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Q9H112 (CST11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Cystatin-11
Gene names
Name:CST11
Synonyms:CST8L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length138 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has antibacterial activity against the Gram-negative bacteria E.coli. May play a role in sperm maturation and fertilization. Ref.1

Subcellular location

Nucleus. Cytoplasm. Note: Nuclear and cytoplasmic in the epididymis. Localized to the postacrosomal and tail regions of sperm. Probably localized to the outer surface of sperm. Ref.1

Tissue specificity

Detected in the epithelium and lumen of the epididymis, and in sperm (at protein level). Ref.1

Sequence similarities

Belongs to the cystatin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
Protease inhibitor
Thiol protease inhibitor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H112-1)

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: Q9H112-2)

The sequence of this isoform differs from the canonical sequence as follows:
     77-111: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 138112Cystatin-11
PRO_0000006658

Regions

Motif76 – 805Secondary area of contact Potential

Amino acid modifications

Glycosylation1321N-linked (GlcNAc...) Potential
Disulfide bond94 ↔ 102 By similarity
Disulfide bond115 ↔ 135 By similarity

Natural variations

Alternative sequence77 – 11135Missing in isoform 2.
VSP_001260

Sequences

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

Last modified September 27, 2005. Version 2.
Checksum: E49440ACA3585C64

FASTA13816,506
        10         20         30         40         50         60 
MMAEPWQALQ LLLAILLTLM ALPYQARKKT FLSVHEVMAV ENYAKDSLQW ITDQYNKESD 

        70         80         90        100        110        120 
DKYHFRIFRV LKVQRQVTDH LEYHLNVEMQ WTTCQKPETT NCVPQERELH KQVNCFFSVF 

       130 
AVPWFEQYKI LNKSCSSD 

« Hide

Isoform 2 [UniParc].

Checksum: 05DD92C47387B022
Show »

FASTA10312,285

References

« Hide 'large scale' references
[1]"Cystatin 11: a new member of the cystatin type 2 family."
Hamil K.G., Liu Q., Sivashanmugam P., Yenugu S., Soundararajan R., Grossman G., Richardson R.T., Zhang Y.-L., O'Rand M.G., Petrusz P., French F.S., Hall S.H.
Endocrinology 143:2787-2796(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[4]"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] (ISOFORMS 1 AND 2).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF335480 mRNA. Translation: AAL71991.1.
AF335481 mRNA. Translation: AAL71992.1.
AL096677 Genomic DNA. Translation: CAI20158.1.
AL096677 Genomic DNA. Translation: CAI20159.1.
CH471133 Genomic DNA. Translation: EAX10146.1.
BC121079 mRNA. Translation: AAI21080.1.
BC121080 mRNA. Translation: AAI21081.1.
RefSeqNP_543020.2. NM_080830.2.
NP_570612.1. NM_130794.1.
UniGeneHs.128100.

3D structure databases

ProteinModelPortalQ9H112.
SMRQ9H112. Positions 47-135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126748. 1 interaction.
STRING9606.ENSP00000366208.

Protein family/group databases

MEROPSI25.027.

PTM databases

PhosphoSiteQ9H112.

Polymorphism databases

DMDM76803548.

Proteomic databases

PaxDbQ9H112.
PRIDEQ9H112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377007; ENSP00000366206; ENSG00000125831. [Q9H112-2]
ENST00000377009; ENSP00000366208; ENSG00000125831. [Q9H112-1]
GeneID140880.
KEGGhsa:140880.
UCSCuc002wtf.1. human. [Q9H112-1]
uc002wtg.1. human. [Q9H112-2]

Organism-specific databases

CTD140880.
GeneCardsGC20M023379.
HGNCHGNC:15959. CST11.
HPAHPA053399.
MIM609731. gene.
neXtProtNX_Q9H112.
PharmGKBPA26974.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47633.
HOGENOMHOG000231754.
HOVERGENHBG096361.
InParanoidQ9H112.
KOK13906.
OMAEMRRTTC.
OrthoDBEOG7M98J9.
PhylomeDBQ9H112.

Gene expression databases

BgeeQ9H112.
CleanExHS_CST11.
GenevestigatorQ9H112.

Family and domain databases

InterProIPR027214. Cystatin.
IPR000010. Prot_inh_cystat.
[Graphical view]
PANTHERPTHR11413. PTHR11413. 1 hit.
PfamPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTSM00043. CY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCST11.
GenomeRNAi140880.
NextBio84520.
PROQ9H112.
SOURCESearch...

Entry information

Entry nameCST11_HUMAN
AccessionPrimary (citable) accession number: Q9H112
Secondary accession number(s): Q0VAF2 expand/collapse secondary AC list , Q0VAF3, Q8WXU5, Q8WXU6, Q9H113
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 106 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

MIM cross-references

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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM