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P09455

- RET1_HUMAN

UniProt

P09455 - RET1_HUMAN

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Protein

Retinol-binding protein 1

Gene
RBP1, CRBP1
Organism
Homo sapiens (Human)
Status
Reviewed - 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 acid By similarity

GO - Molecular functioni

  1. retinal binding Source: UniProtKB-KW
  2. retinoid binding Source: ProtInc
  3. retinol binding Source: UniProtKB-KW
  4. transporter activity Source: InterPro

GO - Biological processi

  1. phototransduction, visible light Source: Reactome
  2. retinoid metabolic process Source: Reactome
  3. 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.
ReactomeiREACT_160130. Retinoid cycle disease events.
REACT_160156. The canonical retinoid cycle in rods (twilight vision).
REACT_24968. 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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9919. RBP1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34286.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 135134Retinol-binding protein 1PRO_0000067392Add
BLAST

Proteomic databases

MaxQBiP09455.
PaxDbiP09455.
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

ArrayExpressiP09455.
BgeeiP09455.
CleanExiHS_RBP1.
GenevestigatoriP09455.

Organism-specific databases

HPAiCAB018603.
CAB019276.
HPA007338.

Interactioni

Protein-protein interaction databases

BioGridi111881. 9 interactions.
IntActiP09455. 2 interactions.
STRINGi9606.ENSP00000232219.

Structurei

3D structure databases

ProteinModelPortaliP09455.
SMRiP09455. Positions 1-135.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG306453.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP09455.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP09455.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
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. Align

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

MPVDFTGYWK MLVNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM    50
IIRTLSTFRN YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG 100
EKEGRGWTQW IEGDELHLEM RVEGVVCKQV FKKVQ 135
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.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDPPAGFVRAGNPAVAAPQS PLSPEGAHFRAAHHPRSTGS RCPGSLQPSRPLVANWLQSL PEM in isoform 2 and isoform 3. VSP_046201
Alternative sequencei85 – 13551TTVSW…FKKVQ → SETGFSS in isoform 2. VSP_046202Add
BLAST
Alternative sequencei85 – 13551TTVSW…FKKVQ → AGVQSRDLSSL in isoform 3. VSP_046203Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P09455-2)
Sequence conflicti18 – 181P → L in BAH13536. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000483943; ENSP00000424813; ENSG00000114115. [P09455-2]
ENST00000492918; ENSP00000429166; ENSG00000114115. [P09455-3]
GeneIDi5947.
KEGGihsa:5947.

Polymorphism databases

DMDMi132387.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS46925.1. [P09455-2 ]
CCDS46926.1. [P09455-3 ]
PIRi S00399. RJHUO.
RefSeqi NP_001124464.1. NM_001130992.1. [P09455-3 ]
NP_001124465.1. NM_001130993.1. [P09455-2 ]
NP_002890.2. NM_002899.3.
UniGenei Hs.529571.

3D structure databases

ProteinModelPortali P09455.
SMRi P09455. Positions 1-135.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111881. 9 interactions.
IntActi P09455. 2 interactions.
STRINGi 9606.ENSP00000232219.

Chemistry

BindingDBi P09455.
DrugBanki DB00162. Vitamin A.

Polymorphism databases

DMDMi 132387.

Proteomic databases

MaxQBi P09455.
PaxDbi P09455.
PRIDEi P09455.

Protocols and materials databases

DNASUi 5947.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000483943 ; ENSP00000424813 ; ENSG00000114115 . [P09455-2 ]
ENST00000492918 ; ENSP00000429166 ; ENSG00000114115 . [P09455-3 ]
GeneIDi 5947.
KEGGi hsa:5947.

Organism-specific databases

CTDi 5947.
GeneCardsi GC03M139236.
H-InvDB HIX0030850.
HGNCi HGNC:9919. RBP1.
HPAi CAB018603.
CAB019276.
HPA007338.
MIMi 180260. gene.
neXtProti NX_P09455.
PharmGKBi PA34286.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306453.
HOGENOMi HOG000004831.
HOVERGENi HBG005633.
InParanoidi P09455.
OrthoDBi EOG7NW6BZ.
PhylomeDBi P09455.
TreeFami TF316894.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000114115-MONOMER.
Reactomei REACT_160130. Retinoid cycle disease events.
REACT_160156. The canonical retinoid cycle in rods (twilight vision).
REACT_24968. Retinoid metabolism and transport.

Miscellaneous databases

GeneWikii RBP1.
GenomeRNAii 5947.
NextBioi 23170.
PROi P09455.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09455.
Bgeei P09455.
CleanExi HS_RBP1.
Genevestigatori P09455.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR00178. FATTYACIDBP.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00214. FABP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 138 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 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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