RNASE1

Functionⁱ

Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.1 Publication

Catalytic activityⁱ

Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	35	SubstrateBy similarity	1
Binding siteⁱ	38	SubstrateBy similarity	1
Active siteⁱ	40	Proton acceptor	1
Binding siteⁱ	94	SubstrateBy similarity	1
Binding siteⁱ	113	SubstrateBy similarity	1
Active siteⁱ	147	Proton donor	1

GO - Molecular functionⁱ

nucleic acid binding Source: InterPro
ribonuclease A activity
Source: ProtInc
Traceable author statementⁱ
- 8049276
ribonuclease activity
Source: UniProtKB
Inferred from direct assayⁱ
- 9826755

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

RNA phosphodiester bond hydrolysis
Source: UniProtKB
Inferred from direct assayⁱ
- 9826755

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Endonuclease, Hydrolase, Nuclease

Molecular function

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDAⁱ	3.1.27.5 2681

BRENDAⁱ

3.1.27.5 2681

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ribonuclease pancreatic (EC:3.1.27.5) Alternative name(s): HP-RNase RIB-1 RNase UpI-1 Ribonuclease 1 Short name: RNase 1 Ribonuclease A Short name: RNase A
Gene namesⁱ	Name:RNASE1 Synonyms:RIB1, RNS1
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 14

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000129538.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:10044 RNASE1
MIMⁱ	180440 gene
neXtProtⁱ	NX_P07998

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	67	R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-95, A-116, D-117 and D-119. 1 Publication	1
Mutagenesisⁱ	95	N → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, A-116, D-117 and D-119. 1 Publication	1
Mutagenesisⁱ	116 – 117	NG → RS: No effect on inhibition by RNH1. 1 Publication	2
Mutagenesisⁱ	116	N → A: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, D-117 and D-119. 1 Publication	1
Mutagenesisⁱ	117	G → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-119. 1 Publication	1
Mutagenesisⁱ	119	R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-117. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6035
Open Targets More...OpenTargetsⁱ	ENSG00000129538
PharmGKBⁱ	PA34412

Chemistry databases

ChEMBLⁱ	CHEMBL5425
Drug and drug target database More...DrugBankⁱ	DB03765 2'-cytidylic acid DB03448 2'-Deoxyuridine 3'-Monophosphate DB02363 2'-Monophosphoadenosine-5'-Diphosphate DB03900 2-Methyl-2-Propanol DB01842 3'-Phosphate-Adenosine-5'-Diphosphate DB02714 3'-Uridinemonophosphate DB08596 5'-deoxy-5'-piperidin-1-ylthymidine DB02098 Adenosine-2'-5'-Diphosphate DB01812 Adenosine-3'-5'-Diphosphate DB04272 Citric Acid DB02987 Cysteine-S-Acetamide DB01961 Cytidine-3'-Monophosphate DB01942 Formic Acid DB00536 Guanidine DB02325 Isopropyl Alcohol DB00128 L-Aspartic Acid DB04464 N-Formylmethionine DB04514 Phosphoric Acid-2'-[2'-Deoxy-Uridine]Ester-5'-Guanosine Ester DB03726 Purine Riboside-5'-Monophosphate DB03186 U-Pi-a-Pi DB02805 Uracil arabinose-3'-phosphate DB03447 Uridylyl-2'-5'-Phospho-Adenosine

ChEMBLⁱ

CHEMBL5425

DrugBankⁱ

DB03765 2'-cytidylic acid
DB03448 2'-Deoxyuridine 3'-Monophosphate
DB02363 2'-Monophosphoadenosine-5'-Diphosphate
DB03900 2-Methyl-2-Propanol
DB01842 3'-Phosphate-Adenosine-5'-Diphosphate
DB02714 3'-Uridinemonophosphate
DB08596 5'-deoxy-5'-piperidin-1-ylthymidine
DB02098 Adenosine-2'-5'-Diphosphate
DB01812 Adenosine-3'-5'-Diphosphate
DB04272 Citric Acid
DB02987 Cysteine-S-Acetamide
DB01961 Cytidine-3'-Monophosphate
DB01942 Formic Acid
DB00536 Guanidine
DB02325 Isopropyl Alcohol
DB00128 L-Aspartic Acid
DB04464 N-Formylmethionine
DB04514 Phosphoric Acid-2'-[2'-Deoxy-Uridine]Ester-5'-Guanosine Ester
DB03726 Purine Riboside-5'-Monophosphate
DB03186 U-Pi-a-Pi
DB02805 Uracil arabinose-3'-phosphate
DB03447 Uridylyl-2'-5'-Phospho-Adenosine

Polymorphism and mutation databases

BioMutaⁱ	RNASE1
DMDMⁱ	1350818

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 28	6 PublicationsAdd BLAST		28
ChainⁱPRO_0000030921	29 – 156	Ribonuclease pancreaticAdd BLAST		128

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	54 ↔ 112
Glycosylationⁱ	62	N-linked (GlcNAc...) asparagine; partial1 Publication	1
Disulfide bondⁱ	68 ↔ 123
Disulfide bondⁱ	86 ↔ 138
Disulfide bondⁱ	93 ↔ 100
Glycosylationⁱ	104	N-linked (GlcNAc...) asparagine1 Publication	1
Glycosylationⁱ	116	N-linked (GlcNAc...) asparagine1 Publication	1

Post-translational modificationⁱ

N-linked glycans are of complex type.1 Publication

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbⁱ	P07998
PeptideAtlas More...PeptideAtlasⁱ	P07998
PRIDEⁱ	P07998
ProteomicsDBⁱ	52059

PTM databases

iPTMnetⁱ	P07998
PhosphoSitePlusⁱ	P07998

Expressionⁱ

Tissue specificityⁱ

Pancreas and other tissues and body fluids (indicating it may have other physiological functions besides its role in digestion).

Gene expression databases

Bgeeⁱ	ENSG00000129538 Expressed in 226 organ(s), highest expression level in right testis
CleanExⁱ	HS_RNASE1
ExpressionAtlasⁱ	P07998 baseline and differential
Genevisibleⁱ	P07998 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA001140

HPAⁱ

HPA001140

Interactionⁱ

Subunit structureⁱ

Monomer. Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
RNH1	P13489	2	EBI-2823523,EBI-1237106

With

Entry

#Exp.

IntAct

Notes

RNH1

P13489

2

EBI-2823523,EBI-1237106

Protein-protein interaction databases

BioGridⁱ	111964, 5 interactors
IntActⁱ	P07998, 7 interactors
Molecular INTeraction database More...MINTⁱ	P07998
STRINGⁱ	9606.ENSP00000344193

Chemistry databases

BindingDBⁱ

P07998

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	32 – 40	Combined sources	9
Turnⁱ	47 – 50	Combined sources	4
Helixⁱ	53 – 60	Combined sources	8
Turnⁱ	61 – 64	Combined sources	4
Beta strandⁱ	65 – 67	Combined sources	3
Beta strandⁱ	70 – 75	Combined sources	6
Helixⁱ	79 – 83	Combined sources	5
Helixⁱ	84 – 87	Combined sources	4
Beta strandⁱ	88 – 92	Combined sources	5
Beta strandⁱ	96 – 102	Combined sources	7
Beta strandⁱ	107 – 114	Combined sources	8
Beta strandⁱ	120 – 122	Combined sources	3
Beta strandⁱ	125 – 139	Combined sources	15
Turnⁱ	140 – 143	Combined sources	4
Beta strandⁱ	144 – 152	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	P07998
SMRⁱ	P07998
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P07998

EvolutionaryTraceⁱ

P07998

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	69 – 73	Substrate bindingBy similarity		5

Sequence similaritiesⁱ

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	ENOG410IYEN Eukaryota ENOG41113F1 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00900000140967
HOVERGENⁱ	HBG008396
InParanoidⁱ	P07998
KEGG Orthology (KO) More...KOⁱ	K01168
OMAⁱ	SNSTYCN
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G15X3
PhylomeDBⁱ	P07998
TreeFamⁱ	TF333393

Family and domain databases

Gene3Dⁱ	3.10.130.10, 1 hit
InterProⁱ	View protein in InterPro IPR001427 RNaseA IPR036816 RNaseA-like_dom_sf IPR023411 RNaseA_AS IPR023412 RNaseA_domain
PANTHERⁱ	PTHR11437 PTHR11437, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00074 RnaseA, 1 hit
PRINTSⁱ	PR00794 RIBONUCLEASE
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD000535 RNaseA, 1 hit
SMARTⁱ	View protein in SMART SM00092 RNAse_Pc, 1 hit
SUPFAMⁱ	SSF54076 SSF54076, 1 hit
PROSITEⁱ	View protein in PROSITE PS00127 RNASE_PANCREATIC, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

P07998-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS 
        60         70         80         90        100
STYCNQMMRR RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC 
       110        120        130        140        150
YKSNSSMHIT DCRLTNGSRY PNCAYRTSPK ERHIIVACEG SPYVPVHFDA 

SVEDST

Length:156

Mass (Da):17,644

Last modified:February 1, 1996 - v4

Checksum:ⁱF63B17B8B55115F9

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	G3V357	G3V357_HUMAN		Ribonuclease pancreatic Ribonuclease pancreatic	RNASE1	116	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	2	A → G in CAA55817 (PubMed:8588814).Curated	1
Sequence conflictⁱ	4	Missing in AAB35096 (PubMed:7649283).Curated	1
Sequence conflictⁱ	9 – 11	RLL → VLP in AAB35096 (PubMed:7649283).Curated	3
Sequence conflictⁱ	16 – 22	ILLVLGW → VLLLVR in AAB35096 (PubMed:7649283).Curated	7
Sequence conflictⁱ	67	R → L in CAG29314 (Ref. 4) Curated	1
Sequence conflictⁱ	151	S → T in CAA55817 (PubMed:8588814).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D26129 mRNA Translation: BAA05124.1 DQ494867 Genomic DNA Translation: ABF00144.1 AK312100 mRNA Translation: BAG35036.1 CR450318 mRNA Translation: CAG29314.1 CH471078 Genomic DNA Translation: EAW66437.1 CH471078 Genomic DNA Translation: EAW66438.1 BC005324 mRNA Translation: AAH05324.1 BC022882 mRNA Translation: AAH22882.1 X79235 Genomic DNA Translation: CAA55817.1 S79281 mRNA Translation: AAB35096.1 X62946 Genomic DNA Translation: CAA44718.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS9559.1
PIRⁱ	I53530 S45003 NRHU1
NCBI Reference Sequences More...RefSeqⁱ	NP_002924.1, NM_002933.4 NP_937875.1, NM_198232.2 NP_937877.1, NM_198234.2 NP_937878.1, NM_198235.2
UniGeneⁱ	Hs.78224

Genome annotation databases

Ensemblⁱ	ENST00000340900; ENSP00000344193; ENSG00000129538 ENST00000397967; ENSP00000381057; ENSG00000129538 ENST00000397970; ENSP00000381060; ENSG00000129538 ENST00000412779; ENSP00000399493; ENSG00000129538
GeneIDⁱ	6035
KEGGⁱ	hsa:6035

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P07998	Ribonuclease A C1		HUMAN		156	UniRef100_P07998
Ribonuclease pancreatic		HUMAN		116
UPI000002C248		HUMAN		127

Protein	Similar proteins		Species	Score	Length	Source
P07998	Ribonuclease pancreatic		ATEGE		156	UniRef90_P07998
Ribonuclease pancreatic		GORGO		156
Ribonuclease pancreatic		LAGLA		156
Ribonuclease pancreatic		NOMLE		156
Ribonuclease pancreatic		PANTR		156
+11

Protein	Similar proteins		Species	Score	Length	Source
P07998	Ribonuclease pancreatic		ATEGE		156	UniRef50_P07998
Ribonuclease pancreatic		LAGLA		156
Ribonuclease pancreatic		SAGOE		156
Ribonuclease pancreatic		SAISC		156
Ribonuclease pancreatic		PONPY		156
+41

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D26129 mRNA Translation: BAA05124.1 DQ494867 Genomic DNA Translation: ABF00144.1 AK312100 mRNA Translation: BAG35036.1 CR450318 mRNA Translation: CAG29314.1 CH471078 Genomic DNA Translation: EAW66437.1 CH471078 Genomic DNA Translation: EAW66438.1 BC005324 mRNA Translation: AAH05324.1 BC022882 mRNA Translation: AAH22882.1 X79235 Genomic DNA Translation: CAA55817.1 S79281 mRNA Translation: AAB35096.1 X62946 Genomic DNA Translation: CAA44718.1
CCDSⁱ	CCDS9559.1
PIRⁱ	I53530 S45003 NRHU1
RefSeqⁱ	NP_002924.1, NM_002933.4 NP_937875.1, NM_198232.2 NP_937877.1, NM_198234.2 NP_937878.1, NM_198235.2
UniGeneⁱ	Hs.78224

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
	1DZA	X-ray	1.65	A/B	28-156	[»]
	1E21	X-ray	1.90	A	29-156	[»]
	1H8X	X-ray	2.00	A/B	29-156	[»]
	1Z7X	X-ray	1.95	X/Z	29-156	[»]
	2E0J	X-ray	1.60	A/B	29-156	[»]
	2E0L	X-ray	1.60	A/B	29-156	[»]
	2E0M	X-ray	1.70	A/B	29-156	[»]
	2E0O	X-ray	2.00	A/B	29-156	[»]
	2K11	NMR	-	A	29-155	[»]
	2Q4G	X-ray	1.95	X/Z	29-156	[»]
	3F8G	X-ray	2.60	A/B	29-153	[»]
	4KXH	X-ray	2.70	A/B/C/D	29-156	[»]
ProteinModelPortalⁱ	P07998
SMRⁱ	P07998
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111964, 5 interactors
IntActⁱ	P07998, 7 interactors
MINTⁱ	P07998
STRINGⁱ	9606.ENSP00000344193

Chemistry databases

BindingDBⁱ	P07998
ChEMBLⁱ	CHEMBL5425
DrugBankⁱ	DB03765 2'-cytidylic acid DB03448 2'-Deoxyuridine 3'-Monophosphate DB02363 2'-Monophosphoadenosine-5'-Diphosphate DB03900 2-Methyl-2-Propanol DB01842 3'-Phosphate-Adenosine-5'-Diphosphate DB02714 3'-Uridinemonophosphate DB08596 5'-deoxy-5'-piperidin-1-ylthymidine DB02098 Adenosine-2'-5'-Diphosphate DB01812 Adenosine-3'-5'-Diphosphate DB04272 Citric Acid DB02987 Cysteine-S-Acetamide DB01961 Cytidine-3'-Monophosphate DB01942 Formic Acid DB00536 Guanidine DB02325 Isopropyl Alcohol DB00128 L-Aspartic Acid DB04464 N-Formylmethionine DB04514 Phosphoric Acid-2'-[2'-Deoxy-Uridine]Ester-5'-Guanosine Ester DB03726 Purine Riboside-5'-Monophosphate DB03186 U-Pi-a-Pi DB02805 Uracil arabinose-3'-phosphate DB03447 Uridylyl-2'-5'-Phospho-Adenosine

PTM databases

iPTMnetⁱ	P07998
PhosphoSitePlusⁱ	P07998

Polymorphism and mutation databases

BioMutaⁱ	RNASE1
DMDMⁱ	1350818

Proteomic databases

PaxDbⁱ	P07998
PeptideAtlasⁱ	P07998
PRIDEⁱ	P07998
ProteomicsDBⁱ	52059

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000340900; ENSP00000344193; ENSG00000129538 ENST00000397967; ENSP00000381057; ENSG00000129538 ENST00000397970; ENSP00000381060; ENSG00000129538 ENST00000412779; ENSP00000399493; ENSG00000129538
GeneIDⁱ	6035
KEGGⁱ	hsa:6035

Organism-specific databases

CTDⁱ	6035
DisGeNETⁱ	6035
EuPathDBⁱ	HostDB:ENSG00000129538.13
GeneCardsⁱ	RNASE1
HGNCⁱ	HGNC:10044 RNASE1
HPAⁱ	HPA001140
MIMⁱ	180440 gene
neXtProtⁱ	NX_P07998
OpenTargetsⁱ	ENSG00000129538
PharmGKBⁱ	PA34412
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IYEN Eukaryota ENOG41113F1 LUCA
GeneTreeⁱ	ENSGT00900000140967
HOVERGENⁱ	HBG008396
InParanoidⁱ	P07998
KOⁱ	K01168
OMAⁱ	SNSTYCN
OrthoDBⁱ	EOG091G15X3
PhylomeDBⁱ	P07998
TreeFamⁱ	TF333393

Enzyme and pathway databases

BRENDAⁱ	3.1.27.5 2681

BRENDAⁱ

3.1.27.5 2681

Miscellaneous databases

ChiTaRSⁱ	RNASE1 human
EvolutionaryTraceⁱ	P07998
GeneWikiⁱ	RNASE1
GenomeRNAiⁱ	6035
Protein Ontology More...PROⁱ	PR:P07998
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000129538 Expressed in 226 organ(s), highest expression level in right testis
CleanExⁱ	HS_RNASE1
ExpressionAtlasⁱ	P07998 baseline and differential
Genevisibleⁱ	P07998 HS

Family and domain databases

Gene3Dⁱ	3.10.130.10, 1 hit
InterProⁱ	View protein in InterPro IPR001427 RNaseA IPR036816 RNaseA-like_dom_sf IPR023411 RNaseA_AS IPR023412 RNaseA_domain
PANTHERⁱ	PTHR11437 PTHR11437, 1 hit
Pfamⁱ	View protein in Pfam PF00074 RnaseA, 1 hit
PRINTSⁱ	PR00794 RIBONUCLEASE
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD000535 RNaseA, 1 hit
SMARTⁱ	View protein in SMART SM00092 RNAse_Pc, 1 hit
SUPFAMⁱ	SSF54076 SSF54076, 1 hit
PROSITEⁱ	View protein in PROSITE PS00127 RNASE_PANCREATIC, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RNAS1_HUMAN
Accessionⁱ	P07998Primary (citable) accession number: P07998 Secondary accession number(s): B2R589 Q9UCB5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
	Last sequence update:	February 1, 1996
	Last modified:	November 7, 2018
	This is version 189 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM

UniProtKB

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UniRef

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Supporting data

UniProtKB - P07998 (RNAS1_HUMAN)

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Ribonuclease pancreatic

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

Extracellular region or secreted

Extracellular region or secreted

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

Chemistry 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

Miscellaneous 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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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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<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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 - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ