UniProt Accession

 SPIN1_HUMAN; Q9Y657; A8K0X6; B3KRQ4; Q7KZJ8; Q9GZT2; Q9H0N7 

Genbank Protein ID

 AF106682; AF087864; AF317228; AL136719; BT007314; AK092017; AK289691; AK290009; AK315854; AL353748; CH471089; BC013571; BC114515; BC114565; CR533484 

Genbank Nucleotide ID

 AAD43035.1; AAG48367.1; AAG38112.1; CAB66653.1; AAP35978.1; BAG52466.1; BAF82380.1; BAF82698.1; BAF98745.1; CAH72406.1; EAW62753.1; AAI14516.1; AAI14566.1; CAG38515.1 

Protein Name

 Spindlin-1 

Protein Synonyms/Alias

 Ovarian cancer-related protein 

Gene Name

 SPIN1 

Gene Synonyms/Alias

 OCR; SPIN 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
7	*MKTPFGKTPGQRSR	acetylation	[1, 2]
44	RSSVGPSKPVSQPRR	acetylation	[3]
63	CRIQHGWKEGNGPVT	ubiquitination	[4, 5]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 May play a role in cell-cycle regulation during the transition from gamete to embryo (By similarity). 

Sequence Annotation

 REGION 53 116 Tudor-like domain 1.
 REGION 132 193 Tudor-like domain 2.
 REGION 213 262 Tudor-like domain 3.
 MOD_RES 124 124 Phosphoserine.
 MOD_RES 199 199 Phosphoserine.  

Keyword

 3D-structure; Cell cycle; Complete proteome; Developmental protein; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 262 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; IDA:LIFEdb.
 GO:0005819; C:spindle; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0007276; P:gamete generation; IEA:InterPro.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. 

Interpro

 IPR003671; Spin_Ssty. 

Pfam

 PF02513; Spin-Ssty 

SMART

  

PROSITE

  

PRINTS