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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Actin-binding Calmodulin-binding
PTM	Acetylation
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 PubMed 16236705. Source: MGI cytoskeleton organization Traceable author statement Ref.1. Source: ProtInc hemopoiesis Inferred from electronic annotation. Source: Compara negative regulation of cell migration Inferred from electronic annotation. Source: Compara negative regulation of phagocytosis Inferred from electronic annotation. Source: Compara positive regulation of gene expression Inferred from electronic annotation. Source: Compara regulation of actin filament-based process Inferred from direct assay PubMed 16236705. Source: MGI regulation of cell proliferation Inferred from electronic annotation. Source: Compara wound healing Inferred from electronic annotation. Source: Compara
Cellular_component	cell-cell junction Traceable author statement Ref.1. Source: ProtInc stress fiber Inferred from direct assay PubMed 16236705. Source: MGI
Molecular_function	actin binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99439-1)

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.

Isoform 2 (identifier: Q99439-2)

The sequence of this isoform differs from the canonical sequence as follows:
     131-169: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

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

2

1

N-acetylserine Ref.8

Modified residue

8

1

N6-acetyllysine Ref.8

Modified residue

25

1

N6-acetyllysine Ref.8

Natural variations

Alternative sequence

131 – 169

39

Missing in isoform 2.

VSP_042941

Experimental info

Sequence conflict

52

1

K → R in BAA20887. Ref.6

Sequence conflict

142

1

I → V in BAA20887. Ref.6

Sequence conflict

165

1

V → G in BAA20887. Ref.6

Sequence conflict

182 – 183

2

TA → HL in BAA20887. Ref.6

Sequence conflict

187 – 202

16

RRHLY…LPPMD → AGISMTPRTISCPPWT in BAA20887. Ref.6

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)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: 6CCEFDE1EE200798	FASTA	270	29,500
	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 MGTNKCASQS GMTAYGTRRH LYDPKNHILP PMDHSTISLQ MGTNKCASQV 190 200 210 220 230 240 GMTAPGTRRH IYDTKLGTDK CDNSSMSLQM GYTQGANQSG QVFGLGRQIY DPKYCPQGTV 250 260 270 ADGAPSGTGD CPDPGEVPEY PPYYQEEAGY

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Heart.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Uterus.
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-202 (ISOFORM 1). Tissue: Placenta.
[7]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Tissue: Platelet.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-8 AND LYS-25, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[9]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D83735 mRNA. Translation: BAA12090.1.
AK126391 mRNA. Translation: BAG54322.1.
AC004528 Genomic DNA. No translation available.
AC011558 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69565.1.
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.
IPI00398735.

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.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99439. 1 interaction.

STRING

9606.ENSP00000263097.

PTM databases

PhosphoSite

Q99439.

Polymorphism databases

DMDM

6226844.

2D gel databases

OGP

Q99439.

Proteomic databases

PaxDb

Q99439.

PeptideAtlas

Q99439.

PRIDE

Q99439.

Protocols and materials databases

DNASU

1265.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263097; ENSP00000263097; ENSG00000064666.
ENST00000348419; ENSP00000340129; ENSG00000064666.

GeneID

1265.

KEGG

hsa:1265.

UCSC

uc002lqt.1. human.
uc002lqu.3. human.

Organism-specific databases

CTD

1265.

GeneCards

GC19P001026.

HGNC

HGNC:2156. CNN2.

HPA

HPA049095.

MIM

602373. gene.

neXtProt

NX_Q99439.

PharmGKB

PA26666.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5199.

HOGENOM

HOG000232113.

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

Gene3D

1.10.418.10. 1 hit.

InterPro

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

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

ChiTaRS

CNN2. human.

EvolutionaryTrace

Q99439.

GenomeRNAi

1265.

NextBio

5119.

SOURCE

Search...

Entry information

Entry name

CNN2_HUMAN

Accession

Primary (citable) accession number: Q99439
Secondary accession number(s): A5D8U8 , A6NFI4, D6W5X9, Q92578

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 128 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.