Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Retinol-binding protein 2

Gene

RBP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Intracellular transport of retinol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411Retinoic acid
Binding sitei109 – 1091Retinoic acidBy 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. epidermis development Source: ProtInc
  2. phototransduction, visible light Source: Reactome
  3. retinoid metabolic process Source: Reactome
  4. vitamin A metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000114113-MONOMER.
ReactomeiREACT_24968. Retinoid metabolism and transport.

Protein family/group databases

TCDBi8.A.33.1.3. the fatty acid binding protein (fabp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol-binding protein 2
Alternative name(s):
Cellular retinol-binding protein II
Short name:
CRBP-II
Gene namesi
Name:RBP2
Synonyms:CRBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9920. RBP2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34287.

Chemistry

DrugBankiDB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRBP2.
DMDMi62297500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 134133Retinol-binding protein 2PRO_0000067395Add
BLAST

Proteomic databases

MaxQBiP50120.
PaxDbiP50120.
PRIDEiP50120.

PTM databases

PhosphoSiteiP50120.

Expressioni

Tissue specificityi

Higher expression in adult small intestine and to a much lesser extent in fetal kidney.1 Publication

Gene expression databases

BgeeiP50120.
CleanExiHS_RBP2.
ExpressionAtlasiP50120. baseline and differential.
GenevestigatoriP50120.

Organism-specific databases

HPAiHPA035866.

Interactioni

Protein-protein interaction databases

BioGridi111882. 3 interactions.
IntActiP50120. 3 interactions.
STRINGi9606.ENSP00000232217.

Structurei

Secondary structure

1
134
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 – 10412Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi125 – 1339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RCQX-ray1.20A2-134[»]
2RCTX-ray1.20A2-134[»]
4EDEX-ray1.40A/B2-134[»]
4EEJX-ray1.50A/B2-134[»]
4EFGX-ray1.58A/B2-134[»]
4EXZX-ray1.61A/B2-134[»]
4GKCX-ray1.30A/B2-134[»]
4QYNX-ray1.19A/B2-134[»]
4QYPX-ray1.62A/B/C/D2-134[»]
4QZTX-ray1.90A/B/C/D2-134[»]
4QZUX-ray1.50A/B/C/D2-134[»]
4RUUX-ray1.40A/B2-134[»]
ProteinModelPortaliP50120.
SMRiP50120. Positions 2-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50120.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG284832.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP50120.
KOiK14622.
OMAiQNGTWEM.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP50120.
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]

Sequencei

Sequence statusi: Complete.

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

P50120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KVIDQDGDNF
60 70 80 90 100
KTKTTSTFRN YDVDFTVGVE FDEYTKSLDN RHVKALVTWE GDVLVCVQKG
110 120 130
EKENRGWKQW IEGDKLYLEL TCGDQVCRQV FKKK
Length:134
Mass (Da):15,707
Last modified:January 23, 2007 - v3
Checksum:iA4A7FB157B099A7D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311R → P in AAC50162 (PubMed:7657783).Curated
Sequence conflicti114 – 1141D → G in AAH69396 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13831 mRNA. Translation: AAC50162.1.
AK291978 mRNA. Translation: BAF84667.1.
CH471052 Genomic DNA. Translation: EAW79036.1.
BC069296 mRNA. Translation: AAH69296.1.
BC069361 mRNA. Translation: AAH69361.1.
BC069396 mRNA. Translation: AAH69396.1.
BC069424 mRNA. Translation: AAH69424.1.
BC069447 mRNA. Translation: AAH69447.1.
BC069513 mRNA. Translation: AAH69513.1.
BC069522 mRNA. Translation: AAH69522.1.
CCDSiCCDS3109.1.
RefSeqiNP_004155.2. NM_004164.2.
UniGeneiHs.655516.

Genome annotation databases

EnsembliENST00000232217; ENSP00000232217; ENSG00000114113.
GeneIDi5948.
KEGGihsa:5948.
UCSCiuc003eth.3. human.

Polymorphism and mutation databases

BioMutaiRBP2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13831 mRNA. Translation: AAC50162.1.
AK291978 mRNA. Translation: BAF84667.1.
CH471052 Genomic DNA. Translation: EAW79036.1.
BC069296 mRNA. Translation: AAH69296.1.
BC069361 mRNA. Translation: AAH69361.1.
BC069396 mRNA. Translation: AAH69396.1.
BC069424 mRNA. Translation: AAH69424.1.
BC069447 mRNA. Translation: AAH69447.1.
BC069513 mRNA. Translation: AAH69513.1.
BC069522 mRNA. Translation: AAH69522.1.
CCDSiCCDS3109.1.
RefSeqiNP_004155.2. NM_004164.2.
UniGeneiHs.655516.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RCQX-ray1.20A2-134[»]
2RCTX-ray1.20A2-134[»]
4EDEX-ray1.40A/B2-134[»]
4EEJX-ray1.50A/B2-134[»]
4EFGX-ray1.58A/B2-134[»]
4EXZX-ray1.61A/B2-134[»]
4GKCX-ray1.30A/B2-134[»]
4QYNX-ray1.19A/B2-134[»]
4QYPX-ray1.62A/B/C/D2-134[»]
4QZTX-ray1.90A/B/C/D2-134[»]
4QZUX-ray1.50A/B/C/D2-134[»]
4RUUX-ray1.40A/B2-134[»]
ProteinModelPortaliP50120.
SMRiP50120. Positions 2-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111882. 3 interactions.
IntActiP50120. 3 interactions.
STRINGi9606.ENSP00000232217.

Chemistry

DrugBankiDB00162. Vitamin A.

Protein family/group databases

TCDBi8.A.33.1.3. the fatty acid binding protein (fabp) family.

PTM databases

PhosphoSiteiP50120.

Polymorphism and mutation databases

BioMutaiRBP2.
DMDMi62297500.

Proteomic databases

MaxQBiP50120.
PaxDbiP50120.
PRIDEiP50120.

Protocols and materials databases

DNASUi5948.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000232217; ENSP00000232217; ENSG00000114113.
GeneIDi5948.
KEGGihsa:5948.
UCSCiuc003eth.3. human.

Organism-specific databases

CTDi5948.
GeneCardsiGC03M139171.
HGNCiHGNC:9920. RBP2.
HPAiHPA035866.
MIMi180280. gene.
neXtProtiNX_P50120.
PharmGKBiPA34287.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG284832.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP50120.
KOiK14622.
OMAiQNGTWEM.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP50120.
TreeFamiTF316894.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000114113-MONOMER.
ReactomeiREACT_24968. Retinoid metabolism and transport.

Miscellaneous databases

EvolutionaryTraceiP50120.
GeneWikiiRBP2.
GenomeRNAii5948.
NextBioi23174.
PROiP50120.
SOURCEiSearch...

Gene expression databases

BgeeiP50120.
CleanExiHS_RBP2.
ExpressionAtlasiP50120. baseline and differential.
GenevestigatoriP50120.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Variation in the expression of cellular retinoid binding proteins in human endometrium throughout the menstrual cycle."
    Loughney A.D., Kumarendran M.K., Thomas E.J., Redfern C.P.F.
    Hum. Reprod. 10:1297-1304(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
    , 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].
    Tissue: Small intestine.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "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.
  6. "Crystal structure of human cellular retinol-binding protein II to 1.2 A resolution."
    Tarter M., Capaldi S., Carrizo M.E., Ambrosi E., Perduca M., Monaco H.L.
    Proteins 70:1626-1630(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH RETINOL.

Entry informationi

Entry nameiRET2_HUMAN
AccessioniPrimary (citable) accession number: P50120
Secondary accession number(s): A8K7G3, Q6ISQ9, Q6ISS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 134 of the entry and version 3 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

External Data

Dasty 3

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 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.