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Q9Y6Q1 (CAN6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calpain-6
Alternative name(s):
Calpain-like protease X-linked
Calpamodulin
Short name=CalpM
Gene names
Name:CAPN6
Synonyms:CALPM, CANPX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues By similarity. Ref.8

Subunit structure

Interacts (via domain III) with microtubules By similarity. Interacts (via domain II) with ARHGEF2 (via the N-terminal zinc finger) By similarity. Ref.8

Subcellular location

Cytoplasmperinuclear region. Cytoplasmcytoskeletonspindle. Note: During mitose associated with the mitotic spindle. At telophase colocalized to the midbody spindle. Ref.8

Tissue specificity

Expressed only in placenta.

Sequence similarities

Belongs to the peptidase C2 family.

Contains 1 C2 domain.

Contains 1 calpain catalytic domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 641641Calpain-6
PRO_0000207717

Regions

Domain26 – 343318Calpain catalytic
Domain518 – 620103C2
Region344 – 495152Domain III

Natural variations

Natural variant2771V → L. Ref.4
Corresponds to variant rs12013711 [ dbSNP | Ensembl ].
VAR_021084
Natural variant3581G → R in a colorectal cancer sample; somatic mutation. Ref.9
VAR_036048
Natural variant5181T → I.
Corresponds to variant rs12851517 [ dbSNP | Ensembl ].
VAR_051515

Experimental info

Sequence conflict421N → F in CAA04051. Ref.3
Sequence conflict415 – 4162RP → KT in AAB86605. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Y6Q1 [UniParc].

Last modified May 4, 2001. Version 2.
Checksum: A48E5291169B1028

FASTA64174,576
        10         20         30         40         50         60 
MGPPLKLFKN QKYQELKQEC IKDSRLFCDP TFLPENDSLF YNRLLPGKVV WKRPQDICDD 

        70         80         90        100        110        120 
PHLIVGNISN HQLTQGRLGH KPMVSAFSCL AVQESHWTKT IPNHKEQEWD PQKTEKYAGI 

       130        140        150        160        170        180 
FHFRFWHFGE WTEVVIDDLL PTINGDLVFS FSTSMNEFWN ALLEKAYAKL LGCYEALDGL 

       190        200        210        220        230        240 
TITDIIVDFT GTLAETVDMQ KGRYTELVEE KYKLFGELYK TFTKGGLICC SIESPNQEEQ 

       250        260        270        280        290        300 
EVETDWGLLK GHTYTMTDIR KIRLGERLVE VFSAEKVYMV RLRNPLGRQE WSGPWSEISE 

       310        320        330        340        350        360 
EWQQLTASDR KNLGLVMSDD GEFWMSLEDF CRNFHKLNVC RNVNNPIFGR KELESVLGCW 

       370        380        390        400        410        420 
TVDDDPLMNR SGGCYNNRDT FLQNPQYIFT VPEDGHKVIM SLQQKDLRTY RRMGRPDNYI 

       430        440        450        460        470        480 
IGFELFKVEM NRKFRLHHLY IQERAGTSTY IDTRTVFLSK YLKKGNYVLV PTMFQHGRTS 

       490        500        510        520        530        540 
EFLLRIFSEV PVQLRELTLD MPKMSCWNLA RGYPKVVTQI TVHSAEDLEK KYANETVNPY 

       550        560        570        580        590        600 
LVIKCGKEEV RSPVQKNTVH AIFDTQAIFY RRTTDIPIIV QVWNSRKFCD QFLGQVTLDA 

       610        620        630        640 
DPSDCRDLKS LYLRKKGGPT AKVKQGHISF KVISSDDLTE L 

« Hide

References

« Hide 'large scale' references
[1]"A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution."
Dear T.N., Matena K., Vingron M., Boehm T.
Genomics 45:175-184(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Crotty P.L.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"A novel X-linked calpain-like protease."
Belsito A., Piluso G., Nigro V.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]NIEHS SNPs program
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-277.
[5]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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].
[7]"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].
Tissue: Placenta.
[8]"Calpain 6 is involved in microtubule stabilization and cytoskeletal organization."
Tonami K., Kurihara Y., Aburatani H., Uchijima Y., Asano T., Kurihara H.
Mol. Cell. Biol. 27:2548-2561(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH MICROTUBULE.
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-358.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029232 mRNA. Translation: AAB86605.1.
AJ000388 mRNA. Translation: CAA04051.1.
AY800242 Genomic DNA. Translation: AAV41896.1.
AL031117 Genomic DNA. Translation: CAA19965.1.
CH471120 Genomic DNA. Translation: EAX02650.1.
CH471120 Genomic DNA. Translation: EAX02651.1.
BC000730 mRNA. Translation: AAH00730.1.
CCDSCCDS14555.1.
RefSeqNP_055104.2. NM_014289.3.
UniGeneHs.496593.

3D structure databases

ProteinModelPortalQ9Y6Q1.
SMRQ9Y6Q1. Positions 8-489, 513-602.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Y6Q1. 1 interaction.
MINTMINT-195834.
STRING9606.ENSP00000317214.

Protein family/group databases

MEROPSC02.971.

PTM databases

PhosphoSiteQ9Y6Q1.

Polymorphism databases

DMDM13959315.

Proteomic databases

PaxDbQ9Y6Q1.
PRIDEQ9Y6Q1.

Protocols and materials databases

DNASU827.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324068; ENSP00000317214; ENSG00000077274.
GeneID827.
KEGGhsa:827.
UCSCuc004epc.2. human.

Organism-specific databases

CTD827.
GeneCardsGC0XM110488.
HGNCHGNC:1483. CAPN6.
HPAHPA040383.
MIM300146. gene.
neXtProtNX_Q9Y6Q1.
PharmGKBPA26063.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258770.
HOGENOMHOG000232036.
HOVERGENHBG001095.
InParanoidQ9Y6Q1.
KOK08575.
OMAFCDQFLG.
OrthoDBEOG75J0MJ.
PhylomeDBQ9Y6Q1.
TreeFamTF314748.

Gene expression databases

ArrayExpressQ9Y6Q1.
BgeeQ9Y6Q1.
CleanExHS_CAPN6.
GenevestigatorQ9Y6Q1.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSPR00704. CALPAIN.
SMARTSM00239. C2. 1 hit.
SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEPS50203. CALPAIN_CAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAPN6. human.
GenomeRNAi827.
NextBio3404.
PROQ9Y6Q1.
SOURCESearch...

Entry information

Entry nameCAN6_HUMAN
AccessionPrimary (citable) accession number: Q9Y6Q1
Secondary accession number(s): D3DUY7, Q9UEQ1, Q9UJA8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 4, 2001
Last modified: July 9, 2014
This is version 126 of the entry and version 2 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

Peptidase families

Classification of peptidase families and list of entries

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 X

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