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Q05682 (CALD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caldesmon

Short name=CDM
Gene names
Name:CALD1
Synonyms:CAD, CDM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration By similarity. Ref.7

Subcellular location

Cytoplasmcytoskeleton By similarity. Cytoplasmmyofibril By similarity. Note: On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle) By similarity.

Tissue specificity

High-molecular-weight caldesmon (isoform 1)is predominantly expressed in smooth muscles, whereas low-molecular-weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart.

Domain

The N-terminal part seems to be a myosin/calmodulin-binding domain, and the C-terminal a tropomyosin/actin/calmodulin-binding domain. These two domains are separated by a central helical region in the smooth-muscle form.

Post-translational modification

In non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration By similarity.

Sequence similarities

Belongs to the caldesmon family.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q05682-1)

Also known as: H-CAD;

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: Q05682-2)

Also known as: WI-38 L-CAD I;

The sequence of this isoform differs from the canonical sequence as follows:
     208-436: Missing.
Note: Contains a phosphoserine at position 202.
Isoform 3 (identifier: Q05682-3)

Also known as: HELA L-CAD I;

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MDDFERRRELRRQKREEMRLEAER → MLGGSGSHGRRSLAALSQ
     208-436: Missing.
Note: Contains a phosphoserine at position 196. Contains a phosphoserine at position 12. Contains a phosphotyrosine at position 21.
Isoform 4 (identifier: Q05682-4)

Also known as: WI-38 L-CAD II; 1-CAD;

The sequence of this isoform differs from the canonical sequence as follows:
     208-462: Missing.
Note: Contains a phosphoserine at position 202.
Isoform 5 (identifier: Q05682-5)

Also known as: HELA L-CAD II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MDDFERRRELRRQKREEMRLEAER → MLGGSGSHGRRSLAALSQ
     208-462: Missing.
Note: Contains a phosphoserine at position 196. Contains a phosphoserine at position 12. Contains a phosphotyrosine at position 21.
Isoform 6 (identifier: Q05682-6)

The sequence of this isoform differs from the canonical sequence as follows:
     208-436: Missing.
     660-660: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 202.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 793793Caldesmon
PRO_0000089288

Regions

Repeat319 – 332141
Repeat333 – 346142
Repeat347 – 360143
Region26 – 207182Myosin and calmodulin-binding By similarity
Region319 – 375573 X 14 AA tandem repeats of E-E-E-K-R-A-A-E-E-R-Q-R-I-K
Region564 – 62158Tropomyosin-binding Potential
Region653 – 68634Strong actin-binding By similarity
Region664 – 67411Tropomyosin-binding Potential
Region716 – 7227Calmodulin-binding By similarity
Region768 – 79326Weak actin-binding By similarity
Compositional bias39 – 468Poly-Arg
Compositional bias81 – 866Poly-Thr
Compositional bias189 – 1968Poly-Glu
Compositional bias376 – 3794Poly-Glu
Compositional bias540 – 5434Poly-Arg
Compositional bias580 – 5834Poly-Glu
Compositional bias597 – 6004Poly-Glu

Amino acid modifications

Modified residue731Phosphoserine Ref.14
Modified residue6431Phosphoserine Ref.14
Modified residue7241Phosphoserine Ref.10 Ref.12
Modified residue7301Phosphothreonine Ref.8 Ref.9 Ref.10 Ref.12
Modified residue7531Phosphothreonine Ref.10 Ref.12
Modified residue7591Phosphoserine By similarity
Modified residue7891Phosphoserine Ref.10 Ref.14

Natural variations

Alternative sequence1 – 2424MDDFE…LEAER → MLGGSGSHGRRSLAALSQ in isoform 3 and isoform 5.
VSP_004154
Alternative sequence208 – 462255Missing in isoform 4 and isoform 5.
VSP_004156
Alternative sequence208 – 436229Missing in isoform 2, isoform 3 and isoform 6.
VSP_004155
Alternative sequence6601Missing in isoform 6.
VSP_043292
Natural variant3971H → R. Ref.2
Corresponds to variant rs6973420 [ dbSNP | Ensembl ].
VAR_065254

Experimental info

Sequence conflict5301V → M in AAA35636. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (H-CAD) [UniParc].

Last modified June 28, 2011. Version 3.
Checksum: 7468E2C3E40BF697

FASTA79393,231
        10         20         30         40         50         60 
MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL RQKQEEESLG 

        70         80         90        100        110        120 
QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL ARREERRQKR LQEALERQKE 

       130        140        150        160        170        180 
FDPTITDASL SLPSRRMQND TAENETTEKE EKSESRQERY EIEETETVTK SYQKNDWRDA 

       190        200        210        220        230        240 
EENKKEDKEK EEEEEEKPKR GSIGENQVEV MVEEKTTESQ EETVVMSLKN GQISSEEPKQ 

       250        260        270        280        290        300 
EEEREQGSDE ISHHEKMEEE DKERAEAERA RLEAEERERI KAEQDKKIAD ERARIEAEEK 

       310        320        330        340        350        360 
AAAQERERRE AEERERMREE EKRAAEERQR IKEEEKRAAE ERQRIKEEEK RAAEERQRIK 

       370        380        390        400        410        420 
EEEKRAAEER QRARAEEEEK AKVEEQKRNK QLEEKKHAMQ ETKIKGEKVE QKIEGKWVNE 

       430        440        450        460        470        480 
KKAQEDKLQT AVLKKQGEEK GTKVQAKREK LQEDKPTFKK EEIKDEKIKK DKEPKEEVKS 

       490        500        510        520        530        540 
FMDRKKGFTE VKSQNGEFMT HKLKHTENTF SRPGGRASVD TKEAEGAPQV EAGKRLEELR 

       550        560        570        580        590        600 
RRRGETESEE FEKLKQKQQE AALELEELKK KREERRKVLE EEEQRRKQEE ADRKLREEEE 

       610        620        630        640        650        660 
KRRLKEEIER RRAEAAEKRQ KMPEDGLSDD KKPFKCFTPK GSSLKIEERA EFLNKSVQKS 

       670        680        690        700        710        720 
SGVKSTHQAA IVSKIDSRLE QYTSAIEGTK SAKPTKPAAS DLPVPAEGVR NIKSMWEKGN 

       730        740        750        760        770        780 
VFSSPTAAGT PNKETAGLKV GVSSRINEWL TKTPDGNKSP APKPSDLRPG DVSSKRNLWE 

       790 
KQSVDKVTSP TKV 

« Hide

Isoform 2 (WI-38 L-CAD I) [UniParc].

Checksum: 57791B75720D2902
Show »

FASTA56465,707
Isoform 3 (HELA L-CAD I) [UniParc].

Checksum: AA511974B9C483DC
Show »

FASTA55864,256
Isoform 4 (WI-38 L-CAD II) (1-CAD) [UniParc].

Checksum: 7EBF78B53217E77A
Show »

FASTA53862,663
Isoform 5 (HELA L-CAD II) [UniParc].

Checksum: 2A222B2C1AD79975
Show »

FASTA53261,213
Isoform 6 [UniParc].

Checksum: FF15BFCFCF19C248
Show »

FASTA56365,620

References

« Hide 'large scale' references
[1]"Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells."
Novy R.E., Lin J.L.-C., Lin J.J.-C.
J. Biol. Chem. 266:16917-16924(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Lung fibroblast.
[2]"Cloning of cDNAs encoding human caldesmons."
Humphrey M.B., Herrera-Sosa H., Gonzalez G., Lee R., Bryan J.
Gene 112:197-204(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), VARIANT ARG-397.
Tissue: Aorta.
[3]"Genomic structure of the human caldesmon gene."
Hayashi K., Yano H., Hashida T., Takeuchi R., Takeda O., Asada K., Takahashi E., Kato I., Sobue K.
Proc. Natl. Acad. Sci. U.S.A. 89:12122-12126(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
[4]"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. expand/collapse author list , 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 6).
Tissue: Amygdala.
[5]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 4).
Tissue: Skin.
[7]"Identification of functioning regulatory sites and a new myosin binding site in the C-terminal 288 amino acids of caldesmon expressed from a human clone."
Huber P.A.J., Redwood C.S., Avent N.D., Tanner M.J.A., Marston S.B.
J. Muscle Res. Cell Motil. 14:385-391(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 497-793, FUNCTION.
Tissue: Fetal liver.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-730, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-730, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-730; THR-753 AND SER-789, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-730 AND THR-753, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; TYR-21 AND SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-643 AND SER-789, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64110 mRNA. Translation: AAA35636.1.
M83216 mRNA. Translation: AAA58420.1.
M83216 mRNA. Translation: AAA58419.1.
D90452 mRNA. Translation: BAA14418.1.
D90453 mRNA. Translation: BAA14419.1.
AK289686 mRNA. Translation: BAF82375.1.
AC019014 Genomic DNA. No translation available.
AC083870 Genomic DNA. No translation available.
BC040354 mRNA. Translation: AAH40354.1.
CCDSCCDS47716.1. [Q05682-3]
CCDS47717.1. [Q05682-5]
CCDS5834.1. [Q05682-4]
CCDS5835.1. [Q05682-1]
CCDS5836.2. [Q05682-6]
PIRJH0628.
RefSeqNP_004333.1. NM_004342.6. [Q05682-4]
NP_149129.2. NM_033138.3. [Q05682-1]
NP_149130.1. NM_033139.3. [Q05682-3]
NP_149131.1. NM_033140.3. [Q05682-5]
NP_149347.2. NM_033157.3. [Q05682-6]
UniGeneHs.490203.

3D structure databases

ProteinModelPortalQ05682.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107251. 25 interactions.
IntActQ05682. 7 interactions.
STRING9606.ENSP00000354826.

PTM databases

PhosphoSiteQ05682.

Polymorphism databases

DMDM338817891.

2D gel databases

OGPQ05682.

Proteomic databases

MaxQBQ05682.
PaxDbQ05682.
PRIDEQ05682.

Protocols and materials databases

DNASU800.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361388; ENSP00000355000; ENSG00000122786. [Q05682-2]
ENST00000361675; ENSP00000354826; ENSG00000122786. [Q05682-1]
ENST00000361901; ENSP00000354513; ENSG00000122786. [Q05682-4]
ENST00000393118; ENSP00000376826; ENSG00000122786. [Q05682-3]
ENST00000417172; ENSP00000398826; ENSG00000122786. [Q05682-4]
ENST00000422748; ENSP00000395710; ENSG00000122786. [Q05682-6]
ENST00000424922; ENSP00000393621; ENSG00000122786. [Q05682-5]
GeneID800.
KEGGhsa:800.
UCSCuc003vrz.3. human. [Q05682-1]
uc003vsb.3. human. [Q05682-4]
uc003vsc.3. human. [Q05682-3]
uc003vsd.3. human. [Q05682-5]
uc010lmm.3. human. [Q05682-6]

Organism-specific databases

CTD800.
GeneCardsGC07P134429.
HGNCHGNC:1441. CALD1.
HPACAB000006.
HPA008066.
HPA017330.
MIM114213. gene.
neXtProtNX_Q05682.
PharmGKBPA26034.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253189.
HOGENOMHOG000013012.
HOVERGENHBG050785.
InParanoidQ05682.
KOK12327.
OMATHKLKHA.
OrthoDBEOG7FNC7W.
PhylomeDBQ05682.
TreeFamTF331771.

Enzyme and pathway databases

ReactomeREACT_17044. Muscle contraction.

Gene expression databases

ArrayExpressQ05682.
BgeeQ05682.
CleanExHS_CAD.
HS_CALD1.
GenevestigatorQ05682.

Family and domain databases

InterProIPR006017. Caldesmon.
IPR006018. Caldesmon_LSP.
[Graphical view]
PANTHERPTHR18949. PTHR18949. 1 hit.
PTHR18949:SF0. PTHR18949:SF0. 1 hit.
PfamPF02029. Caldesmon. 2 hits.
[Graphical view]
PRINTSPR01076. CALDESMON.
ProtoNetSearch...

Other

ChiTaRSCALD1. human.
GeneWikiCaldesmon.
GenomeRNAi800.
NextBio3252.
PROQ05682.
SOURCESearch...

Entry information

Entry nameCALD1_HUMAN
AccessionPrimary (citable) accession number: Q05682
Secondary accession number(s): A8K0X1 expand/collapse secondary AC list , Q13978, Q13979, Q14741, Q14742, Q9UD91
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM