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Q96NA2 (RILP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rab-interacting lysosomal protein
Gene names
Name:RILP
ORF Names:PP10141
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes. Ref.1 Ref.7 Ref.9 Ref.10

Subunit structure

Homodimer. Each subunit can interact with either RAB7A or RAB34. Interacts with CLN3. Ref.1 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14

Subcellular location

Endomembrane system. Late endosome membrane. Lysosome membrane. Cytoplasmic vesiclephagosome membrane. Note: Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7A is necessary for its recruitment to phagosomes. Ref.1 Ref.9 Ref.10

Tissue specificity

Ubiquitous. Strongly expressed in fetal heart, heart, stomach, spleen, adrenal gland, thyroid gland, salivary gland, fetal liver, liver and lung. Poorly expressed in brain. Ref.1 Ref.6 Ref.10

Sequence similarities

Contains 1 RILP-like domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96NA2-1)

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.
Isoform 2 (identifier: Q96NA2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-210: Missing.
     211-213: WAT → MGA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Rab-interacting lysosomal protein
PRO_0000097339

Regions

Domain236 – 27035RILP-like
Region272 – 33362Necessary for the interaction with RAB7A and RAB34, lysosomal distribution and morphology
Coiled coil75 – 181107 Potential

Amino acid modifications

Modified residue3141Phosphoserine Ref.12
Modified residue3151Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 210210Missing in isoform 2.
VSP_016043
Alternative sequence211 – 2133WAT → MGA in isoform 2.
VSP_016044
Natural variant811A → T. Ref.2
Corresponds to variant rs9909321 [ dbSNP | Ensembl ].
VAR_051321
Natural variant2811R → Q.
Corresponds to variant rs34982553 [ dbSNP | Ensembl ].
VAR_034417

Experimental info

Mutagenesis2481F → A: Strongly reduces dimerization and localization to late endosomal/lysosomal compartments. Ref.14
Mutagenesis2511I → A: Abolishes dimerization, interaction with RAB7A and localization to late endosomal/lysosomal compartments. Ref.14
Mutagenesis2521L → A: Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments. Ref.14
Mutagenesis2551R → A: Abolishes dimerization, interaction with RAB7A and localization to late endosomal/lysosomal compartments. Ref.14
Mutagenesis2581L → A: Reduces dimerization, interaction with RAB7A and localization to late endosomal/lysosomal compartments. Ref.14
Mutagenesis3041K → A: Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments. Ref.14
Mutagenesis3051M → A: Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments. Ref.14
Mutagenesis3061L → A: Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments. Ref.14
Sequence conflict2841G → S in CAC33443. Ref.1

Secondary structure

..... 401
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1057A1DAC2FFED94

FASTA40144,200
        10         20         30         40         50         60 
MEPRRAAPGV PGWGSREAAG SASAAELVYH LAGALGTELQ DLARRFGPEA AAGLVPLVVR 

        70         80         90        100        110        120 
ALELLEQAAV GPAPDSLQVS AQPAEQELRR LREENERLRR ELRAGPQEER ALLRQLKEVT 

       130        140        150        160        170        180 
DRQRDELRAH NRDLRQRGQE TEALQEQLQR LLLVNAELRH KLAAMQTQLR AAQDRERERQ 

       190        200        210        220        230        240 
QPGEAATPQA KERARGQAGR PGHQHGQEPE WATAGAGAPG NPEDPAEAAQ QLGRPSEAGQ 

       250        260        270        280        290        300 
CRFSREEFEQ ILQERNELKA KVFLLKEELA YFQRELLTDH RVPGLLLEAM KVAVRKQRKK 

       310        320        330        340        350        360 
IKAKMLGTPE EAESSEDEAG PWILLSDDKG DHPPPPESKI QSFFGLWYRG KAESSEDETS 

       370        380        390        400 
SPAPSKLGGE EEAQPQSPAP DPPCSALHEH LCLGASAAPE A 

« Hide

Isoform 2 [UniParc].

Checksum: 76673702E0FF4FFD
Show »

FASTA19120,726

References

« Hide 'large scale' references
[1]"Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes."
Cantalupo G., Alifano P., Roberti V., Bruni C.B., Bucci C.
EMBO J. 20:683-693(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN LATE ENDOCYTOSIS, INTERACTION WITH RAB7A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[2]"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. expand/collapse author list , 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 1), VARIANT THR-81.
Tissue: Kidney and Thalamus.
[3]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"Study of 100 skeletal muscle full length mRNA (Telethon project B41)."
Frigimelica E., Lanfranchi G.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skeletal muscle.
[5]"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 1).
Tissue: Brain, Lung, Testis and Uterus.
[6]"Expression analysis and chromosomal assignment of PRA1 and RILP genes."
Bucci C., De Gregorio L., Bruni C.B.
Biochem. Biophys. Res. Commun. 286:815-819(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors."
Jordens I., Fernandez-Borja M., Marsman M., Dusseljee S., Janssen L., Calafat J., Janssen H., Wubbolts R., Neefjes J.
Curr. Biol. 11:1680-1685(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DYNEIN-DYNACTIN COMPLEX RECRUITMENT.
[8]"Interorganellar regulation of lysosome positioning by the Golgi apparatus through Rab34 interaction with Rab-interacting lysosomal protein."
Wang T., Hong W.
Mol. Biol. Cell 13:4317-4332(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB34.
[9]"Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP."
Harrison R.E., Bucci C., Vieira O.V., Schroer T.A., Grinstein S.
Mol. Cell. Biol. 23:6494-6506(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHAGOSOME MIGRATION AND PHAGOLYSOSOMAL FUSION, SUBCELLULAR LOCATION.
[10]"A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34."
Wang T., Wong K.K., Hong W.
Mol. Biol. Cell 15:815-826(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LYSOSOMAL MORPHOLOGY AND DISTRIBUTION, INTERACTION WITH RAB7A AND RAB34, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]"The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is capable of self-interaction."
Colucci A.M.R., Campana M.C., Bellopede M., Bucci C.
Biochem. Biophys. Res. Commun. 334:128-133(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments."
Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K., Neefjes J., Olkkonen V.M., Jalanko A.
Cell. Mol. Life Sci. 69:2075-2089(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLN3.
[14]"Structural basis for recruitment of RILP by small GTPase Rab7."
Wu M., Wang T., Loh E., Hong W., Song H.
EMBO J. 24:1491-1501(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 244-308 IN COMPLEX WITH RAB7A, SUBUNIT, MUTAGENESIS OF PHE-248; ILE-251; LEU-252; ARG-255; LEU-258; LYS-304; MET-305 AND LEU-306.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ404317 mRNA. Translation: CAC33443.1.
AK055755 mRNA. Translation: BAB71003.1.
AK314767 mRNA. Translation: BAG37305.1.
AF370391 mRNA. Translation: AAQ15227.1.
AJ278711 mRNA. Translation: CAC82174.1.
BC004961 mRNA. Translation: AAH04961.1.
BC031621 mRNA. Translation: AAH31621.1.
RefSeqNP_113618.2. NM_031430.2.
UniGeneHs.534497.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YHNX-ray3.00B244-308[»]
ProteinModelPortalQ96NA2.
SMRQ96NA2. Positions 23-99, 244-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123679. 6 interactions.
IntActQ96NA2. 3 interactions.
STRING9606.ENSP00000301336.

PTM databases

PhosphoSiteQ96NA2.

Polymorphism databases

DMDM74732524.

Proteomic databases

PaxDbQ96NA2.
PRIDEQ96NA2.

Protocols and materials databases

DNASU83547.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301336; ENSP00000301336; ENSG00000167705. [Q96NA2-1]
GeneID83547.
KEGGhsa:83547.
UCSCuc002ftd.3. human. [Q96NA2-1]

Organism-specific databases

CTD83547.
GeneCardsGC17M001549.
HGNCHGNC:30266. RILP.
HPAHPA052041.
MIM607848. gene.
neXtProtNX_Q96NA2.
PharmGKBPA134915969.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG28812.
HOGENOMHOG000007529.
HOVERGENHBG082629.
InParanoidQ96NA2.
KOK13883.
OMAFEQILQE.
PhylomeDBQ96NA2.
TreeFamTF313489.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ96NA2.
BgeeQ96NA2.
CleanExHS_RILP.
GenevestigatorQ96NA2.

Family and domain databases

InterProIPR019143. JNK/Rab-associated_protein-1_N.
IPR021563. RILP.
[Graphical view]
PfamPF09744. Jnk-SapK_ap_N. 1 hit.
PF11461. RILP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96NA2.
GeneWikiRILP_(gene).
GenomeRNAi83547.
NextBio72481.
PROQ96NA2.
SOURCESearch...

Entry information

Entry nameRILP_HUMAN
AccessionPrimary (citable) accession number: Q96NA2
Secondary accession number(s): B2RBQ8 expand/collapse secondary AC list , Q71RE6, Q9BSL3, Q9BYS3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM