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Q9Y6Q1

- CAN6_HUMAN

UniProt

Q9Y6Q1 - CAN6_HUMAN

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Protein

Calpain-6

Gene

CAPN6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. calcium-dependent cysteine-type endopeptidase activity Source: RefGenome
  2. microtubule binding Source: UniProtKB

GO - Biological processi

  1. microtubule bundle formation Source: UniProtKB
  2. proteolysis Source: RefGenome
  3. regulation of cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Protein family/group databases

MEROPSiC02.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-6
Alternative name(s):
Calpain-like protease X-linked
Calpamodulin
Short name:
CalpM
Gene namesi
Name:CAPN6
Synonyms:CALPM, CANPX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:1483. CAPN6.

Subcellular locationi

Cytoplasmperinuclear region 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication
Note: During mitose associated with the mitotic spindle. At telophase colocalized to the midbody spindle.

GO - Cellular componenti

  1. perinuclear region of cytoplasm Source: UniProtKB
  2. spindle microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26063.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 641641Calpain-6PRO_0000207717Add
BLAST

Proteomic databases

PaxDbiQ9Y6Q1.
PRIDEiQ9Y6Q1.

PTM databases

PhosphoSiteiQ9Y6Q1.

Expressioni

Tissue specificityi

Expressed only in placenta.

Gene expression databases

BgeeiQ9Y6Q1.
CleanExiHS_CAPN6.
ExpressionAtlasiQ9Y6Q1. baseline and differential.
GenevestigatoriQ9Y6Q1.

Organism-specific databases

HPAiHPA040383.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9Y6Q1. 1 interaction.
MINTiMINT-195834.
STRINGi9606.ENSP00000317214.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6Q1.
SMRiQ9Y6Q1. Positions 8-489, 513-602.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 343318Calpain catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini518 – 620103C2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni344 – 495152Domain IIIAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated
Contains 1 C2 domain.Curated
Contains 1 calpain catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG258770.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232036.
HOVERGENiHBG001095.
InParanoidiQ9Y6Q1.
KOiK08575.
OMAiFCDQFLG.
OrthoDBiEOG75J0MJ.
PhylomeDBiQ9Y6Q1.
TreeFamiTF314748.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029540. CAPN6.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PANTHERiPTHR10183:SF281. PTHR10183:SF281. 1 hit.
PfamiPF00168. C2. 1 hit.
PF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00239. C2. 1 hit.
SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y6Q1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGPPLKLFKN QKYQELKQEC IKDSRLFCDP TFLPENDSLF YNRLLPGKVV
60 70 80 90 100
WKRPQDICDD PHLIVGNISN HQLTQGRLGH KPMVSAFSCL AVQESHWTKT
110 120 130 140 150
IPNHKEQEWD PQKTEKYAGI FHFRFWHFGE WTEVVIDDLL PTINGDLVFS
160 170 180 190 200
FSTSMNEFWN ALLEKAYAKL LGCYEALDGL TITDIIVDFT GTLAETVDMQ
210 220 230 240 250
KGRYTELVEE KYKLFGELYK TFTKGGLICC SIESPNQEEQ EVETDWGLLK
260 270 280 290 300
GHTYTMTDIR KIRLGERLVE VFSAEKVYMV RLRNPLGRQE WSGPWSEISE
310 320 330 340 350
EWQQLTASDR KNLGLVMSDD GEFWMSLEDF CRNFHKLNVC RNVNNPIFGR
360 370 380 390 400
KELESVLGCW TVDDDPLMNR SGGCYNNRDT FLQNPQYIFT VPEDGHKVIM
410 420 430 440 450
SLQQKDLRTY RRMGRPDNYI IGFELFKVEM NRKFRLHHLY IQERAGTSTY
460 470 480 490 500
IDTRTVFLSK YLKKGNYVLV PTMFQHGRTS EFLLRIFSEV PVQLRELTLD
510 520 530 540 550
MPKMSCWNLA RGYPKVVTQI TVHSAEDLEK KYANETVNPY LVIKCGKEEV
560 570 580 590 600
RSPVQKNTVH AIFDTQAIFY RRTTDIPIIV QVWNSRKFCD QFLGQVTLDA
610 620 630 640
DPSDCRDLKS LYLRKKGGPT AKVKQGHISF KVISSDDLTE L
Length:641
Mass (Da):74,576
Last modified:May 4, 2001 - v2
Checksum:iA48E5291169B1028
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421N → F in CAA04051. 1 PublicationCurated
Sequence conflicti415 – 4162RP → KT in AAB86605. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti277 – 2771V → L.1 Publication
Corresponds to variant rs12013711 [ dbSNP | Ensembl ].
VAR_021084
Natural varianti358 – 3581G → R in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036048
Natural varianti518 – 5181T → I.
Corresponds to variant rs12851517 [ dbSNP | Ensembl ].
VAR_051515

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14555.1.
RefSeqiNP_055104.2. NM_014289.3.
UniGeneiHs.496593.

Genome annotation databases

EnsembliENST00000324068; ENSP00000317214; ENSG00000077274.
GeneIDi827.
KEGGihsa:827.
UCSCiuc004epc.2. human.

Polymorphism databases

DMDMi13959315.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14555.1.
RefSeqi NP_055104.2. NM_014289.3.
UniGenei Hs.496593.

3D structure databases

ProteinModelPortali Q9Y6Q1.
SMRi Q9Y6Q1. Positions 8-489, 513-602.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9Y6Q1. 1 interaction.
MINTi MINT-195834.
STRINGi 9606.ENSP00000317214.

Protein family/group databases

MEROPSi C02.971.

PTM databases

PhosphoSitei Q9Y6Q1.

Polymorphism databases

DMDMi 13959315.

Proteomic databases

PaxDbi Q9Y6Q1.
PRIDEi Q9Y6Q1.

Protocols and materials databases

DNASUi 827.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324068 ; ENSP00000317214 ; ENSG00000077274 .
GeneIDi 827.
KEGGi hsa:827.
UCSCi uc004epc.2. human.

Organism-specific databases

CTDi 827.
GeneCardsi GC0XM110488.
HGNCi HGNC:1483. CAPN6.
HPAi HPA040383.
MIMi 300146. gene.
neXtProti NX_Q9Y6Q1.
PharmGKBi PA26063.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258770.
GeneTreei ENSGT00760000118971.
HOGENOMi HOG000232036.
HOVERGENi HBG001095.
InParanoidi Q9Y6Q1.
KOi K08575.
OMAi FCDQFLG.
OrthoDBi EOG75J0MJ.
PhylomeDBi Q9Y6Q1.
TreeFami TF314748.

Miscellaneous databases

ChiTaRSi CAPN6. human.
GenomeRNAii 827.
NextBioi 3404.
PROi Q9Y6Q1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6Q1.
CleanExi HS_CAPN6.
ExpressionAtlasi Q9Y6Q1. baseline and differential.
Genevestigatori Q9Y6Q1.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000008. C2_dom.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029540. CAPN6.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view ]
PANTHERi PTHR10183:SF281. PTHR10183:SF281. 1 hit.
Pfami PF00168. C2. 1 hit.
PF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view ]
PRINTSi PR00704. CALPAIN.
SMARTi SM00239. C2. 1 hit.
SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEi PS50203. CALPAIN_CAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-358.

Entry informationi

Entry nameiCAN6_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6Q1
Secondary accession number(s): D3DUY7, Q9UEQ1, Q9UJA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 4, 2001
Last modified: October 29, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3