller P.J.
    Biochemistry 30:3351-3356(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-91, PYROGLUTAMATE FORMATION AT GLN-17.
    Tissue: Saliva.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-251 AND 300-392 (ALLELE M).
  5. "Length polymorphisms in human proline-rich protein genes generated by intragenic unequal crossing over."
    Lyons K.M., Stein J.H., Smithies O.
    Genetics 120:267-278(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-392 (ALLELES M AND S), POLYMORPHISM.
  6. "PRBI gene variants coding for length and null polymorphisms among human salivary Ps, PmF, PmS, and Pe proline-rich proteins (PRPs)."
    Azen E.A., Latreille P., Niece R.L.
    Am. J. Hum. Genet. 53:264-278(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-392 (ALLELES L AND M).
  7. "Basic proline-rich proteins from human parotid saliva: complete covalent structures of proteins IB-1 and IB-6."
    Kauffman D., Hofmann T., Bennick A., Keller P.
    Biochemistry 25:2387-2392(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 275-392, SUBCELLULAR LOCATION.
    Tissue: Saliva.
  8. "Further fractionation of basic proline-rich peptides from human parotid saliva and complete amino acid sequence of basic proline-rich peptide P-H."
    Saitoh E., Isemura S., Sanada K.
    J. Biochem. 94:1991-1999(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 337-392.
    Tissue: Saliva.
  9. "Identification of Lys-Pro-Gln as a novel cleavage site specificity of saliva-associated proteases."
    Helmerhorst E.J., Sun X., Salih E., Oppenheim F.G.
    J. Biol. Chem. 283:19957-19966(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Finding new posttranslational modifications in salivary proline-rich proteins."
    Vitorino R., Alves R., Barros A., Caseiro A., Ferreira R., Lobo M.C., Bastos A., Duarte J., Carvalho D., Santos L.L., Amado F.L.
    Proteomics 10:3732-3742(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-40; SER-87 AND SER-150, PHOSPHORYLATION AT SER-40; SER-92 AND SER-150, PYROGLUTAMATE FORMATION AT GLN-17, IDENTIFICATION BY MASS SPECTROMETRY, VARIANTS ALLELE M AND S.

Entry informationi

Entry nameiPRP1_HUMAN
AccessioniPrimary (citable) accession number: P04280
Secondary accession number(s): Q08805
, Q15186, Q15187, Q15214, Q15215, Q16038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: September 13, 2004
Last modified: June 8, 2016
This is version 122 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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.