CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015322
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inactive rhomboid protein 2 
Protein Synonyms/Alias
 iRhom2; Rhomboid 5 homolog 2; Rhomboid family member 2; Rhomboid veinlet-like protein 5; Rhomboid veinlet-like protein 6 
Gene Name
 RHBDF2 
Gene Synonyms/Alias
 IRHOM2; RHBDL5; RHBDL6 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
337DGVQIPLKEYGRAPVubiquitination[1, 2, 3, 4]
358KRIASKVKHFAFDRKubiquitination[3]
472DLIHLGAKFSPCIRKubiquitination[5]
573IWPDDITKWPICTEQubiquitination[5]
605RPCCIGTKGSCEITTubiquitination[5]
848FTSRFCEKYELDQVLubiquitination[5]
Reference
 [1] 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]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Rhomboid protease-like protein which has no protease activity but regulates the secretion of several ligands of the epidermal growth factor receptor. Indirectly activates the epidermal growth factor receptor signaling pathway and may thereby regulate sleep, cell survival, proliferation and migration (By similarity). 
Sequence Annotation
 MOD_RES 90 90 Phosphoserine.
 MOD_RES 113 113 Phosphoserine (By similarity).
 MOD_RES 117 117 Phosphoserine (By similarity).
 MOD_RES 323 323 Phosphoserine (By similarity).
 MOD_RES 325 325 Phosphoserine.
 MOD_RES 328 328 Phosphoserine.
 MOD_RES 387 387 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Disease mutation; Endoplasmic reticulum; Growth factor binding; Membrane; Palmoplantar keratoderma; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 856 AA 
Protein Sequence
MASADKNGGS VSSVSSSRLQ SRKPPNLSIT IPPPEKETQA PGEQDSMLPE GFQNRRLKKS 60
QPRTWAAHTT ACPPSFLPKR KNPAYLKSVS LQEPRSRWQE SSEKRPGFRR QASLSQSIRK 120
GAAQWFGVSG DWEGQRQQWQ RRSLHHCSMR YGRLKASCQR DLELPSQEAP SFQGTESPKP 180
CKMPKIVDPL ARGRAFRHPE EMDRPHAPHP PLTPGVLSLT SFTSVRSGYS HLPRRKRMSV 240
AHMSLQAAAA LLKGRSVLDA TGQRCRVVKR SFAFPSFLEE DVVDGADTFD SSFFSKEEMS 300
SMPDDVFESP PLSASYFRGI PHSASPVSPD GVQIPLKEYG RAPVPGPRRG KRIASKVKHF 360
AFDRKKRHYG LGVVGNWLNR SYRRSISSTV QRQLESFDSH RPYFTYWLTF VHVIITLLVI 420
CTYGIAPVGF AQHVTTQLVL RNKGVYESVK YIQQENFWVG PSSIDLIHLG AKFSPCIRKD 480
GQIEQLVLRE RDLERDSGCC VQNDHSGCIQ TQRKDCSETL ATFVKWQDDT GPPMDKSDLG 540
QKRTSGAVCH QDPRTCEEPA SSGAHIWPDD ITKWPICTEQ ARSNHTGFLH MDCEIKGRPC 600
CIGTKGSCEI TTREYCEFMH GYFHEEATLC SQVHCLDKVC GLLPFLNPEV PDQFYRLWLS 660
LFLHAGVVHC LVSVVFQMTI LRDLEKLAGW HRIAIIFILS GITGNLASAI FLPYRAEVGP 720
AGSQFGLLAC LFVELFQSWP LLERPWKAFL NLSAIVLFLF ICGLLPWIDN IAHIFGFLSG 780
LLLAFAFLPY ITFGTSDKYR KRALILVSLL AFAGLFAALV LWLYIYPINW PWIEHLTCFP 840
FTSRFCEKYE LDQVLH 856 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0050709; P:negative regulation of protein secretion; ISS:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0006508; P:proteolysis; IEA:InterPro. 
Interpro
 IPR002610; Peptidase_S54_rhomboid.
 IPR022764; Peptidase_S54_rhomboid_dom.
 IPR022241; Rhomboid_SP. 
Pfam
 PF01694; Rhomboid
 PF12595; Rhomboid_SP 
SMART
  
PROSITE
  
PRINTS