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Protein

Retinol-binding protein 1

Gene

RBP1

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

Functioni

Intracellular transport of retinol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Retinoic acidBy similarity

GO - Molecular functioni

  • retinal binding Source: UniProtKB-KW
  • retinoid binding Source: ProtInc
  • retinol binding Source: UniProtKB-KW
  • transporter activity Source: InterPro

GO - Biological processi

  • retinoic acid biosynthetic process Source: InterPro
  • retinoid metabolic process Source: Reactome
  • vitamin A metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000114115-MONOMER.
ReactomeiR-HSA-2453864. Retinoid cycle disease events.
R-HSA-2453902. The canonical retinoid cycle in rods (twilight vision).
R-HSA-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol-binding protein 1
Alternative name(s):
Cellular retinol-binding protein
Short name:
CRBP
Cellular retinol-binding protein I
Short name:
CRBP-I
Gene namesi
Name:RBP1
Synonyms:CRBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9919. RBP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34286.

Chemistry

DrugBankiDB00459. Acitretin.
DB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRBP1.
DMDMi132387.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 135134Retinol-binding protein 1PRO_0000067392Add
BLAST

Proteomic databases

EPDiP09455.
MaxQBiP09455.
PaxDbiP09455.
PeptideAtlasiP09455.
PRIDEiP09455.

Expressioni

Tissue specificityi

Detected in nearly all the tissues with higher expression in adult ovary, pancreas, pituitary gland and adrenal gland, and fetal liver.1 Publication

Gene expression databases

BgeeiP09455.
CleanExiHS_RBP1.
ExpressionAtlasiP09455. baseline and differential.
GenevisibleiP09455. HS.

Organism-specific databases

HPAiCAB018603.
CAB019276.
HPA007338.

Interactioni

Protein-protein interaction databases

BioGridi111881. 11 interactions.
IntActiP09455. 2 interactions.
STRINGi9606.ENSP00000232219.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1610Combined sources
Helixi17 – 237Combined sources
Helixi28 – 347Combined sources
Beta strandi40 – 467Combined sources
Beta strandi49 – 557Combined sources
Beta strandi61 – 666Combined sources
Beta strandi71 – 744Combined sources
Turni76 – 794Combined sources
Beta strandi82 – 909Combined sources
Beta strandi93 – 10210Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi125 – 13410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5H8TX-ray1.21A2-135[»]
5H9AX-ray1.38A2-135[»]
5HA1X-ray1.35A2-135[»]
5HBSX-ray0.89A2-135[»]
ProteinModelPortaliP09455.
SMRiP09455. Positions 1-135.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP09455.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP09455.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031264. CRBP1.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF56. PTHR11955:SF56. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: P09455-1) [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
MPVDFTGYWK MLVNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM
60 70 80 90 100
IIRTLSTFRN YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG
110 120 130
EKEGRGWTQW IEGDELHLEM RVEGVVCKQV FKKVQ
Length:135
Mass (Da):15,850
Last modified:January 23, 2007 - v2
Checksum:iFA47545761AFA3A2
GO
Isoform 2 (identifier: P09455-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPPAGFVRAGNPAVAAPQSPLSPEGAHFRAAHHPRSTGSRCPGSLQPSRPLVANWLQSLPEM
     85-135: TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ → SETGFSS

Note: No experimental confirmation available.Curated
Show »
Length:153
Mass (Da):17,104
Checksum:i6142D55498572358
GO
Isoform 3 (identifier: P09455-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPPAGFVRAGNPAVAAPQSPLSPEGAHFRAAHHPRSTGSRCPGSLQPSRPLVANWLQSLPEM
     85-135: TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ → AGVQSRDLSSL

Note: No experimental confirmation available.
Show »
Length:157
Mass (Da):17,523
Checksum:i454E1DC7BE53793A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P09455-2)
Sequence conflicti18 – 181P → L in BAH13536 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDPPAGFVRAGNPAVAAPQS PLSPEGAHFRAAHHPRSTGS RCPGSLQPSRPLVANWLQSL PEM in isoform 2 and isoform 3. 1 PublicationVSP_046201
Alternative sequencei85 – 13551TTVSW…FKKVQ → SETGFSS in isoform 2. 1 PublicationVSP_046202Add
BLAST
Alternative sequencei85 – 13551TTVSW…FKKVQ → AGVQSRDLSSL in isoform 3. 1 PublicationVSP_046203Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11433 mRNA. Translation: AAA60257.1.
X07437, X07438 Genomic DNA. Translation: CAA30318.1.
AK290315 mRNA. Translation: BAF83004.1.
AK301684 mRNA. Translation: BAH13536.1.
AK309492 Genomic DNA. No translation available.
CR541979 mRNA. Translation: CAG46776.1.
CR542005 mRNA. Translation: CAG46802.1.
AC046134 Genomic DNA. No translation available.
BC121052 mRNA. Translation: AAI21053.1.
M36809 mRNA. Translation: AAA35714.1.
CCDSiCCDS46925.1. [P09455-2]
CCDS46926.1. [P09455-3]
PIRiS00399. RJHUO.
RefSeqiNP_001124464.1. NM_001130992.1. [P09455-3]
NP_001124465.1. NM_001130993.1. [P09455-2]
NP_002890.2. NM_002899.3.
UniGeneiHs.529571.

Genome annotation databases

EnsembliENST00000492918; ENSP00000429166; ENSG00000114115. [P09455-3]
ENST00000617459; ENSP00000477621; ENSG00000114115. [P09455-2]
ENST00000619087; ENSP00000482165; ENSG00000114115. [P09455-1]
GeneIDi5947.
KEGGihsa:5947.
UCSCiuc011bmx.2. human. [P09455-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11433 mRNA. Translation: AAA60257.1.
X07437, X07438 Genomic DNA. Translation: CAA30318.1.
AK290315 mRNA. Translation: BAF83004.1.
AK301684 mRNA. Translation: BAH13536.1.
AK309492 Genomic DNA. No translation available.
CR541979 mRNA. Translation: CAG46776.1.
CR542005 mRNA. Translation: CAG46802.1.
AC046134 Genomic DNA. No translation available.
BC121052 mRNA. Translation: AAI21053.1.
M36809 mRNA. Translation: AAA35714.1.
CCDSiCCDS46925.1. [P09455-2]
CCDS46926.1. [P09455-3]
PIRiS00399. RJHUO.
RefSeqiNP_001124464.1. NM_001130992.1. [P09455-3]
NP_001124465.1. NM_001130993.1. [P09455-2]
NP_002890.2. NM_002899.3.
UniGeneiHs.529571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5H8TX-ray1.21A2-135[»]
5H9AX-ray1.38A2-135[»]
5HA1X-ray1.35A2-135[»]
5HBSX-ray0.89A2-135[»]
ProteinModelPortaliP09455.
SMRiP09455. Positions 1-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111881. 11 interactions.
IntActiP09455. 2 interactions.
STRINGi9606.ENSP00000232219.

Chemistry

DrugBankiDB00459. Acitretin.
DB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRBP1.
DMDMi132387.

Proteomic databases

EPDiP09455.
MaxQBiP09455.
PaxDbiP09455.
PeptideAtlasiP09455.
PRIDEiP09455.

Protocols and materials databases

DNASUi5947.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000492918; ENSP00000429166; ENSG00000114115. [P09455-3]
ENST00000617459; ENSP00000477621; ENSG00000114115. [P09455-2]
ENST00000619087; ENSP00000482165; ENSG00000114115. [P09455-1]
GeneIDi5947.
KEGGihsa:5947.
UCSCiuc011bmx.2. human. [P09455-1]

Organism-specific databases

CTDi5947.
GeneCardsiRBP1.
H-InvDBHIX0030850.
HGNCiHGNC:9919. RBP1.
HPAiCAB018603.
CAB019276.
HPA007338.
MIMi180260. gene.
neXtProtiNX_P09455.
PharmGKBiPA34286.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP09455.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP09455.
TreeFamiTF316894.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000114115-MONOMER.
ReactomeiR-HSA-2453864. Retinoid cycle disease events.
R-HSA-2453902. The canonical retinoid cycle in rods (twilight vision).
R-HSA-975634. Retinoid metabolism and transport.

Miscellaneous databases

GeneWikiiRBP1.
GenomeRNAii5947.
PROiP09455.
SOURCEiSearch...

Gene expression databases

BgeeiP09455.
CleanExiHS_RBP1.
ExpressionAtlasiP09455. baseline and differential.
GenevisibleiP09455. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031264. CRBP1.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF56. PTHR11955:SF56. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a full length cDNA corresponding to human cellular retinol-binding protein."
    Colantuoni V., Cortese R., Nilsson M., Lundvall J., Baavik C.-O., Eriksson U., Peterson P.A., Sundelin J.
    Biochem. Biophys. Res. Commun. 130:431-439(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Human cellular retinol-binding protein gene organization and chromosomal location."
    Nilsson M.H.L., Spurr N.K., Lundvall J., Rask L., Peterson P.A.
    Eur. J. Biochem. 173:35-44(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Esophagus, Heart and Tongue.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    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 1).
  7. "Cellular retinoic acid- and cellular retinol-binding proteins: complementary deoxyribonucleic acid cloning, chromosomal assignment, and tissue specific expression."
    Wei L.-N., Mertz J.R., Goodman D.S., Nguyen-Huu M.C.
    Mol. Endocrinol. 1:526-534(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-121 (ISOFORM 1).
  8. "Identification, retinoid binding and X-ray analysis of a human retinol-binding protein."
    Folli C., Calderone V., Ottonello S., Bolchi A., Zanotti G., Stoppini M., Berni R.
    Proc. Natl. Acad. Sci. U.S.A. 98:3710-3715(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 nameiRET1_HUMAN
AccessioniPrimary (citable) accession number: P09455
Secondary accession number(s): A8K2Q0
, B7Z7A0, E7EWV0, F2Z2F2, Q6FGX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 156 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.