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Protein

Basic salivary proline-rich protein 4

Gene

PRB4

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 4
Short name:
Salivary proline-rich protein Po
Alternative name(s):
Parotid o protein
Salivary proline-rich protein II-1
Cleaved into the following 3 chains:
Alternative name(s):
Proline-rich peptide IB-5
Gene namesi
Name:PRB4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:9340. PRB4.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33702.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 310294Basic salivary proline-rich protein 4PRO_0000022102Add
BLAST
Peptidei17 – 3923Protein N1PRO_0000022103Add
BLAST
Chaini40 – 177138Glycosylated protein APRO_0000022104Add
BLAST
Chaini241 – 31070Peptide P-DPRO_0000022099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi87 – 871N-linked (GlcNAc...)1 Publication
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-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. Pyroglutamate formation found on at least Gln-46, Gln-48, Gln-67, Gln-88; Gln-90; Gln-193; Gln-288 Gln-214 and Gln-295, preferentially in diabetic, and head and neck cancer patients.1 Publication

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP10163.
PRIDEiP10163.

Expressioni

Gene expression databases

CleanExiHS_PRB4.
GenevestigatoriP10163.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000279575.

Structurei

3D structure databases

DisProtiDP00119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati35 – 55211Add
BLAST
Repeati56 – 76212Add
BLAST
Repeati77 – 97213Add
BLAST
Repeati98 – 118214Add
BLAST
Repeati119 – 139215Add
BLAST
Repeati140 – 160216Add
BLAST
Repeati161 – 181217Add
BLAST
Repeati182 – 202218Add
BLAST
Repeati203 – 223219Add
BLAST
Repeati224 – 2341110; truncatedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 2342009.5 X 21 AA tandem repeats of K-P-[EQ]-[GR]-[PR]-[PR]-P-Q-G-G-N-Q-[PS]-[QH]-[RG]-[PT]-P-P-[PH]-P-GAdd
BLAST

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

InParanoidiP10163.

Family and domain databases

InterProiIPR026086. Pro-rich.
[Graphical view]
PANTHERiPTHR23203. PTHR23203. 1 hit.
PfamiPF15240. Pro-rich. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10163-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLILLSVAL LALSSAESSS EDVSQEESLF LISGKPEGRR PQGGNQPQRP
60 70 80 90 100
PPPPGKPQGP PPQGGNQSQG PPPPPGKPEG RPPQGGNQSQ GPPPHPGKPE
110 120 130 140 150
RPPPQGGNQS QGPPPHPGKP ESRPPQGGHQ SQGPPPTPGK PEGPPPQGGN
160 170 180 190 200
QSQGTPPPPG KPEGRPPQGG NQSQGPPPHP GKPERPPPQG GNQSHRPPPP
210 220 230 240 250
PGKPERPPPQ GGNQSQGPPP HPGKPEGPPP QEGNKSRSAR SPPGKPQGPP
260 270 280 290 300
QQEGNKPQGP PPPGKPQGPP PAGGNPQQPQ APPAGKPQGP PPPPQGGRPP
310
RPAQGQQPPQ
Length:310
Mass (Da):31,326
Last modified:May 13, 2014 - v4
Checksum:i079538A1BC412D0F
GO

Sequence cautioni

The sequence CAA30543.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA30729.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281S → P AA sequence (PubMed:8373986).Curated
Sequence conflicti31 – 399LISGKPEGR → IIPPKPPG AA sequence (PubMed:8373986).Curated
Sequence conflicti31 – 333LIS → PPP in AAB50687 (PubMed:8554050).Curated
Sequence conflicti37 – 371E → Q in CAA30543 (PubMed:2851479).Curated
Sequence conflicti37 – 371E → Q in CAA30542 (PubMed:3220251).Curated
Sequence conflicti66 – 661N → D AA sequence (PubMed:8373986).Curated
Sequence conflicti74 – 9421Missing in CAA30542 (PubMed:3220251).CuratedAdd
BLAST
Sequence conflicti96 – 961P → PP AA sequence (PubMed:8373986).Curated
Sequence conflicti101 – 1011R → E AA sequence (PubMed:8373986).Curated
Sequence conflicti122 – 1232SR → RP in CAA30542 (PubMed:3220251).Curated
Sequence conflicti129 – 1291H → N in CAA30542 (PubMed:3220251).Curated
Sequence conflicti154 – 17421Missing in CAA30542 (PubMed:3220251).CuratedAdd
BLAST
Sequence conflicti169 – 1713GGN → QGG AA sequence (PubMed:8373986).Curated
Sequence conflicti192 – 1921N → D AA sequence (PubMed:8373986).Curated
Sequence conflicti213 – 2131N → D AA sequence (PubMed:8373986).Curated

Polymorphismi

The number of repeats is polymorphic and varies among different alleles. Allele S (short), allele M (medium) and allele L (long) contain 6, 7 and 9 tandem repeats respectively.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti113 – 15442Missing in allele M and allele S.
VAR_035034Add
BLAST
Natural varianti164 – 18421Missing in allele S.
VAR_035035Add
BLAST
Natural varianti185 – 1851R → G.
Corresponds to variant rs11054244 [ dbSNP | Ensembl ].
VAR_031548
Natural varianti186 – 1861P → R.
Corresponds to variant rs11054243 [ dbSNP | Ensembl ].
VAR_031549
Natural varianti200 – 2001P → H.
Corresponds to variant rs12308244 [ dbSNP | Ensembl ].
VAR_031550
Natural varianti272 – 2721A → P.3 Publications
Corresponds to variant rs1052808 [ dbSNP | Ensembl ].
VAR_031551

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03207 mRNA. Translation: AAA60188.1.
X07882 Genomic DNA. Translation: CAA30729.1. Sequence problems.
X07715 Genomic DNA. Translation: CAA30543.1. Sequence problems.
AC010176 Genomic DNA. No translation available.
BC130386 mRNA. Translation: AAI30387.1.
S80916 Genomic DNA. Translation: AAB50687.2.
X07704 Genomic DNA. Translation: CAA30542.1.
PIRiS03176. PIHUSD.
RefSeqiNP_001248328.1. NM_001261399.1.
NP_002714.2. NM_002723.4.
UniGeneiHs.528651.

Genome annotation databases

GeneIDi5545.
KEGGihsa:5545.

Polymorphism databases

DMDMi158517854.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03207 mRNA. Translation: AAA60188.1.
X07882 Genomic DNA. Translation: CAA30729.1. Sequence problems.
X07715 Genomic DNA. Translation: CAA30543.1. Sequence problems.
AC010176 Genomic DNA. No translation available.
BC130386 mRNA. Translation: AAI30387.1.
S80916 Genomic DNA. Translation: AAB50687.2.
X07704 Genomic DNA. Translation: CAA30542.1.
PIRiS03176. PIHUSD.
RefSeqiNP_001248328.1. NM_001261399.1.
NP_002714.2. NM_002723.4.
UniGeneiHs.528651.

3D structure databases

DisProtiDP00119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000279575.

Polymorphism databases

DMDMi158517854.

Proteomic databases

PaxDbiP10163.
PRIDEiP10163.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5545.
KEGGihsa:5545.

Organism-specific databases

CTDi5545.
GeneCardsiGC12M011460.
H-InvDBHIX0079490.
HGNCiHGNC:9340. PRB4.
MIMi180990. gene.
neXtProtiNX_P10163.
PharmGKBiPA33702.
GenAtlasiSearch...

Phylogenomic databases

InParanoidiP10163.

Miscellaneous databases

ChiTaRSiPRB4. human.
GeneWikiiPRB4.
GenomeRNAii5545.
NextBioi21484.
PROiP10163.
SOURCEiSearch...

Gene expression databases

CleanExiHS_PRB4.
GenevestigatoriP10163.

Family and domain databases

InterProiIPR026086. Pro-rich.
[Graphical view]
PANTHERiPTHR23203. PTHR23203. 1 hit.
PfamiPF15240. Pro-rich. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE S), POLYMORPHISM.
  2. "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(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES L AND S).
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE M), VARIANT PRO-272.
    Tissue: Cerebellum.
  5. "Alignment of amino acid and DNA sequences of human proline-rich proteins."
    Kauffman D.L., Keller P.J., Bennick A., Blum M.
    Crit. Rev. Oral Biol. Med. 4:287-292(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-112 AND 155-240.
    Tissue: Saliva.
  6. "PRB1, PRB2, and PRB4 coded polymorphisms among human salivary concanavalin-A binding, II-1, and Po proline-rich proteins."
    Azen E.A., Amberger E., Fisher S., Prakobphol A., Niece R.L.
    Am. J. Hum. Genet. 58:143-153(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-310 (ALLELE M), VARIANT PRO-272.
  7. "Many protein products from a few loci: assignment of human salivary proline-rich proteins to specific loci."
    Lyons K.M., Stein J.H., Smithies O.
    Genetics 120:255-265(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-310, VARIANT PRO-272.
  8. "Complete amino acid sequence of a basic proline-rich peptide, P-D, from human parotid saliva."
    Saitoh E., Isemura S., Sanada K.
    J. Biochem. 93:495-502(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 241-310.
    Tissue: Saliva.
  9. "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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 241-310.
    Tissue: Saliva.
  10. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-87, PYROGLUTAMATE FORMATION, VARIANTS ALLELE L AND M, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPRB4_HUMAN
AccessioniPrimary (citable) accession number: P10163
Secondary accession number(s): A1L439
, O00600, P02813, P10161, P10162, P81489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: May 13, 2014
Last modified: January 6, 2015
This is version 106 of the entry and version 4 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. 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

External Data

Dasty 3

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 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.