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Protein

Cysteine and glycine-rich protein 2

Gene

CSRP2

Organism
Coturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression. Totally down-regulated in transformed cells.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine and glycine-rich protein 2
Alternative name(s):
Cysteine-rich protein 2
Short name:
CRP2
Gene namesi
Name:CSRP2
OrganismiCoturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Taxonomic identifieri93934 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePerdicinaeCoturnix

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000757252 – 194Cysteine and glycine-rich protein 2Add BLAST193

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Beta strandi22 – 25Combined sources4
Beta strandi28 – 36Combined sources9
Beta strandi38 – 40Combined sources3
Beta strandi50 – 52Combined sources3
Beta strandi55 – 57Combined sources3
Helixi60 – 65Combined sources6
Beta strandi118 – 120Combined sources3
Turni121 – 123Combined sources3
Beta strandi129 – 131Combined sources3
Beta strandi133 – 137Combined sources5
Beta strandi138 – 140Combined sources3
Turni142 – 144Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi159 – 162Combined sources4
Beta strandi165 – 167Combined sources3
Helixi169 – 174Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A7INMR-A1-81[»]
1CXXNMR-A82-194[»]
1IBINMR-A82-194[»]
1QLINMR-A82-194[»]
DisProtiDP00438.
ProteinModelPortaliQ05158.
SMRiQ05158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05158.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 61LIM zinc-binding 1PROSITE-ProRule annotationAdd BLAST52
Domaini120 – 171LIM zinc-binding 2PROSITE-ProRule annotationAdd BLAST52

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi64 – 69Nuclear localization signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi63 – 78Gly-richAdd BLAST16
Compositional biasi177 – 188Gly-richAdd BLAST12

Sequence similaritiesi

Contains 2 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

HOVERGENiHBG051143.

Family and domain databases

Gene3Di2.10.110.10. 2 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 2 hits.
[Graphical view]
SMARTiSM00132. LIM. 2 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q05158-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNWGGGNKC GACGRTVYHA EEVQCDGRSF HRCCFLCMVC RKNLDSTTVA
60 70 80 90 100
IHDAEVYCKS CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESSPSPHR
110 120 130 140 150
PTTNPNTSKF AQKFGGAEKC SRCGDSVYAA EKVIGAGKPW HKNCFRCAKC
160 170 180 190
GKSLESTTLT EKEGEIYCKG CYAKNFGPKG FGYGQGAGAL VHAQ
Length:194
Mass (Da):20,911
Last modified:January 23, 2007 - v2
Checksum:iD59CA624D1C1269E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21643 mRNA. Translation: CAA79759.1.
PIRiS41761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21643 mRNA. Translation: CAA79759.1.
PIRiS41761.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A7INMR-A1-81[»]
1CXXNMR-A82-194[»]
1IBINMR-A82-194[»]
1QLINMR-A82-194[»]
DisProtiDP00438.
ProteinModelPortaliQ05158.
SMRiQ05158.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG051143.

Miscellaneous databases

EvolutionaryTraceiQ05158.

Family and domain databases

Gene3Di2.10.110.10. 2 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 2 hits.
[Graphical view]
SMARTiSM00132. LIM. 2 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCSRP2_COTJA
AccessioniPrimary (citable) accession number: Q05158
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.