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Protein

RILP-like protein 1

Gene

RILPL1

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

Functioni

Plays a role in the regulation of cell shape and polarity. Plays a role in cellular protein transport, including protein transport away from primary cilia. Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus. Competes with SIAH1 for binding GAPDH (By similarity). Does not regulate lysosomal morphology and distribution.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
RILP-like protein 1
Alternative name(s):
Rab-interacting lysosomal-like protein 1
Gene namesi
Name:RILPL1
Synonyms:RLP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:26814. RILPL1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162401302.

Polymorphism and mutation databases

BioMutaiRILPL1.
DMDMi74736071.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403RILP-like protein 1PRO_0000299310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71PhosphoserineBy similarity
Modified residuei47 – 471S-nitrosocysteineBy similarity
Modified residuei259 – 2591PhosphoserineBy similarity

Post-translational modificationi

S-nitrosylation is required for the interaction with GAPDH.By similarity

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiQ5EBL4.
MaxQBiQ5EBL4.
PaxDbiQ5EBL4.
PRIDEiQ5EBL4.

PTM databases

iPTMnetiQ5EBL4.
PhosphoSiteiQ5EBL4.

Expressioni

Tissue specificityi

Widely expressed. Expressed at lower level in liver and kidney.1 Publication

Gene expression databases

BgeeiQ5EBL4.
CleanExiHS_RILPL1.
ExpressionAtlasiQ5EBL4. baseline and differential.
GenevisibleiQ5EBL4. HS.

Organism-specific databases

HPAiHPA041314.

Interactioni

Subunit structurei

Interacts (when S-nitrosylated) with GAPDH.By similarity

Protein-protein interaction databases

BioGridi131631. 1 interaction.
IntActiQ5EBL4. 2 interactions.
STRINGi9606.ENSP00000366070.

Structurei

3D structure databases

ProteinModelPortaliQ5EBL4.
SMRiQ5EBL4. Positions 12-91.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 9788RH1PROSITE-ProRule annotationAdd
BLAST
Domaini291 – 35666RH2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili76 – 258183Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the RILPL family.Curated
Contains 1 RH1 domain.PROSITE-ProRule annotation
Contains 1 RH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IRRU. Eukaryota.
ENOG410ZCJ1. LUCA.
GeneTreeiENSGT00530000063269.
HOGENOMiHOG000007529.
HOVERGENiHBG060448.
InParanoidiQ5EBL4.
OMAiQWANSHR.
OrthoDBiEOG7T1RBP.
PhylomeDBiQ5EBL4.
TreeFamiTF313489.

Family and domain databases

InterProiIPR019143. JNK/Rab-associated_protein-1_N.
IPR021563. RILP.
[Graphical view]
PfamiPF09744. Jnk-SapK_ap_N. 1 hit.
PF11461. RILP. 1 hit.
[Graphical view]
PROSITEiPS51776. RH1. 1 hit.
PS51777. RH2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5EBL4-1) [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
MEEERGSALA AESALEKNVA ELTVMDVYDI ASLVGHEFER VIDQHGCEAI
60 70 80 90 100
ARLMPKVVRV LEILEVLVSR HHVAPELDEL RLELDRLRLE RMDRIEKERK
110 120 130 140 150
HQKELELVED VWRGEAQDLL SQIAQLQEEN KQLMTNLSHK DVNFSEEEFQ
160 170 180 190 200
KHEGMSERER QVMKKLKEVV DKQRDEIRAK DRELGLKNED VEALQQQQTR
210 220 230 240 250
LMKINHDLRH RVTVVEAQGK ALIEQKVELE ADLQTKEQEM GSLRAELGKL
260 270 280 290 300
RERLQGEHSQ NGEEEPETEP VGEESISDAE KVAMDLKDPN RPRFTLQELR
310 320 330 340 350
DVLHERNELK SKVFLLQEEL AYYKSEEMEE ENRIPQPPPI AHPRTSPQPE
360 370 380 390 400
SGIKRLFSFF SRDKKRLANT QRNVHIQESF GQWANTHRDD GYTEQGQEAL

QHL
Length:403
Mass (Da):47,108
Last modified:March 15, 2005 - v1
Checksum:i907F7120DE1C8D29
GO
Isoform 2 (identifier: Q5EBL4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     357-403: FSFFSRDKKR...EQGQEALQHL → IFTAIMPMVAAGLIIDDPTLQPVRRLVSLV

Note: No experimental confirmation available.
Show »
Length:362
Mass (Da):42,236
Checksum:iE7184472F0F6DD17
GO
Isoform 3 (identifier: Q5EBL4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     152-153: HE → MT

Note: No experimental confirmation available.
Show »
Length:252
Mass (Da):29,468
Checksum:iBA5E51C86CCDF67B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 151151Missing in isoform 3. 1 PublicationVSP_027605Add
BLAST
Alternative sequencei1 – 2424Missing in isoform 2. 1 PublicationVSP_027606Add
BLAST
Alternative sequencei152 – 1532HE → MT in isoform 3. 1 PublicationVSP_027607
Alternative sequencei357 – 40347FSFFS…ALQHL → IFTAIMPMVAAGLIIDDPTL QPVRRLVSLV in isoform 2. 1 PublicationVSP_027608Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096697 mRNA. Translation: BAC04845.1.
AC055713 Genomic DNA. No translation available.
AC145423 Genomic DNA. No translation available.
BC080626 mRNA. Translation: AAH80626.1.
BC089444 mRNA. Translation: AAH89444.1.
CCDSiCCDS45006.1. [Q5EBL4-1]
RefSeqiNP_001306172.1. NM_001319243.1.
NP_001306173.1. NM_001319244.1. [Q5EBL4-3]
NP_001306231.1. NM_001319302.1. [Q5EBL4-3]
NP_847884.2. NM_178314.4. [Q5EBL4-1]
UniGeneiHs.530315.

Genome annotation databases

EnsembliENST00000376874; ENSP00000366070; ENSG00000188026. [Q5EBL4-1]
GeneIDi353116.
KEGGihsa:353116.
UCSCiuc001ufe.3. human. [Q5EBL4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096697 mRNA. Translation: BAC04845.1.
AC055713 Genomic DNA. No translation available.
AC145423 Genomic DNA. No translation available.
BC080626 mRNA. Translation: AAH80626.1.
BC089444 mRNA. Translation: AAH89444.1.
CCDSiCCDS45006.1. [Q5EBL4-1]
RefSeqiNP_001306172.1. NM_001319243.1.
NP_001306173.1. NM_001319244.1. [Q5EBL4-3]
NP_001306231.1. NM_001319302.1. [Q5EBL4-3]
NP_847884.2. NM_178314.4. [Q5EBL4-1]
UniGeneiHs.530315.

3D structure databases

ProteinModelPortaliQ5EBL4.
SMRiQ5EBL4. Positions 12-91.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131631. 1 interaction.
IntActiQ5EBL4. 2 interactions.
STRINGi9606.ENSP00000366070.

PTM databases

iPTMnetiQ5EBL4.
PhosphoSiteiQ5EBL4.

Polymorphism and mutation databases

BioMutaiRILPL1.
DMDMi74736071.

Proteomic databases

EPDiQ5EBL4.
MaxQBiQ5EBL4.
PaxDbiQ5EBL4.
PRIDEiQ5EBL4.

Protocols and materials databases

DNASUi353116.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376874; ENSP00000366070; ENSG00000188026. [Q5EBL4-1]
GeneIDi353116.
KEGGihsa:353116.
UCSCiuc001ufe.3. human. [Q5EBL4-1]

Organism-specific databases

CTDi353116.
GeneCardsiRILPL1.
H-InvDBHIX0023431.
HGNCiHGNC:26814. RILPL1.
HPAiHPA041314.
MIMi614092. gene.
neXtProtiNX_Q5EBL4.
PharmGKBiPA162401302.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IRRU. Eukaryota.
ENOG410ZCJ1. LUCA.
GeneTreeiENSGT00530000063269.
HOGENOMiHOG000007529.
HOVERGENiHBG060448.
InParanoidiQ5EBL4.
OMAiQWANSHR.
OrthoDBiEOG7T1RBP.
PhylomeDBiQ5EBL4.
TreeFamiTF313489.

Miscellaneous databases

ChiTaRSiRILPL1. human.
GenomeRNAii353116.
NextBioi99657.
PROiQ5EBL4.
SOURCEiSearch...

Gene expression databases

BgeeiQ5EBL4.
CleanExiHS_RILPL1.
ExpressionAtlasiQ5EBL4. baseline and differential.
GenevisibleiQ5EBL4. HS.

Family and domain databases

InterProiIPR019143. JNK/Rab-associated_protein-1_N.
IPR021563. RILP.
[Graphical view]
PfamiPF09744. Jnk-SapK_ap_N. 1 hit.
PF11461. RILP. 1 hit.
[Graphical view]
PROSITEiPS51776. RH1. 1 hit.
PS51777. RH2. 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 2).
    Tissue: Pericardium.
  2. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORMS 1 AND 3).
    Tissue: Brain and Chondrosarcoma.
  4. "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: LACK OF FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRIPL1_HUMAN
AccessioniPrimary (citable) accession number: Q5EBL4
Secondary accession number(s): Q66K36, Q8N1M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 15, 2005
Last modified: May 11, 2016
This is version 93 of the entry and version 1 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families
  4. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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.