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Basic salivary proline-rich protein 2 (Salivary proline-rich protein) (Con1 glycoprotein) [Cleaved into: Basic proline-rich peptide IB-1; Basic proline-rich peptide P-E (IB-9); Basic proline-rich peptide IB-7; Basic proline-rich peptide IB-8c (Basic peptide P-F); Basic proline-rich peptide IB-4]

 PRB2_HUMAN              Reviewed;         416 AA.
P02812; O00599; P02811; P04281;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 3.
13-FEB-2019, entry version 133.
RecName: Full=Basic salivary proline-rich protein 2;
Short=Salivary proline-rich protein;
AltName: Full=Con1 glycoprotein;
Contains:
RecName: Full=Basic proline-rich peptide IB-1;
Contains:
RecName: Full=Basic proline-rich peptide P-E;
AltName: Full=IB-9;
Contains:
RecName: Full=Basic proline-rich peptide IB-7;
Contains:
RecName: Full=Basic proline-rich peptide IB-8c;
AltName: Full=Basic peptide P-F;
Contains:
RecName: Full=Basic proline-rich peptide IB-4;
Flags: Precursor;
Name=PRB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-274.
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-156.
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
PROTEIN SEQUENCE OF 17-112, PYROGLUTAMATE FORMATION AT GLN-17, AND
PHOSPHORYLATION AT SER-24.
TISSUE=Saliva;
PubMed=3521730; DOI=10.1021/bi00357a013;
Kauffman D., Hofmann T., Bennick A., Keller P.;
"Basic proline-rich proteins from human parotid saliva: complete
covalent structures of proteins IB-1 and IB-6.";
Biochemistry 25:2387-2392(1986).
[4]
PROTEIN SEQUENCE OF 52-112.
TISSUE=Saliva;
PubMed=6924859; DOI=10.1021/bi00268a036;
Kauffman D., Wong R., Bennick A., Keller P.;
"Basic proline-rich proteins from human parotid saliva: complete
covalent structure of protein IB-9 and partial structure of protein
IB-6, members of a polymorphic pair.";
Biochemistry 21:6558-6562(1982).
[5]
PROTEIN SEQUENCE OF 52-112.
TISSUE=Saliva;
PubMed=7118863; DOI=10.1093/oxfordjournals.jbchem.a133900;
Isemura S., Saitoh E., Sanada K.;
"Fractionation and characterization of basic proline-rich peptides of
human parotid saliva and the amino acid sequence of proline-rich
peptide P-E.";
J. Biochem. 91:2067-2075(1982).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-416, PROTEIN SEQUENCE OF
175-235, GLYCOSYLATION, AND VARIANT CON1- PRO-274.
PubMed=8554050;
Azen E.A., Amberger E., Fisher S., Prakobphol A., Niece R.L.;
"PRB1, PRB2, and PRB4 coded polymorphisms among human salivary
concanavalin-A binding, II-1, and Po proline-rich proteins.";
Am. J. Hum. Genet. 58:143-153(1996).
[7]
PROTEIN SEQUENCE OF 113-171; 299-359 AND 361-416.
TISSUE=Saliva;
PubMed=1849422; DOI=10.1021/bi00228a001;
Kauffman D.L., Bennick A., Blum M., Keller P.J.;
"Basic proline-rich proteins from human parotid saliva: relationships
of the covalent structures of ten proteins from a single individual.";
Biochemistry 30:3351-3356(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 166-416.
PubMed=2993301;
Maeda N., Kim H.-S., Azen E.A., Smithies O.;
"Differential RNA splicing and post-translational cleavages in the
human salivary proline-rich protein gene system.";
J. Biol. Chem. 260:11123-11130(1985).
[9]
PROTEIN SEQUENCE OF 299-359.
TISSUE=Saliva;
PubMed=6874669; DOI=10.1093/jb/93.3.883;
Saitoh E., Isemura S., Sanada K.;
"Complete amino acid sequence of a basic proline-rich peptide, P-F,
from human parotid saliva.";
J. Biochem. 93:883-888(1983).
[10]
POLYMORPHISM.
PubMed=2851479;
Lyons K.M., Stein J.H., Smithies O.;
"Length polymorphisms in human proline-rich protein genes generated by
intragenic unequal crossing over.";
Genetics 120:267-278(1988).
[11]
PROTEOLYTIC PROCESSING, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18463091; DOI=10.1074/jbc.M708282200;
Helmerhorst E.J., Sun X., Salih E., Oppenheim F.G.;
"Identification of Lys-Pro-Gln as a novel cleavage site specificity of
saliva-associated proteases.";
J. Biol. Chem. 283:19957-19966(2008).
[12]
GLYCOSYLATION AT ASN-230; SER-232 AND ASN-272, PHOSPHORYLATION AT
SER-52, PYROGLUTAMATE FORMATION AT GLN-17, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20879038; DOI=10.1002/pmic.201000261;
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.;
"Finding new posttranslational modifications in salivary proline-rich
proteins.";
Proteomics 10:3732-3742(2010).
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- PTM: N- and O-glycosylated. In head and neck cancer patients, O-
glycosylated with glucosylgalactosyl carbohydrate moiety. This
modification would require prior hydroxylation on the lysine
residue. {ECO:0000269|PubMed:20879038,
ECO:0000269|PubMed:8554050}.
-!- PTM: Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where
Xaa in the P(3) position is mostly lysine. The endoprotease may be
of microbial origin. {ECO:0000269|PubMed:18463091}.
-!- PTM: Pyroglutamate formation occurs on terminal Gln residues of
cleaved peptides. Pyroglutamate formation found on at least Gln-
398 and Gln-400. {ECO:0000269|PubMed:18463091}.
-!- POLYMORPHISM: The number of repeats is polymorphic and varies
among different alleles (PubMed:2851479).
{ECO:0000269|PubMed:2851479}.
-!- MISCELLANEOUS: Peptides IB-9 and P-E are the same peptide.
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EMBL; AC078950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX484538; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S80905; AAB50686.1; -; Genomic_DNA.
EMBL; K03208; AAA60189.1; -; mRNA.
CCDS; CCDS41757.2; -.
PIR; B40750; PIHUB6.
PIR; E25372; PIHUPF.
UniGene; Hs.654486; -.
IntAct; P02812; 2.
STRING; 9606.ENSP00000374013; -.
iPTMnet; P02812; -.
PhosphoSitePlus; P02812; -.
BioMuta; PRB2; -.
DMDM; 160409933; -.
jPOST; P02812; -.
PaxDb; P02812; -.
PeptideAtlas; P02812; -.
PRIDE; P02812; -.
ProteomicsDB; 51604; -.
TopDownProteomics; P02812; -.
Ensembl; ENST00000389362; ENSP00000374013; ENSG00000121335.
UCSC; uc010shk.2; human.
DisGeNET; 653247; -.
EuPathDB; HostDB:ENSG00000121335.11; -.
GeneCards; PRB2; -.
HGNC; HGNC:9338; PRB2.
MIM; 168810; gene.
neXtProt; NX_P02812; -.
eggNOG; ENOG410KCD2; Eukaryota.
eggNOG; ENOG4110P3B; LUCA.
InParanoid; P02812; -.
ChiTaRS; PRB2; human.
PRO; PR:P02812; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000121335; Expressed in 71 organ(s), highest expression level in temporal lobe.
ExpressionAtlas; P02812; baseline and differential.
Genevisible; P02812; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
InterPro; IPR026086; Pro-rich.
PANTHER; PTHR23203; PTHR23203; 7.
Pfam; PF15240; Pro-rich; 6.
SMART; SM01412; Pro-rich; 2.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Glycoprotein;
Phosphoprotein; Polymorphism; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 416 Basic salivary proline-rich protein 2.
/FTId=PRO_0000022095.
CHAIN 17 112 Basic proline-rich peptide IB-1.
/FTId=PRO_0000097038.
CHAIN 52 112 Basic proline-rich peptide P-E.
/FTId=PRO_0000395485.
CHAIN 113 171 Basic proline-rich peptide IB-7.
/FTId=PRO_0000372439.
CHAIN 299 359 Basic proline-rich peptide IB-8c.
/FTId=PRO_0000022096.
CHAIN 361 416 Basic proline-rich peptide IB-4.
/FTId=PRO_0000372440.
REPEAT 53 72 1.
REPEAT 74 93 2.
REPEAT 94 113 3.
REPEAT 114 133 4.
REPEAT 135 154 5.
REPEAT 155 174 6.
REPEAT 176 195 7.
REPEAT 197 216 8.
REPEAT 217 236 9.
REPEAT 238 257 10.
REPEAT 259 278 11.
REPEAT 279 298 12.
REPEAT 300 319 13.
REPEAT 321 340 14.
REPEAT 341 360 15.
REGION 53 360 15 X 20 AA approximate tandem repeats of
P-P-G-K-P-Q-G-P-P-P-Q-G-[GD]-[NKS]-[KSQ]-
[PRS]-[QRS] [GPS]-[PSAR]-[PSR].
MOD_RES 17 17 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20879038,
ECO:0000269|PubMed:3521730}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000269|PubMed:3521730}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000269|PubMed:20879038}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20879038}.
CARBOHYD 232 232 O-linked (Hex) serine.
{ECO:0000269|PubMed:20879038}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20879038}.
VARIANT 233 233 Q -> R (in dbSNP:rs34305575).
/FTId=VAR_061693.
VARIANT 274 274 S -> P (may abrogate glycosylation at N-
272; dbSNP:rs10845349).
{ECO:0000269|PubMed:16541075,
ECO:0000269|PubMed:8554050}.
/FTId=VAR_019695.
CONFLICT 68 68 P -> S (in Ref. 2; BX484538).
{ECO:0000305}.
CONFLICT 88 88 K -> R (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 151 151 Q -> P (in Ref. 2; BX484538).
{ECO:0000305}.
CONFLICT 271 271 G -> D (in Ref. 8; AAA60189).
{ECO:0000305}.
SEQUENCE 416 AA; 40799 MW; 5CF67F42B368A622 CRC64;
MLLILLSVAL LALSSAQNLN EDVSQEESPS LIAGNPQGAP PQGGNKPQGP PSPPGKPQGP
PPQGGNQPQG PPPPPGKPQG PPPQGGNKPQ GPPPPGKPQG PPPQGDKSRS PRSPPGKPQG
PPPQGGNQPQ GPPPPPGKPQ GPPPQGGNKP QGPPPPGKPQ GPPPQGDNKS RSSRSPPGKP
QGPPPQGGNQ PQGPPPPPGK PQGPPPQGGN KPQGPPPPGK PQGPPPQGDN KSQSARSPPG
KPQGPPPQGG NQPQGPPPPP GKPQGPPPQG GNKSQGPPPP GKPQGPPPQG GSKSRSSRSP
PGKPQGPPPQ GGNQPQGPPP PPGKPQGPPP QGGNKPQGPP PPGKPQGPPP QGGSKSRSAR
SPPGKPQGPP QQEGNNPQGP PPPAGGNPQQ PQAPPAGQPQ GPPRPPQGGR PSRPPQ


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Pathways :
WP1621: Arginine and proline metabolism
WP1001: Peptide GPCRs
WP1117: Peptide GPCRs
WP131: Peptide GPCRs
WP1338: Peptide GPCRs
WP234: Peptide GPCRs
WP24: Peptide GPCRs
WP771: Peptide GPCRs
WP883: Peptide GPCRs
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism

Related Genes :
[PRH1; PRH2] Salivary acidic proline-rich phosphoprotein 1/2 (Db-s) (PRP-1/PRP-2) (Parotid acidic protein) (Pa) (Parotid double-band protein) (Parotid isoelectric focusing variant protein) (PIF-S) (Parotid proline-rich protein 1/2) (Pr1/Pr2) (Protein C) [Cleaved into: Salivary acidic proline-rich phosphoprotein 1/2; Salivary acidic proline-rich phosphoprotein 3/4 (Db-F) (PIF-F) (PRP-3/PRP-4) (Protein A); Peptide P-C]
[] Bradykinin-potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide 6a (BPP-6a); Bradykinin-potentiating peptide 10a (BPP-10a) (Bradykinin-potentiating peptide IV-1-A) (BPPIV-1-A) (Bradykinin-potentiating peptide V-8); Bradykinin-potentiating peptide 13a+QQWA (BPP-13a+QQWA); Bradykinin-potentiating peptide 13a+QWA (BPP-13a+QWA); Bradykinin-potentiating peptide 13a (BPP-13a) (Bradykinin-potentiating peptide III-1-A) (III-1-A) (Bradykinin-potentiating peptide V-9); Bradykinin-potentiating peptide 10c+QQWA (BPP-10c+QQWA); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Bradykinin-potentiating peptide IV-1-Bbeta) (BPP IV-1-Bbeta) (Bradykinin-potentiating peptide V-7); Bradykinin-potentiating peptide 10c-F (BPP-10c-F); Bradykinin-potentiating peptide 11b (BPP-11b) (Bradykinin-potentiating peptide IIa) (BPP-IIa); Bradykinin-potentiating peptide IIb (BPP-IIb); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide Va) (BPPVa) (Proline-rich peptide 5a) (Bj-PRO-5a) (PRO-5a); Poly-His-poly-Gly peptide 1 (pHpG-1); C-type natriuretic peptide (Bj-CNP)]
[] Bradykinin-potentiating and C-type natriuretic peptides (Angiotensin-converting enzyme inhibitor) (BPP-CNP homolog) [Cleaved into: Bradykinin-potentiating peptide 13a (BPP-13a) (Bradykinin-potentiating peptide S3,1); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Bradykinin-potentiating peptide S4,3,1); Bradykinin-potentiating peptide 12b (BPP-12b) (Bradykinin-potentiating peptide S4,3,2); Bradykinin-potentiating peptide 11e (BPP-11e); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide S5,2) (Bradykinin-potentiating peptide Va) (BPPVa) (Proline-rich peptide 5a) (PRO-5a); C-type natriuretic peptide (CNP)]
[] Bradykinin-potentiating and C-type natriuretic peptides (Brain BPP-CNP) (bBPP-CNP) (Evasin-CNP) [Cleaved into: Bradykinin-potentiating peptide 13a+QQWA (BPP-13a+QQWA); Bradykinin-potentiating peptide 13a+QWA (BPP-13a+QWA); Bradykinin-potentiating peptide 13a (BPP-13a); Bradykinin-potentiating peptide 10c+QQWA (BPP-10c+QQWA); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Evasin-10c); Bradykinin-potentiating peptide 12b (BPP-12b) (Evasin-12b); Bradykinin-potentiating peptide AP; Bradykinin-potentiating peptide APL (BPP-APL); Bradykinin-potentiating peptide 11e (BPP-11e) (Evasin-11e); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide Va) (BPPVa) (Evasin-5a) (Proline-rich peptide 5a) (Bj-PRO-5a) (PRO-5a); Poly-His-poly-Gly peptide 1 (pHpG-1); C-type natriuretic peptide (Bj-CNP)]
[HRG] Histidine-rich glycoprotein (Histidine-proline-rich glycoprotein) (HPRG)
[SMR3B PBII PRL3 PROL3] Submaxillary gland androgen-regulated protein 3B (Proline-rich peptide P-B) (Proline-rich protein 3) [Cleaved into: Peptide P-A; Peptide D1A]
[PTK2B FAK2 PYK2 RAFTK] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Hrg Hrg1] Histidine-rich glycoprotein (Histidine-proline-rich glycoprotein) (HPRG) (Histidine-rich glycoprotein 1) (HRG1)
[Ptk2b Fak2 Pyk2 Raftk] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)
[Hrg] Histidine-rich glycoprotein (Histidine-proline-rich glycoprotein) (HPRG)
[AKT1S1 PRAS40] Proline-rich AKT1 substrate 1 (40 kDa proline-rich AKT substrate)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[PPBP CTAP3 CXCL7 SCYB7 TGB1 THBGB1] Platelet basic protein (PBP) (C-X-C motif chemokine 7) (Leukocyte-derived growth factor) (LDGF) (Macrophage-derived growth factor) (MDGF) (Small-inducible cytokine B7) [Cleaved into: Connective tissue-activating peptide III (CTAP-III) (LA-PF4) (Low-affinity platelet factor IV); TC-2; Connective tissue-activating peptide III(1-81) (CTAP-III(1-81)); Beta-thromboglobulin (Beta-TG); Neutrophil-activating peptide 2(74) (NAP-2(74)); Neutrophil-activating peptide 2(73) (NAP-2(73)); Neutrophil-activating peptide 2 (NAP-2); TC-1; Neutrophil-activating peptide 2(1-66) (NAP-2(1-66)); Neutrophil-activating peptide 2(1-63) (NAP-2(1-63))]
[CARMIL2 LRRC16C RLTPR] Capping protein, Arp2/3 and myosin-I linker protein 2 (Capping protein regulator and myosin 1 linker 2) (F-actin-uncapping protein RLTPR) (Leucine-rich repeat-containing protein 16C) (RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein)
[EPRS GLNS PARS QARS QPRS PIG32] Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[MAP3K11 MLK3 PTK1 SPRK] Mitogen-activated protein kinase kinase kinase 11 (EC 2.7.11.25) (Mixed lineage kinase 3) (Src-homology 3 domain-containing proline-rich kinase)
[Enah Mena Ndpp1] Protein enabled homolog (NPC-derived proline-rich protein 1) (NDPP-1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Eprs Qprs] Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)]
[LRRC8C AD158 FAD158] Volume-regulated anion channel subunit LRRC8C (Factor for adipocyte differentiation 158) (Leucine-rich repeat-containing protein 8C)
[Lrrc8c Ad158 Fad158] Volume-regulated anion channel subunit LRRC8C (Factor for adipocyte differentiation 158) (Leucine-rich repeat-containing protein 8C)
[PRODH PIG6 POX2 PRODH2] Proline dehydrogenase 1, mitochondrial (EC 1.5.5.2) (Proline oxidase) (Proline oxidase 2) (p53-induced gene 6 protein)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[BAG6 BAT3 G3] Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6) (BCL2-associated athanogene 6) (BAG-6) (HLA-B-associated transcript 3) (Protein G3) (Protein Scythe)
[egl-9 F22E12.4] Hypoxia-inducible factor prolyl hydroxylase (HIF-PH) (EC 1.14.11.29) (Egg-laying defective protein 9) (Hypoxia-inducible factor-proline dioxygenase)
[PELP1 HMX3 MNAR] Proline-, glutamic acid- and leucine-rich protein 1 (Modulator of non-genomic activity of estrogen receptor) (Transcription factor HMX3)

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