CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017023
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger CCCH domain-containing protein 7A 
Protein Synonyms/Alias
  
Gene Name
 ZC3H7A 
Gene Synonyms/Alias
 ZC3H7; ZC3HDC7; HSPC055 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
85SEEILIPKEIIEKLYubiquitination[1]
90IPKEIIEKLYINRIAubiquitination[1]
124SLNASNCKALYRKSKubiquitination[1]
131KALYRKSKALSDLGRubiquitination[1]
140LSDLGRYKKAYDAVAubiquitination[1]
141SDLGRYKKAYDAVAKubiquitination[1]
148KAYDAVAKCSLAVPQubiquitination[1]
169LTQELAQKLGFKIRKubiquitination[1]
186VRAELSLKSVPGDGAubiquitination[1]
195VPGDGATKALNHSVEubiquitination[1]
425FFGSAVTKPSSSVTPubiquitination[1, 2, 3, 4, 5, 6]
452ACQICFVKSGPKLMDubiquitination[4]
456CFVKSGPKLMDFTYHubiquitination[1]
471ANIDHKCKKDILIGRubiquitination[1]
472NIDHKCKKDILIGRIubiquitination[1]
507EGPYYICKDVAAEEEubiquitination[1]
600ACSHPVTKHEFEDNKubiquitination[1]
607KHEFEDNKCLVHILRubiquitination[1]
709GFLNMKIKFVCAQCLubiquitination[1]
726GQVIEPDKNRKYCSAubiquitination[1]
729IEPDKNRKYCSAKARubiquitination[1]
766IRPLPTKKQMPLQFDubiquitination[1]
783NHIASGKKCQYVGNCubiquitination[1, 4]
870GKNCNSEKQWQGHISubiquitination[1]
882HISSEKHKEKVFHTEubiquitination[1]
884SSEKHKEKVFHTEDDubiquitination[1]
962PNDNDFGKYSFLFKDubiquitination[1, 4]
968GKYSFLFKDLN****ubiquitination[1, 4]
Reference
 [1] 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]
 [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] 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]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] 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
  
Sequence Annotation
 REPEAT 43 76 TPR 1.
 REPEAT 89 122 TPR 2.
 REPEAT 124 156 TPR 3.
 ZN_FING 634 656 C3H1-type 1.
 ZN_FING 769 797 C3H1-type 2.
 ZN_FING 857 881 C2H2-type.
 ZN_FING 906 928 C3H1-type 3.  
Keyword
 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat; TPR repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 971 AA 
Protein Sequence
MSNVSEERRK RQQNIKEGLQ FIQSPLSYPG TQEQYAVYLR ALVRNLFNEG NDVYREHDWN 60
NSISQYTEAL NIADYAKSEE ILIPKEIIEK LYINRIACYS NMGFHDKVLE DCNIVLSLNA 120
SNCKALYRKS KALSDLGRYK KAYDAVAKCS LAVPQDEHVI KLTQELAQKL GFKIRKAYVR 180
AELSLKSVPG DGATKALNHS VEDIEPDLLT PRQEAVPVVS LPAPSFSHEV GSELASVPVM 240
PLTSILPLQV EESALPSAVL ANGGKMPFTM PEAFLDDGDM VLGDELDDLL DSAPETNETV 300
MPSALVRGPL QTASVSPSMP FSASLLGTLP IGARYAPPPS FSEFYPPLTS SLEDFCSSLN 360
SFSMSESKRD LSTSTSREGT PLNNSNSSLL LMNGPGSLFA SENFLGISSQ PRNDFGNFFG 420
SAVTKPSSSV TPRHPLEGTH ELRQACQICF VKSGPKLMDF TYHANIDHKC KKDILIGRIK 480
NVEDKSWKKI RPRPTKTNYE GPYYICKDVA AEEECRYSGH CTFAYCQEEI DVWTLERKGA 540
FSREAFFGGN GKINLTVFKL LQEHLGEFIF LCEKCFDHKP RMISKRNKDN STACSHPVTK 600
HEFEDNKCLV HILRETTVKY SKIRSFHGQC QLDLCRHEVR YGCLREDECF YAHSLVELKV 660
WIMQNETGIS HDAIAQESKR YWQNLEANVP GAQVLGNQIM PGFLNMKIKF VCAQCLRNGQ 720
VIEPDKNRKY CSAKARHSWT KDRRAMRVMS IERKKWMNIR PLPTKKQMPL QFDLCNHIAS 780
GKKCQYVGNC SFAHSPEERE VWTYMKENGI QDMEQFYELW LKSQKNEKSE DIASQSNKEN 840
GKQIHMPTDY AEVTVDFHCW MCGKNCNSEK QWQGHISSEK HKEKVFHTED DQYCWQHRFP 900
TGYFSICDRY MNGTCPEGNS CKFAHGNAEL HEWEERRDAL KMKLNKARKD HLIGPNDNDF 960
GKYSFLFKDL N 971 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR011990; TPR-like_helical.
 IPR015880; Znf_C2H2-like.
 IPR000571; Znf_CCCH. 
Pfam
 PF00642; zf-CCCH 
SMART
 SM00355; ZnF_C2H2
 SM00356; ZnF_C3H1 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION
 PS50103; ZF_C3H1
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS