UniProt Accession

 CYTB_HUMAN; P04080 

Genbank Protein ID

 U46692; L03558; AF208234; AP001752; BC003370; BC010532 

Genbank Nucleotide ID

 AAA99014.1; AAA35727.1; AAF44059.1; BAA95541.1; AAH03370.1; AAH10532.1 

Protein Name

 Cystatin-B 

Protein Synonyms/Alias

 CPI-B; Liver thiol proteinase inhibitor; Stefin-B 

Gene Name

 CSTB 

Gene Synonyms/Alias

 CST6; STFB 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
39	NKKFPVFKAVSFKSQ	ubiquitination	[1, 2, 3]
44	VFKAVSFKSQVVAGT	ubiquitination	[2]
78	QSLPHENKPLTLSNY	acetylation	[4]
78	QSLPHENKPLTLSNY	ubiquitination	[2, 3]
91	NYQTNKAKHDELTYF	acetylation	[4, 5, 6]
91	NYQTNKAKHDELTYF	ubiquitination	[7]

Reference

 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. 

Sequence Annotation

 MOTIF 46 50 Secondary area of contact.
 MOD_RES 1 1 N-acetylmethionine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Epilepsy; Nucleus; Protease inhibitor; Reference proteome; Thiol protease inhibitor. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 98 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
 GO:0008344; P:adult locomotory behavior; IEA:Compara.
 GO:0042981; P:regulation of apoptotic process; IEA:Compara. 

Interpro

 IPR000010; Prot_inh_cystat.
 IPR018073; Prot_inh_cystat_CS.
 IPR001713; Prot_inh_stefinA. 

Pfam

 PF00031; Cystatin 

SMART

 SM00043; CY 

PROSITE

 PS00287; CYSTATIN 

PRINTS

 PR00295; STEFINA.