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P50120 (RET2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinol-binding protein 2
Alternative name(s):
Cellular retinol-binding protein II
Short name=CRBP-II
Gene names
Name:RBP2
Synonyms:CRBP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length134 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Intracellular transport of retinol.

Subcellular location

Cytoplasm.

Tissue specificity

Higher expression in adult small intestine and to a much lesser extent in fetal kidney. Ref.5

Domain

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

Sequence similarities

Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 134133Retinol-binding protein 2
PRO_0000067395

Sites

Binding site411Retinoic acid
Binding site1091Retinoic acid By similarity

Experimental info

Sequence conflict311R → P in AAC50162. Ref.1
Sequence conflict1141D → G in AAH69396. Ref.4

Secondary structure

......................... 134
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50120 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A4A7FB157B099A7D

FASTA13415,707
        10         20         30         40         50         60 
MTRDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KVIDQDGDNF KTKTTSTFRN 

        70         80         90        100        110        120 
YDVDFTVGVE FDEYTKSLDN RHVKALVTWE GDVLVCVQKG EKENRGWKQW IEGDKLYLEL 

       130 
TCGDQVCRQV FKKK 

« Hide

References

« Hide 'large scale' references
[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. 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].
Tissue: Small intestine.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3109.1.
RefSeqNP_004155.2. NM_004164.2.
XP_005247750.1. XM_005247693.1.
XP_006713785.1. XM_006713722.1.
UniGeneHs.655516.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP50120.
SMRP50120. Positions 2-134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111882. 3 interactions.
STRING9606.ENSP00000232217.

Chemistry

BindingDBP50120.
DrugBankDB00162. Vitamin A.

Protein family/group databases

TCDB8.A.33.1.3. the fatty acid binding protein (fabp) family.

PTM databases

PhosphoSiteP50120.

Polymorphism databases

DMDM62297500.

Proteomic databases

MaxQBP50120.
PaxDbP50120.
PRIDEP50120.

Protocols and materials databases

DNASU5948.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000232217; ENSP00000232217; ENSG00000114113.
GeneID5948.
KEGGhsa:5948.
UCSCuc003eth.3. human.

Organism-specific databases

CTD5948.
GeneCardsGC03M139171.
HGNCHGNC:9920. RBP2.
HPAHPA035866.
MIM180280. gene.
neXtProtNX_P50120.
PharmGKBPA34287.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284832.
HOGENOMHOG000004831.
HOVERGENHBG005633.
InParanoidP50120.
KOK14622.
OMAKKEGYKP.
OrthoDBEOG7NW6BZ.
PhylomeDBP50120.
TreeFamTF316894.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000114113-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP50120.
BgeeP50120.
CleanExHS_RBP2.
GenevestigatorP50120.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP50120.
GeneWikiRBP2.
GenomeRNAi5948.
NextBio23174.
PROP50120.
SOURCESearch...

Entry information

Entry nameRET2_HUMAN
AccessionPrimary (citable) accession number: P50120
Secondary accession number(s): A8K7G3, Q6ISQ9, Q6ISS7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 125 of the entry and version 3 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 chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM