RBP1

Functionⁱ

Cytoplasmic retinol-binding protein (PubMed:22665496, PubMed:26900151, PubMed:28057518). Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis (PubMed:15632377, PubMed:22665496).4 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	41	RetinolCombined sources1 Publication	1
Binding siteⁱ	63	RetinolCombined sources1 Publication	1
Binding siteⁱ	109	RetinolCombined sources2 Publications	1

GO - Molecular functionⁱ

all-trans-retinol binding
Source: UniProtKB
Inferred from direct assayⁱ
- 28057518
retinal binding Source: UniProtKB-KW
retinoid binding
Source: ProtInc
Traceable author statementⁱ
- 3472205

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

lipid homeostasis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15632377
retinoic acid biosynthetic process Source: InterPro
retinoid metabolic process Source: Reactome
vitamin A metabolic process
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15632377

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Transport
Ligand	Retinol-binding, Vitamin A

Enzyme and pathway databases

BioCycⁱ	MetaCyc:ENSG00000114115-MONOMER
Reactomeⁱ	R-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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 3

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000114115.9
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9919 RBP1
MIMⁱ	180260 gene
neXtProtⁱ	NX_P09455

Keywords - Cellular componentⁱ

Cytoplasm, Lipid droplet

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	22	R → A: No effect on retinol binding. Abolishes interaction with STA6 and the ability to enhance STA6-mediated vitamin A uptake. 1 Publication	1
Mutagenesisⁱ	30	L → A: Decreases cellular retinol uptake and impairs retinol storage. 1 Publication	1
Mutagenesisⁱ	31	R → A: No effect on retinol binding. Abolishes interaction with STA6 and the ability to enhance STA6-mediated vitamin A uptake. 1 Publication	1
Mutagenesisⁱ	32	K → A: No effect on retinol binding. Abolishes interaction with STA6 and the ability to enhance STA6-mediated vitamin A uptake. 1 Publication	1
Mutagenesisⁱ	41	K → L: Strongly decreased affinity for retinol. Further decrease in affinity for retinol; when associated with L-109. 1 Publication	1
Mutagenesisⁱ	59	R → E: Decreases cellular retinol uptake and impairs retinol storage. 1 Publication	1
Mutagenesisⁱ	109	Q → L: Strongly decreased affinity for retinol. Further decrease in for retinol; when associated with L-41. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5947
Open Targets More...OpenTargetsⁱ	ENSG00000114115
PharmGKBⁱ	PA34286

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB00459 Acitretin DB00162 Vitamin A

DrugBankⁱ

DB00459 Acitretin
DB00162 Vitamin A

Polymorphism and mutation databases

BioMutaⁱ	RBP1
DMDMⁱ	132387

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000067392	1 – 135	Retinol-binding protein 1Add BLAST		135

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Isoform 2 (identifier: P09455-2)
Modified residueⁱ	9	Omega-N-methylarginineCombined sourcesCurated	1
Isoform 3 (identifier: P09455-3)
Modified residueⁱ	9	Omega-N-methylarginineCombined sources	1

Keywords - PTMⁱ

Methylation

Proteomic databases

EPDⁱ	P09455
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P09455
PaxDbⁱ	P09455
PeptideAtlas More...PeptideAtlasⁱ	P09455
PRIDEⁱ	P09455
ProteomicsDBⁱ	52219

PTM databases

iPTMnetⁱ	P09455
PhosphoSitePlusⁱ	P09455

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

Bgeeⁱ	ENSG00000114115 Expressed in 211 organ(s), highest expression level in pigmented layer of retina
CleanExⁱ	HS_RBP1
ExpressionAtlasⁱ	P09455 baseline and differential
Genevisibleⁱ	P09455 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB018603 CAB019276 HPA007338

HPAⁱ

CAB018603
CAB019276
HPA007338

Interactionⁱ

Subunit structureⁱ

Interacts (only as retinol-free apoprotein) with STRA6.1 Publication

Protein-protein interaction databases

BioGridⁱ	111881, 13 interactors
IntActⁱ	P09455, 8 interactors
STRINGⁱ	9606.ENSP00000232219

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	7 – 16	Combined sources	10
Helixⁱ	17 – 23	Combined sources	7
Helixⁱ	28 – 34	Combined sources	7
Beta strandⁱ	40 – 46	Combined sources	7
Beta strandⁱ	49 – 55	Combined sources	7
Beta strandⁱ	61 – 66	Combined sources	6
Beta strandⁱ	71 – 74	Combined sources	4
Turnⁱ	76 – 79	Combined sources	4
Beta strandⁱ	82 – 90	Combined sources	9
Beta strandⁱ	93 – 102	Combined sources	10
Beta strandⁱ	106 – 112	Combined sources	7
Beta strandⁱ	115 – 122	Combined sources	8
Beta strandⁱ	125 – 134	Combined sources	10

Show more details

3D structure databases

ProteinModelPortalⁱ	P09455
SMRⁱ	P09455
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	22 – 32	Important for interaction with STRA61 PublicationAdd BLAST		11

Domainⁱ

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.2 Publications

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	KOG4015 Eukaryota ENOG4111US8 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118898
HOGENOMⁱ	HOG000004831
HOVERGENⁱ	HBG005633
InParanoidⁱ	P09455
PhylomeDBⁱ	P09455
TreeFamⁱ	TF316894

Family and domain databases

Gene3Dⁱ	2.40.128.20, 1 hit
InterProⁱ	View protein in InterPro IPR012674 Calycin IPR031264 CRBP1 IPR000463 Fatty_acid-bd IPR031259 ILBP IPR000566 Lipocln_cytosolic_FA-bd_dom
PANTHERⁱ	PTHR11955 PTHR11955, 1 hit PTHR11955:SF56 PTHR11955:SF56, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00061 Lipocalin, 1 hit
PRINTSⁱ	PR00178 FATTYACIDBP
SUPFAMⁱ	SSF50814 SSF50814, 1 hit
PROSITEⁱ	View protein in PROSITE PS00214 FABP, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P09455-1) [UniParc]FASTA Add 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]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MDPPAGFVRA GNPAVAAPQS PLSPEGAHFR AAHHPRSTGS RCPGSLQPSR 
        60         70         80         90        100
PLVANWLQSL PEMPVDFTGY WKMLVNENFE EYLRALDVNV ALRKIANLLK 
       110        120        130        140        150
PDKEIVQDGD HMIIRTLSTF RNYIMDFQVG KEFEEDLTGI DDRKCMSETG 

FSS

Show »

Length:153

Mass (Da):17,104

Checksum:ⁱ6142D55498572358

GO

Isoform 3 (identifier: P09455-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MDPPAGFVRA GNPAVAAPQS PLSPEGAHFR AAHHPRSTGS RCPGSLQPSR 
        60         70         80         90        100
PLVANWLQSL PEMPVDFTGY WKMLVNENFE EYLRALDVNV ALRKIANLLK 
       110        120        130        140        150
PDKEIVQDGD HMIIRTLSTF RNYIMDFQVG KEFEEDLTGI DDRKCMAGVQ 

SRDLSSL

Show »

Length:157

Mass (Da):17,523

Checksum:ⁱ454E1DC7BE53793A

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A0A0MQT0	A0A0A0MQT0_HUMAN	Retinol binding protein 1, cellular Retinol binding protein 1, cellular (Retinol-binding protein 1)	RBP1 hCG_16055	197	Annotation score:
H0YAK8	H0YAK8_HUMAN	Retinol-binding protein 1 Retinol-binding protein 1	RBP1	98	Annotation score:
A0A0A0MTB9	A0A0A0MTB9_HUMAN	Retinol-binding protein 1 Retinol-binding protein 1	RBP1	91	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Isoform 2 (identifier: P09455-2)
Sequence conflictⁱ	18	P → L in BAH13536 (PubMed:14702039).Combined sourcesCurated		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_046201	1	M → MDPPAGFVRAGNPAVAAPQS PLSPEGAHFRAAHHPRSTGS RCPGSLQPSRPLVANWLQSL PEM in isoform 2 and isoform 3. 1 Publication	1
Alternative sequenceⁱVSP_046202	85 – 135	TTVSW…FKKVQ → SETGFSS in isoform 2. 1 PublicationAdd BLAST	51
Alternative sequenceⁱVSP_046203	85 – 135	TTVSW…FKKVQ → AGVQSRDLSSL in isoform 3. 1 PublicationAdd BLAST	51

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS46925.1 [P09455-2] CCDS46926.1 [P09455-3]
PIRⁱ	S00399 RJHUO
NCBI Reference Sequences More...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

Genome annotation databases

Ensemblⁱ	ENST00000492918; ENSP00000429166; ENSG00000114115 [P09455-3] ENST00000617459; ENSP00000477621; ENSG00000114115 [P09455-2] ENST00000619087; ENSP00000482165; ENSG00000114115 [P09455-1]
GeneIDⁱ	5947
KEGGⁱ	hsa:5947
UCSC genome browser More...UCSCⁱ	uc011bmx.2 human [P09455-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P09455	Retinol binding protein 1, cellular		HUMAN		197	UniRef100_P09455
RBP1 isoform 1		PONAB		135
RBP1 isoform 6		PANTR		135

Protein	Similar proteins		Species	Score	Length	Source
P09455	Retinol binding protein 1, cellular		HUMAN		197	UniRef90_P09455
RBP1 isoform 1		PONAB		135
RBP1 isoform 6		PANTR		135
Uncharacterized protein		COLAP		197
Uncharacterized protein		PAPAN		197
+26
P09455-2	Isoform 3 of Retinol-binding protein 1		HUMAN		157	UniRef90_P09455-3
Uncharacterized protein		COLAP		158
Uncharacterized protein		PAPAN		158
Uncharacterized protein		CERAT		158
Uncharacterized protein		MANLE		158
+22
P09455-3	Uncharacterized protein		COLAP		158	UniRef90_P09455-3
Uncharacterized protein		PAPAN		158
Uncharacterized protein		CERAT		158
Uncharacterized protein		MANLE		158
Uncharacterized protein		RHIRO		158
+22

Protein	Similar proteins		Species	Score	Length	Source
P09455	Retinol-binding protein 1		MOUSE		135	UniRef50_P09455
Retinol-binding protein 1	)	RAT		135
Retinol binding protein 1, cellular		HUMAN		197
RBP1 isoform 1		PONAB		135
RBP1 isoform 6		PANTR		135
+79
P09455-2	Isoform 3 of Retinol-binding protein 1		HUMAN		157	UniRef50_P09455-3
Uncharacterized protein		PAPAN		158
Uncharacterized protein		CERAT		158
Uncharacterized protein		MANLE		158
Uncharacterized protein		RHIBE		158
+62
P09455-3	Uncharacterized protein		PAPAN		158	UniRef50_P09455-3
Uncharacterized protein		CERAT		158
Uncharacterized protein		MANLE		158
Uncharacterized protein		RHIBE		158
Uncharacterized protein		RHIRO		158
+62

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
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

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5H8T	X-ray	1.21	A	2-135	[»]
	5H9A	X-ray	1.38	A	2-135	[»]
	5HA1	X-ray	1.35	A	2-135	[»]
	5HBS	X-ray	0.89	A	2-135	[»]
	5LJB	X-ray	1.26	A	1-135	[»]
	5LJC	X-ray	1.43	A	1-135	[»]
	5LJD	X-ray	1.61	A	1-135	[»]
	5LJE	X-ray	1.40	A	1-135	[»]
	5LJG	X-ray	1.15	A	1-135	[»]
	5LJH	X-ray	1.52	A	1-135	[»]
	5LJK	X-ray	1.70	A	1-135	[»]
ProteinModelPortalⁱ	P09455
SMRⁱ	P09455
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111881, 13 interactors
IntActⁱ	P09455, 8 interactors
STRINGⁱ	9606.ENSP00000232219

Chemistry databases

DrugBankⁱ	DB00459 Acitretin DB00162 Vitamin A

DrugBankⁱ

DB00459 Acitretin
DB00162 Vitamin A

PTM databases

iPTMnetⁱ	P09455
PhosphoSitePlusⁱ	P09455

Polymorphism and mutation databases

BioMutaⁱ	RBP1
DMDMⁱ	132387

Proteomic databases

EPDⁱ	P09455
MaxQBⁱ	P09455
PaxDbⁱ	P09455
PeptideAtlasⁱ	P09455
PRIDEⁱ	P09455
ProteomicsDBⁱ	52219

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5947
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000492918; ENSP00000429166; ENSG00000114115 [P09455-3] ENST00000617459; ENSP00000477621; ENSG00000114115 [P09455-2] ENST00000619087; ENSP00000482165; ENSG00000114115 [P09455-1]
GeneIDⁱ	5947
KEGGⁱ	hsa:5947
UCSCⁱ	uc011bmx.2 human [P09455-1]

Organism-specific databases

CTDⁱ	5947
DisGeNETⁱ	5947
EuPathDBⁱ	HostDB:ENSG00000114115.9
GeneCardsⁱ	RBP1
H-InvDBⁱ	HIX0030850
HGNCⁱ	HGNC:9919 RBP1
HPAⁱ	CAB018603 CAB019276 HPA007338
MIMⁱ	180260 gene
neXtProtⁱ	NX_P09455
OpenTargetsⁱ	ENSG00000114115
PharmGKBⁱ	PA34286
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG4015 Eukaryota ENOG4111US8 LUCA
GeneTreeⁱ	ENSGT00760000118898
HOGENOMⁱ	HOG000004831
HOVERGENⁱ	HBG005633
InParanoidⁱ	P09455
PhylomeDBⁱ	P09455
TreeFamⁱ	TF316894

Enzyme and pathway databases

BioCycⁱ	MetaCyc:ENSG00000114115-MONOMER
Reactomeⁱ	R-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

GeneWikiⁱ	RBP1
GenomeRNAiⁱ	5947
Protein Ontology More...PROⁱ	PR:P09455
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000114115 Expressed in 211 organ(s), highest expression level in pigmented layer of retina
CleanExⁱ	HS_RBP1
ExpressionAtlasⁱ	P09455 baseline and differential
Genevisibleⁱ	P09455 HS

Family and domain databases

Gene3Dⁱ	2.40.128.20, 1 hit
InterProⁱ	View protein in InterPro IPR012674 Calycin IPR031264 CRBP1 IPR000463 Fatty_acid-bd IPR031259 ILBP IPR000566 Lipocln_cytosolic_FA-bd_dom
PANTHERⁱ	PTHR11955 PTHR11955, 1 hit PTHR11955:SF56 PTHR11955:SF56, 1 hit
Pfamⁱ	View protein in Pfam PF00061 Lipocalin, 1 hit
PRINTSⁱ	PR00178 FATTYACIDBP
SUPFAMⁱ	SSF50814 SSF50814, 1 hit
PROSITEⁱ	View protein in PROSITE PS00214 FABP, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RET1_HUMAN
Accessionⁱ	P09455Primary (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 12, 2018
	This is version 172 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P09455 (RET1_HUMAN)

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Retinol-binding protein 1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Other locations

Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ