CPLM-014128

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-014128

UniProt Accession

TUT7_HUMAN; Q5VYS8; Q5H9T0; Q5VYS5; Q5VYS7; Q658Z9; Q659A2; Q6MZJ3; Q8N5F0; Q96N57; Q96NE8; Q9C0F2; Q9H8M6

Genbank Protein ID

AL832026; AL832193; BX641077; CR933643; CR933644; CR936608; AL353678; AL137849; AL353678; AL137849; AL353678; AL137849; AL353678; AL137849; AL137849; AL353678; AL137849; AL353678; AL137849; AL353678; AL137849; AL353678; BC032456; AK023471; AK055546; AK055948; AB051498

Genbank Nucleotide ID

CAH56219.1; CAH56214.1; CAE46038.1; CAI45944.1; CAI45945.1; CAI56753.1; CAH71514.1; CAH71514.1; CAH71515.1; CAH71515.1; CAH71518.1; CAH71518.1; CAH71519.1; CAH71519.1; CAI14918.1; CAI14918.1; CAI14919.1; CAI14919.1; CAI14920.1; CAI14920.1; CAI14921.1; CAI14921.1; AAH32456.1; BAB14584.1; BAB70951.1; BAB71052.1; BAB21802.1

Protein Name

Terminal uridylyltransferase 7

Protein Synonyms/Alias

TUTase 7; Zinc finger CCHC domain-containing protein 6

Gene Name

ZCCHC6

Gene Synonyms/Alias

HS2; KIAA1711; TUT7

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
11	TAKPYFVKRTKDRGT	ubiquitination	[1, 2, 3]
212	DESVLSTKELLGLQQ	ubiquitination	[4]
330	MENVFQHKLPDCSLR	ubiquitination	[2]
602	IEDPYSVKRNVARTL	ubiquitination	[1, 2, 3]

Reference

[1] 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]
[2] 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]
[3] 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]
[4] 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]

Functional Description

Uridylyltransferase that mediates the terminal uridylation of some specific RNAs. Not involved in uridylation of precursor let-7 (pre-let-7) miRNA. Does not play a role in replication-dependent histone mRNA degradation.

Sequence Annotation

DOMAIN 551 600 PAP-associated 1.
DOMAIN 1233 1286 PAP-associated 2.
ZN_FING 963 980 CCHC-type 1.
ZN_FING 1345 1362 CCHC-type 2.
ZN_FING 1451 1468 CCHC-type 3.
METAL 1058 1058 Magnesium or manganese; catalytic (By
METAL 1060 1060 Magnesium or manganese; catalytic (By
MOD_RES 57 57 Phosphothreonine.
MOD_RES 64 64 Phosphothreonine.
MOD_RES 132 132 Phosphoserine (By similarity).
MOD_RES 172 172 Phosphoserine.
MOD_RES 939 939 Phosphoserine.

Keyword

Alternative splicing; Complete proteome; Magnesium; Manganese; Metal-binding; Nucleotidyltransferase; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

1495 AA

Protein Sequence

MGDTAKPYFV KRTKDRGTMD DDDFRRGHPQ QDYLIIDDHA KGHGSKMEKG LQKKKITPGN 60
YGNTPRKGPC AVSSNPYAFK NPIYSQPAWM NDSHKDQSKR WLSDEHTGNS DNWREFKPGP 120
RIPVINRQRK DSFQENEDGY RWQDTRGCRT VRRLFHKDLT SLETTSEMEA GSPENKKQRS 180
RPRKPRKTRN EENEQDGDLE GPVIDESVLS TKELLGLQQA EERLKRDCID RLKRRPRNYP 240
TAKYTCRLCD VLIESIAFAH KHIKEKRHKK NIKEKQEEEL LTTLPPPTPS QINAVGIAID 300
KVVQEFGLHN ENLEQRLEIK RIMENVFQHK LPDCSLRLYG SSCSRLGFKN SDVNIDIQFP 360
AIMSQPDVLL LVQECLKNSD SFIDVDADFH ARVPVVVCRE KQSGLLCKVS AGNENACLTT 420
KHLTALGKLE PKLVPLVIAF RYWAKLCSID RPEEGGLPPY VFALMAIFFL QQRKEPLLPV 480
YLGSWIEGFS LSKLGNFNLQ DIEKDVVIWE HTDSAAGDTG ITKEEAPRET PIKRGQVSLI 540
LDVKHQPSVP VGQLWVELLR FYALEFNLAD LVISIRVKEL VSRELKDWPK KRIAIEDPYS 600
VKRNVARTLN SQPVFEYILH CLRTTYKYFA LPHKITKSSL LKPLNAITCI SEHSKEVINH 660
HPDVQTKDDK LKNSVLAQGP GATSSAANTC KVQPLTLKET AESFGSPPKE EMGNEHISVH 720
PENSDCIQAD VNSDDYKGDK VYHPETGRKN EKEKVGRKGK HLLTVDQKRG EHVVCGSTRN 780
NESESTLDLE GFQNPTAKEC EGLATLDNKA DLDGESTEGT EELEDSLNHF THSVQGQTSE 840
MIPSDEEEED DEEEEEEEEP RLTINQREDE DGMANEDELD NTYTGSGDED ALSEEDDELG 900
EAAKYEDVKE CGKHVERALL VELNKISLKE ENVCEEKNSP VDQSDFFYEF SKLIFTKGKS 960
PTVVCSLCKR EGHLKKDCPE DFKRIQLEPL PPLTPKFLNI LDQVCIQCYK DFSPTIIEDQ 1020
AREHIRQNLE SFIRQDFPGT KLSLFGSSKN GFGFKQSDLD VCMTINGLET AEGLDCVRTI 1080
EELARVLRKH SGLRNILPIT TAKVPIVKFF HLRSGLEVDI SLYNTLALHN TRLLSAYSAI 1140
DPRVKYLCYT MKVFTKMCDI GDASRGSLSS YAYTLMVLYF LQQRNPPVIP VLQEIYKGEK 1200
KPEIFVDGWN IYFFDQIDEL PTYWSECGKN TESVGQLWLG LLRFYTEEFD FKEHVISIRR 1260
KSLLTTFKKQ WTSKYIVIED PFDLNHNLGA GLSRKMTNFI MKAFINGRRV FGIPVKGFPK 1320
DYPSKMEYFF DPDVLTEGEL APNDRCCRIC GKIGHFMKDC PMRRKVRRRR DQEDALNQRY 1380
PENKEKRSKE DKEIHNKYTE REVSTKEDKP IQCTPQKAKP MRAAADLGRE KILRPPVEKW 1440
KRQDDKDLRE KRCFICGREG HIKKECPQFK GSSGSLSSKY MTQGKASAKR TQQES 1495

Gene Ontology

GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
GO:0008270; F:zinc ion binding; IEA:InterPro.
GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.

Interpro

IPR002058; PAP_assoc.
IPR001878; Znf_CCHC.

Pfam

PF03828; PAP_assoc
PF00098; zf-CCHC

SMART

SM00343; ZnF_C2HC

PROSITE

PS50158; ZF_CCHC
PS00028; ZINC_FINGER_C2H2_1

PRINTS