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Protein

Proline-rich protein 5-like

Gene

PRR5L

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

Functioni

Associates with the mTORC2 complex that regulates cellular processes including survival and organization of the cytoskeleton. Regulates the activity of the mTORC2 complex in a substrate-specific manner preventing for instance the specific phosphorylation of PKCs and thereby controlling cell migration.2 Publications

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • negative regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of signal transduction Source: UniProtKB-KW
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  • positive regulation of protein phosphorylation Source: Ensembl
  • regulation of fibroblast migration Source: UniProtKB
  • TORC2 signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-rich protein 5-like
Alternative name(s):
Protein observed with Rictor-2
Short name:
Protor-2
Gene namesi
Name:PRR5L
Synonyms:PROTOR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:25878. PRR5L.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: Ensembl
  • TORC2 complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165543593.

Polymorphism and mutation databases

BioMutaiPRR5L.
DMDMi296452872.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368Proline-rich protein 5-likePRO_0000332709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated. Ubiquitination by RFFL promotes proteasomal degradation of PRR5L thereby modifying the substrate-specific activity of the mTORC2 complex. Ubiquitination by RFFL is stimulated by LPA/lysophosphatidic acid.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6MZQ0.
MaxQBiQ6MZQ0.
PaxDbiQ6MZQ0.
PRIDEiQ6MZQ0.

PTM databases

iPTMnetiQ6MZQ0.
PhosphoSiteiQ6MZQ0.

Expressioni

Gene expression databases

BgeeiQ6MZQ0.
ExpressionAtlasiQ6MZQ0. baseline and differential.
GenevisibleiQ6MZQ0. HS.

Interactioni

Subunit structurei

Interacts with the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts with RFFL.2 Publications

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122983. 4 interactions.
IntActiQ6MZQ0. 4 interactions.
STRINGi9606.ENSP00000368144.

Structurei

3D structure databases

ProteinModelPortaliQ6MZQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PROTOR family.Curated

Phylogenomic databases

eggNOGiENOG410IJB2. Eukaryota.
ENOG410ZWNQ. LUCA.
GeneTreeiENSGT00530000063981.
HOGENOMiHOG000290687.
HOVERGENiHBG067971.
InParanoidiQ6MZQ0.
OMAiELNCASL.
OrthoDBiEOG771278.
PhylomeDBiQ6MZQ0.
TreeFamiTF314826.

Family and domain databases

InterProiIPR013745. Bit61/PRR5.
[Graphical view]
PfamiPF08539. HbrB. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6MZQ0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTRGFAPILP VEFHKMGSFR RPRPRFMSSP VLSDLPRFQA ARQALQLSSS
60 70 80 90 100
SAWNSVQTAV INVFKGGGLQ SNELYALNEN IRRLLKSELG SFITDYFQNQ
110 120 130 140 150
LLAKGLFFVE EKIKLCEGEN RIEVLAEVWD HFFTETLPTL QAIFYPVQGQ
160 170 180 190 200
ELTIRQISLL GFRDLVLLKV KLGDLLLLAQ SKLPSSIVQM LLILQSVHEP
210 220 230 240 250
TGPSESYLQL EELVKQVVSP FLGISGDRSF SGPTYTLARR HSRVRPKVTV
260 270 280 290 300
LNYASPITAV SRPLNEMVLT PLTEQEGEAY LEKCGSVRRH TVANAHSDIQ
310 320 330 340 350
LLAMATMMHS GLGEEASSEN KCLLLPPSFP PPHRQCSSEP NITDNPDGLE
360
EGARGSQEGS ELNCASLS
Length:368
Mass (Da):40,836
Last modified:May 18, 2010 - v2
Checksum:iE54122E27B9CDC68
GO
Isoform 2 (identifier: Q6MZQ0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-229: Missing.
     230-237: FSGPTYTL → MPVFSRAP

Note: No experimental confirmation available.
Show »
Length:139
Mass (Da):15,064
Checksum:i3AE661E4DC50D023
GO
Isoform 3 (identifier: Q6MZQ0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     82-82: R → M
     149-195: Missing.

Note: No experimental confirmation available.
Show »
Length:240
Mass (Da):26,594
Checksum:i396993B58B77CE51
GO
Isoform 4 (identifier: Q6MZQ0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     196-205: SVHEPTGPSE → PGGTPGSGPR
     206-368: Missing.

Note: No experimental confirmation available.
Show »
Length:205
Mass (Da):23,005
Checksum:i66E23134F4421F18
GO

Sequence cautioni

The sequence AAI25123.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681S → T in AAI25123 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411A → T.2 Publications
Corresponds to variant rs330261 [ dbSNP | Ensembl ].
VAR_043006
Natural varianti330 – 3301P → S.
Corresponds to variant rs11033639 [ dbSNP | Ensembl ].
VAR_043007

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 229229Missing in isoform 2. 1 PublicationVSP_033375Add
BLAST
Alternative sequencei1 – 8181Missing in isoform 3. 1 PublicationVSP_033376Add
BLAST
Alternative sequencei82 – 821R → M in isoform 3. 1 PublicationVSP_033377
Alternative sequencei149 – 19547Missing in isoform 3. 1 PublicationVSP_033378Add
BLAST
Alternative sequencei196 – 20510SVHEPTGPSE → PGGTPGSGPR in isoform 4. 1 PublicationVSP_044981
Alternative sequencei206 – 368163Missing in isoform 4. 1 PublicationVSP_044982Add
BLAST
Alternative sequencei230 – 2378FSGPTYTL → MPVFSRAP in isoform 2. 1 PublicationVSP_033379

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024275 mRNA. Translation: BAB14870.1.
DR001466 mRNA. No translation available.
BX640959 mRNA. Translation: CAE45978.1.
AC009656 Genomic DNA. No translation available.
AC087277 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68124.1.
BC008922 mRNA. Translation: AAH08922.1.
BC125122 mRNA. Translation: AAI25123.1. Different initiation.
CCDSiCCDS31463.1. [Q6MZQ0-1]
CCDS53617.1. [Q6MZQ0-4]
RefSeqiNP_001153639.1. NM_001160167.1. [Q6MZQ0-1]
NP_001153640.1. NM_001160168.1. [Q6MZQ0-3]
NP_001153641.1. NM_001160169.1. [Q6MZQ0-4]
NP_079117.3. NM_024841.4. [Q6MZQ0-1]
UniGeneiHs.19987.

Genome annotation databases

EnsembliENST00000378867; ENSP00000368144; ENSG00000135362. [Q6MZQ0-1]
ENST00000527487; ENSP00000435241; ENSG00000135362. [Q6MZQ0-4]
ENST00000530639; ENSP00000435050; ENSG00000135362. [Q6MZQ0-1]
GeneIDi79899.
KEGGihsa:79899.
UCSCiuc001mwo.5. human. [Q6MZQ0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024275 mRNA. Translation: BAB14870.1.
DR001466 mRNA. No translation available.
BX640959 mRNA. Translation: CAE45978.1.
AC009656 Genomic DNA. No translation available.
AC087277 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68124.1.
BC008922 mRNA. Translation: AAH08922.1.
BC125122 mRNA. Translation: AAI25123.1. Different initiation.
CCDSiCCDS31463.1. [Q6MZQ0-1]
CCDS53617.1. [Q6MZQ0-4]
RefSeqiNP_001153639.1. NM_001160167.1. [Q6MZQ0-1]
NP_001153640.1. NM_001160168.1. [Q6MZQ0-3]
NP_001153641.1. NM_001160169.1. [Q6MZQ0-4]
NP_079117.3. NM_024841.4. [Q6MZQ0-1]
UniGeneiHs.19987.

3D structure databases

ProteinModelPortaliQ6MZQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122983. 4 interactions.
IntActiQ6MZQ0. 4 interactions.
STRINGi9606.ENSP00000368144.

PTM databases

iPTMnetiQ6MZQ0.
PhosphoSiteiQ6MZQ0.

Polymorphism and mutation databases

BioMutaiPRR5L.
DMDMi296452872.

Proteomic databases

EPDiQ6MZQ0.
MaxQBiQ6MZQ0.
PaxDbiQ6MZQ0.
PRIDEiQ6MZQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378867; ENSP00000368144; ENSG00000135362. [Q6MZQ0-1]
ENST00000527487; ENSP00000435241; ENSG00000135362. [Q6MZQ0-4]
ENST00000530639; ENSP00000435050; ENSG00000135362. [Q6MZQ0-1]
GeneIDi79899.
KEGGihsa:79899.
UCSCiuc001mwo.5. human. [Q6MZQ0-1]

Organism-specific databases

CTDi79899.
GeneCardsiPRR5L.
H-InvDBHIX0171373.
HGNCiHGNC:25878. PRR5L.
MIMi611728. gene.
neXtProtiNX_Q6MZQ0.
PharmGKBiPA165543593.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJB2. Eukaryota.
ENOG410ZWNQ. LUCA.
GeneTreeiENSGT00530000063981.
HOGENOMiHOG000290687.
HOVERGENiHBG067971.
InParanoidiQ6MZQ0.
OMAiELNCASL.
OrthoDBiEOG771278.
PhylomeDBiQ6MZQ0.
TreeFamiTF314826.

Miscellaneous databases

GenomeRNAii79899.
PROiQ6MZQ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6MZQ0.
ExpressionAtlasiQ6MZQ0. baseline and differential.
GenevisibleiQ6MZQ0. HS.

Family and domain databases

InterProiIPR013745. Bit61/PRR5.
[Graphical view]
PfamiPF08539. HbrB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  2. "High-throughput cloning of full-length human cDNAs directly from cDNA libraries optimized for large and rare transcripts."
    Birkett C., Cho J., Gau Y., Hamer R., Kelly S., Kovacs K., Liu L., Liu X., Porter J., Sachs A., Shu Y., Sun Z., Wong J., Wu M., Zhang X., Jay G., He W.
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT THR-41.
    Tissue: Fetal brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-41.
    Tissue: Uterus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 2).
    Tissue: Uterus.
  7. Cited for: IDENTIFICATION, FUNCTION, SUBUNIT.
  8. "PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and cell migration downstream of Galpha12."
    Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D., Offermanns S., Simon M.I., Wu D.
    Nat. Cell Biol. 14:686-696(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MTORC2 SIGNALING, INTERACTION WITH MTORC2 COMPLEX AND RFFL, UBIQUITINATION BY RFFL.

Entry informationi

Entry nameiPRR5L_HUMAN
AccessioniPrimary (citable) accession number: Q6MZQ0
Secondary accession number(s): A4QN22
, E9PKY1, Q96H46, Q9H7V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 86 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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.