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Protein

Nuclear cap-binding protein subunit 2

Gene

NCBP2

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

Functioni

Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (PubMed:26382858).8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201mRNA cap2 Publications
Binding sitei43 – 431mRNA cap2 Publications

GO - Molecular functioni

  • mRNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA 7-methylguanosine cap binding Source: UniProtKB
  • RNA cap binding Source: UniProtKB
  • snRNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA capping, mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, RNA-mediated gene silencing, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-191859. snRNP Assembly.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6803529. FGFR2 alternative splicing.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
R-HSA-77595. Processing of Intronless Pre-mRNAs.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Protein family/group databases

TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear cap-binding protein subunit 2
Alternative name(s):
20 kDa nuclear cap-binding protein
Cell proliferation-inducing gene 55 protein
NCBP 20 kDa subunit
Short name:
CBP20
NCBP-interacting protein 1
Short name:
NIP1
Gene namesi
Name:NCBP2
Synonyms:CBP20
ORF Names:PIG55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:7659. NCBP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • mRNA cap binding complex Source: UniProtKB
  • nuclear cap binding complex Source: GO_Central
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201Y → A: Abolishes mRNA cap-binding. 1 Publication
Mutagenesisi20 – 201Y → F: Strongly impairs mRNA cap-binding. 1 Publication
Mutagenesisi25 – 251F → A: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi43 – 431Y → A: Abolishes mRNA cap-binding. 2 Publications
Mutagenesisi43 – 431Y → F: Does not affect mRNA cap-binding. 2 Publications
Mutagenesisi46 – 461N → A: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi83 – 831F → A: Abolishes mRNA cap-binding. 1 Publication
Mutagenesisi85 – 851F → A: Impairs mRNA cap-binding.
Mutagenesisi112 – 1121R → A or T: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi114 – 1141D → A: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi116 – 1161D → A: Abolishes mRNA cap-binding. 1 Publication
Mutagenesisi119 – 1191F → A: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi138 – 1381Y → A: Does not affect mRNA cap-binding. 1 Publication

Organism-specific databases

PharmGKBiPA31462.

Polymorphism and mutation databases

BioMutaiNCBP2.
DMDMi1705651.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 156155Nuclear cap-binding protein subunit 2PRO_0000081499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei18 – 181PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP52298.
MaxQBiP52298.
PaxDbiP52298.
PeptideAtlasiP52298.
PRIDEiP52298.
TopDownProteomicsiP52298-1. [P52298-1]

PTM databases

iPTMnetiP52298.
PhosphoSiteiP52298.
SwissPalmiP52298.

Expressioni

Gene expression databases

BgeeiENSG00000114503.
CleanExiHS_NCBP2.
ExpressionAtlasiP52298. baseline and differential.
GenevisibleiP52298. HS.

Organism-specific databases

HPAiHPA044850.
HPA062483.

Interactioni

Subunit structurei

Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA (PubMed:26382858). Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Interacts with PHAX/RNUXA, EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY. Interacts with SRRT/ARS2 and KPNA3 (PubMed:26382858).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LZTS2Q9BRK43EBI-464729,EBI-741037
NCBP1Q091618EBI-464729,EBI-464743

Protein-protein interaction databases

BioGridi116578. 46 interactions.
DIPiDIP-33246N.
IntActiP52298. 38 interactions.
MINTiMINT-248711.
STRINGi9606.ENSP00000326806.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104Combined sources
Helixi13 – 153Combined sources
Beta strandi23 – 275Combined sources
Turni34 – 385Combined sources
Beta strandi41 – 466Combined sources
Helixi53 – 608Combined sources
Helixi61 – 633Combined sources
Beta strandi66 – 738Combined sources
Turni75 – 773Combined sources
Beta strandi80 – 9011Combined sources
Helixi91 – 10010Combined sources
Turni101 – 1033Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi112 – 1176Combined sources
Turni121 – 1244Combined sources
Helixi134 – 1374Combined sources
Helixi144 – 1463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2TX-ray2.15Z1-156[»]
1H2UX-ray2.40X/Y1-156[»]
1H2VX-ray2.00Z1-156[»]
1H6KX-ray2.00X/Y/Z22-120[»]
1N52X-ray2.11B1-156[»]
1N54X-ray2.72B1-156[»]
3FEXX-ray3.55B1-156[»]
3FEYX-ray2.20B1-156[»]
DisProtiDP00393.
ProteinModelPortaliP52298.
SMRiP52298. Positions 5-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52298.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 11879RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni112 – 1165mRNA cap-binding
Regioni123 – 1275mRNA cap-binding
Regioni133 – 1342mRNA cap-binding

Sequence similaritiesi

Belongs to the RRM NCBP2 family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0121. Eukaryota.
ENOG4111FJQ. LUCA.
GeneTreeiENSGT00390000003197.
HOGENOMiHOG000217589.
HOVERGENiHBG052581.
InParanoidiP52298.
KOiK12883.
OMAiGNRYEQE.
OrthoDBiEOG091G0RKX.
PhylomeDBiP52298.
TreeFamiTF313897.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR027157. NCBP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR18847. PTHR18847. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 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. AlignAdd to basket

Isoform 1 (identifier: P52298-1) [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

        10         20         30         40         50
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY
60 70 80 90 100
TTEEQIYELF SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY
110 120 130 140 150
INGTRLDDRI IRTDWDAGFK EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG

KLAQNQ
Length:156
Mass (Da):18,001
Last modified:October 1, 1996 - v1
Checksum:iB6C94F3182A2CC3D
GO
Isoform 2 (identifier: P52298-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MSGGLLKALRSDSYVELSQYRDQHFR → MVLRKLYA

Show »
Length:138
Mass (Da):15,937
Checksum:iD2475AF0597FDC0F
GO
Isoform 3 (identifier: P52298-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     40-93: CTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRAD → Y

Note: Gene prediction based on EST data.
Show »
Length:103
Mass (Da):11,932
Checksum:i0790F40FF3E16B61
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971A → S in BAA09599 (PubMed:7478990).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MSGGL…DQHFR → MVLRKLYA in isoform 2. 1 PublicationVSP_038125Add
BLAST
Alternative sequencei40 – 9354CTLYV…YSRAD → Y in isoform 3. CuratedVSP_053823Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84157 mRNA. Translation: CAA58962.1.
D59253 mRNA. Translation: BAA09599.1.
AK297506 mRNA. Translation: BAG59919.1.
AK315903 mRNA. Translation: BAH14274.1.
AK316601 mRNA. Translation: BAG38188.1.
AY644767 mRNA. Translation: AAV85455.1.
BT006842 mRNA. Translation: AAP35488.1.
AC011322 Genomic DNA. No translation available.
CH471191 Genomic DNA. Translation: EAW53624.1.
BC001255 mRNA. Translation: AAH01255.1.
CCDSiCCDS3323.1. [P52298-1]
CCDS46986.1. [P52298-3]
CCDS77878.1. [P52298-2]
PIRiI37222.
S60109.
RefSeqiNP_001036005.1. NM_001042540.1. [P52298-3]
NP_001294965.1. NM_001308036.1. [P52298-2]
NP_031388.2. NM_007362.3. [P52298-1]
UniGeneiHs.591671.

Genome annotation databases

EnsembliENST00000321256; ENSP00000326806; ENSG00000114503. [P52298-1]
ENST00000427641; ENSP00000397619; ENSG00000114503. [P52298-3]
ENST00000452404; ENSP00000412785; ENSG00000114503. [P52298-2]
GeneIDi22916.
KEGGihsa:22916.
UCSCiuc003fxd.2. human. [P52298-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84157 mRNA. Translation: CAA58962.1.
D59253 mRNA. Translation: BAA09599.1.
AK297506 mRNA. Translation: BAG59919.1.
AK315903 mRNA. Translation: BAH14274.1.
AK316601 mRNA. Translation: BAG38188.1.
AY644767 mRNA. Translation: AAV85455.1.
BT006842 mRNA. Translation: AAP35488.1.
AC011322 Genomic DNA. No translation available.
CH471191 Genomic DNA. Translation: EAW53624.1.
BC001255 mRNA. Translation: AAH01255.1.
CCDSiCCDS3323.1. [P52298-1]
CCDS46986.1. [P52298-3]
CCDS77878.1. [P52298-2]
PIRiI37222.
S60109.
RefSeqiNP_001036005.1. NM_001042540.1. [P52298-3]
NP_001294965.1. NM_001308036.1. [P52298-2]
NP_031388.2. NM_007362.3. [P52298-1]
UniGeneiHs.591671.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2TX-ray2.15Z1-156[»]
1H2UX-ray2.40X/Y1-156[»]
1H2VX-ray2.00Z1-156[»]
1H6KX-ray2.00X/Y/Z22-120[»]
1N52X-ray2.11B1-156[»]
1N54X-ray2.72B1-156[»]
3FEXX-ray3.55B1-156[»]
3FEYX-ray2.20B1-156[»]
DisProtiDP00393.
ProteinModelPortaliP52298.
SMRiP52298. Positions 5-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116578. 46 interactions.
DIPiDIP-33246N.
IntActiP52298. 38 interactions.
MINTiMINT-248711.
STRINGi9606.ENSP00000326806.

Protein family/group databases

TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

PTM databases

iPTMnetiP52298.
PhosphoSiteiP52298.
SwissPalmiP52298.

Polymorphism and mutation databases

BioMutaiNCBP2.
DMDMi1705651.

Proteomic databases

EPDiP52298.
MaxQBiP52298.
PaxDbiP52298.
PeptideAtlasiP52298.
PRIDEiP52298.
TopDownProteomicsiP52298-1. [P52298-1]

Protocols and materials databases

DNASUi22916.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321256; ENSP00000326806; ENSG00000114503. [P52298-1]
ENST00000427641; ENSP00000397619; ENSG00000114503. [P52298-3]
ENST00000452404; ENSP00000412785; ENSG00000114503. [P52298-2]
GeneIDi22916.
KEGGihsa:22916.
UCSCiuc003fxd.2. human. [P52298-1]

Organism-specific databases

CTDi22916.
GeneCardsiNCBP2.
HGNCiHGNC:7659. NCBP2.
HPAiHPA044850.
HPA062483.
MIMi605133. gene.
neXtProtiNX_P52298.
PharmGKBiPA31462.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0121. Eukaryota.
ENOG4111FJQ. LUCA.
GeneTreeiENSGT00390000003197.
HOGENOMiHOG000217589.
HOVERGENiHBG052581.
InParanoidiP52298.
KOiK12883.
OMAiGNRYEQE.
OrthoDBiEOG091G0RKX.
PhylomeDBiP52298.
TreeFamiTF313897.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-191859. snRNP Assembly.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6803529. FGFR2 alternative splicing.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
R-HSA-77595. Processing of Intronless Pre-mRNAs.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiNCBP2. human.
EvolutionaryTraceiP52298.
GenomeRNAii22916.
PROiP52298.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000114503.
CleanExiHS_NCBP2.
ExpressionAtlasiP52298. baseline and differential.
GenevisibleiP52298. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR027157. NCBP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR18847. PTHR18847. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNCBP2_HUMAN
AccessioniPrimary (citable) accession number: P52298
Secondary accession number(s): B2RE91
, B4DMK7, E9PAR5, Q14924, Q2TS50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 173 of the entry and version 1 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, Direct protein sequencing, 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

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 one 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.