Q99439 (CNN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calponin-2

Alternative name(s):
Calponin H2, smooth muscle
Neutral calponin

Gene names

Name:

CNN2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
Tissue specificity	Heart and smooth muscle.
Sequence similarities	Belongs to the calponin family. Contains 3 calponin-like repeats. Contains 1 CH (calponin-homology) domain.

Ontologies

Keywords
Domain	Repeat
Ligand	Actin-binding Calmodulin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	actomyosin structure organization Inferred from electronic annotation. Source: InterPro cellular response to mechanical stimulus Inferred from direct assay. Source: MGI regulation of actin filament-based process Inferred from direct assay. Source: MGI
Cellular component	cell-cell junction Traceable author statement. Source: ProtInc stress fiber Inferred from direct assay. Source: MGI
Molecular function	actin binding Traceable author statement. Source: ProtInc calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 309

308

Calponin-2

PRO_0000204773

Regions

Domain

28 – 131

104

CH

Repeat

166 – 191

26

Calponin-like 1

Repeat

206 – 231

26

Calponin-like 2

Repeat

245 – 269

25

Calponin-like 3

Amino acid modifications

Modified residue

8

1

N6-acetyllysine Ref.7

Modified residue

25

1

N6-acetyllysine Ref.7

Modified residue

184

1

Phosphotyrosine Ref.6

Experimental info

Sequence conflict

52

1

K → R in BAA20887. Ref.4

Sequence conflict

142

1

I → V in BAA20887. Ref.4

Sequence conflict

165

1

V → G in BAA20887. Ref.4

Sequence conflict

182 – 183

2

TA → HL in BAA20887. Ref.4

Sequence conflict

187 – 202

16

RRHLY…LPPMD → AGISMTPRTISCPPWT in BAA20887. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

309

Helix Strand Turn

Details...

Helix

30 – 42

13

Helix

50 – 55

6

Helix

59 – 67

9

Helix

81 – 98

18

Beta strand

102 – 104

3

Helix

108 – 112

5

Helix

118 – 131

14

Helix

132 – 134

3

Sequences

	Sequence		Length	Mass (Da)
	Q99439 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 0D767E9040190A5F	FASTA	309	33,697
	10 20 30 40 50 60 MSSTQFNKGP SYGLSAEVKN RLLSKYDPQK EAELRTWIEG LTGLSIGPDF QKGLKDGTIL 70 80 90 100 110 120 CTLMNKLQPG SVPKINRSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFESGNMTQV 130 140 150 160 170 180 QVSLLALAGK AKTKGLQSGV DIGVKYSEKQ ERNFDDATMK AGQCVIGLQM GTNKCASQSG 190 200 210 220 230 240 MTAYGTRRHL YDPKNHILPP MDHSTISLQM GTNKCASQVG MTAPGTRRHI YDTKLGTDKC 250 260 270 280 290 300 DNSSMSLQMG YTQGANQSGQ VFGLGRQIYD PKYCPQGTVA DGAPSGTGDC PDPGEVPEYP PYYQEEAGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of human non-smooth muscle calponin." Masuda H., Tanaka K., Takagi M., Ohgami K., Sakamaki T., Shibata N., Takahashi K. J. Biochem. 120:415-424(1996) [PubMed: 8889829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	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. , 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].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"A unique downregulation of h2-calponin gene expression in Down syndrome: a possible attenuation mechanism for fetal survival by methylation at the CpG island in the trisomic chromosome 21." Kuromitsu J., Yamashita H., Kataoka H., Takahara T., Muramatsu M., Sekine T., Okamoto N., Furuichi Y., Hayashizaki Y. Mol. Cell. Biol. 17:707-712(1997) [PubMed: 9001224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-202. Tissue: Placenta.
[5]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Tissue: Platelet.
[6]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-184, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-25, MASS SPECTROMETRY.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Solution structure of the CH domain of human calponin-2." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 20-152.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D83735 mRNA. Translation: BAA12090.1.
CH471139 Genomic DNA. Translation: EAW69567.1.
CH471139 Genomic DNA. Translation: EAW69570.1.
BC141818 mRNA. Translation: AAI41819.1.
BC141833 mRNA. Translation: AAI41834.1.
D86059 mRNA. Translation: BAA20887.1.

IPI

IPI00015262.

PIR

JC4906.

RefSeq

NP_004359.1. NM_004368.2.
NP_958434.1. NM_201277.1.

UniGene

Hs.651512.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WYN	NMR	-	A	20-151	[»]

ProteinModelPortal

Q99439.

SMR

Q99439. Positions 13-153.

ModBase

Search...

Protein-protein interaction databases

STRING

Q99439.

PTM databases

PhosphoSite

Q99439.

Polymorphism databases

DMDM

6226844.

2D gel databases

OGP

Q99439.

Proteomic databases

PeptideAtlas

Q99439.

PRIDE

Q99439.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263097; ENSP00000263097; ENSG00000064666.

GeneID

1265.

KEGG

hsa:1265.

UCSC

uc002lqu.1. human.

Organism-specific databases

CTD

1265.

GeneCards

GC19P001026.

H-InvDB

HIX0014568.

HGNC

HGNC:2156. CNN2.

MIM

602373. gene.

neXtProt

NX_Q99439.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00550000074447.

HOVERGEN

HBG005186.

InParanoid

Q99439.

OMA

CPQGPAA.

OrthoDB

EOG49W2G2.

PhylomeDB

Q99439.

Gene expression databases

ArrayExpress

Q99439.

Bgee

Q99439.

CleanEx

HS_CNN2.

Genevestigator

Q99439.

GermOnline

ENSG00000064666. Homo sapiens.

Family and domain databases

InterPro

IPR001997. Calponin.
IPR000557. Calponin_repeat.
IPR001715. CH-domain.
IPR003096. SM22_calponin.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 1 hit.

Pfam

PF00402. Calponin. 3 hits.
PF00307. CH. 1 hit.
[Graphical view]

PRINTS

PR00889. CALPONIN.
PR00888. SM22CALPONIN.

SMART

SM00033. CH. 1 hit.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS01052. CALPONIN_1. 3 hits.
PS51122. CALPONIN_2. 3 hits.
PS50021. CH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

5119.

SOURCE

Search...

Entry information

Entry name

CNN2_HUMAN

Accession

Primary (citable) accession number: Q99439
Secondary accession number(s): A5D8U8, D6W5X9, Q92578

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 113 of the entry and version 4 of the sequence. [Complete history]

Entry status

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.