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Protein

Protein monoglycylase TTLL8

Gene

Ttll8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei448 – 4481ATPBy similarity
Binding sitei450 – 4501ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi435 – 4384ATP bindingBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein-glycine ligase activity Source: UniProtKB
  • protein-glycine ligase activity, initiating Source: UniProtKB

GO - Biological processi

  • cilium assembly Source: MGI
  • protein polyglycylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein monoglycylase TTLL8 (EC:6.3.2.-)
Alternative name(s):
Tubulin--tyrosine ligase-like protein 8
Gene namesi
Name:Ttll8Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1922902. Ttll8.

Subcellular locationi

GO - Cellular componenti

  • axoneme Source: UniProtKB
  • cilium Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: UniProtKB-KW
  • microtubule cytoskeleton Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 832832Protein monoglycylase TTLL8PRO_0000326164Add
BLAST

Proteomic databases

PaxDbiA4Q9F1.
PRIDEiA4Q9F1.

PTM databases

PhosphoSiteiA4Q9F1.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis.1 Publication

Gene expression databases

BgeeiA4Q9F1.
CleanExiMM_TTLL8.
ExpressionAtlasiA4Q9F1. baseline.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000104996.

Structurei

3D structure databases

ProteinModelPortaliA4Q9F1.
SMRiA4Q9F1. Positions 392-612.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 624354TTLPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 TTL domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2157. Eukaryota.
ENOG410XQDM. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000154711.
HOVERGENiHBG069401.
InParanoidiA4Q9F1.
KOiK16608.
OMAiYGHYPVV.
OrthoDBiEOG7RBZ7P.
PhylomeDBiA4Q9F1.
TreeFamiTF313087.

Family and domain databases

InterProiIPR004344. TTL/TTLL_fam.
[Graphical view]
PfamiPF03133. TTL. 1 hit.
[Graphical view]
PROSITEiPS51221. TTL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4Q9F1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCPPTPNPP FRPPSHTRVL RTPPLPPWVC LNSKSLSTGV GGQKNQLREA
60 70 80 90 100
SMENGERKKL SSTLSDGDHK EENKLKQGIP QDLSSSPKLD RYKIARQLTE
110 120 130 140 150
KAIKERKIFS IYGHYPVIRA TLRRKGWVEK KFNFFPKALQ NLGSEDKSAE
160 170 180 190 200
TKENQEIALE RFDDIHDVMS RLVKNEIPYL LWTIKRDVVD YHSLTCDQML
210 220 230 240 250
NHYGKTASFT TKIGLCLNMR SLPWYVQANP NTFFPRCYGL CTESEKQEFL
260 270 280 290 300
DDFRRTVAAS ILKWVVLHQN YCSKVKGKSK KEEAKNSDPS PKKDPENPDL
310 320 330 340 350
KLPSLSGQVV DTACKVCQAY LGQLEHEDID VSEASTEALS EEEWNDLTQQ
360 370 380 390 400
YYLLVHGNAS ITDSKSYFAQ CQALLSKISS VNPQTEIDGI RNIWIIKPAA
410 420 430 440 450
KSRGRDIVCM DRVENILSLV AADSQTTKDN KWVVQKYIET PMLIYDTKFD
460 470 480 490 500
IRQWFLVTDW NPLTIWFYKE SYLRFSTQRF SLDKLDSAIH LCNNSIQRRL
510 520 530 540 550
KNDKERSPLL PCHNMWTSTR FQEYLQKRGR GGTWGSIIYP SMKRAVTNAM
560 570 580 590 600
RVAQDHVEAR KNSFELYGAD FILGRDFKPW LIEINSSPTM HPSTPVTAQL
610 620 630 640 650
CAQVQEDTIK VVVDRKLDRN CDIGNFELLW RQPAVELPPF NGSDLCVEGI
660 670 680 690 700
SVKKAKKQMP PIASVGLSES LLDAPPKVRS ARALMETVIR PPRTTVRQDW
710 720 730 740 750
KREEAKVLST TWSMPVMDAE VRGRAKPIYA FEVNDYQHVD NKSHKSGYTR
760 770 780 790 800
VQSSKVPGVT LTSAQHPALF AQTMKPTQMT SSPPPTASGN HRDSSPFCPI
810 820 830
VFEELWLHPN SQRRPSSCIL QSRAQGWIRG IP
Length:832
Mass (Da):94,915
Last modified:May 15, 2007 - v1
Checksum:i086956A17633B1D7
GO

Sequence cautioni

The sequence AAI16294.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI16295.1 differs from that shown. Reason: Frameshift at position 170. Curated
The sequence BAC26811.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM690752 mRNA. Translation: CAM84329.1.
AK030151 mRNA. Translation: BAC26811.1. Different initiation.
BC116293 mRNA. Translation: AAI16294.1. Different initiation.
BC116294 mRNA. Translation: AAI16295.1. Frameshift.
CCDSiCCDS27735.2.
RefSeqiNP_766406.2. NM_172818.3.
XP_006521019.1. XM_006520956.2.
XP_006521020.1. XM_006520957.2.
UniGeneiMm.479911.
Mm.86807.

Genome annotation databases

EnsembliENSMUST00000109371; ENSMUSP00000104996; ENSMUSG00000022388.
GeneIDi239591.
KEGGimmu:239591.
UCSCiuc007xet.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM690752 mRNA. Translation: CAM84329.1.
AK030151 mRNA. Translation: BAC26811.1. Different initiation.
BC116293 mRNA. Translation: AAI16294.1. Different initiation.
BC116294 mRNA. Translation: AAI16295.1. Frameshift.
CCDSiCCDS27735.2.
RefSeqiNP_766406.2. NM_172818.3.
XP_006521019.1. XM_006520956.2.
XP_006521020.1. XM_006520957.2.
UniGeneiMm.479911.
Mm.86807.

3D structure databases

ProteinModelPortaliA4Q9F1.
SMRiA4Q9F1. Positions 392-612.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000104996.

PTM databases

PhosphoSiteiA4Q9F1.

Proteomic databases

PaxDbiA4Q9F1.
PRIDEiA4Q9F1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000109371; ENSMUSP00000104996; ENSMUSG00000022388.
GeneIDi239591.
KEGGimmu:239591.
UCSCiuc007xet.2. mouse.

Organism-specific databases

CTDi164714.
MGIiMGI:1922902. Ttll8.

Phylogenomic databases

eggNOGiKOG2157. Eukaryota.
ENOG410XQDM. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000154711.
HOVERGENiHBG069401.
InParanoidiA4Q9F1.
KOiK16608.
OMAiYGHYPVV.
OrthoDBiEOG7RBZ7P.
PhylomeDBiA4Q9F1.
TreeFamiTF313087.

Miscellaneous databases

NextBioi384189.
PROiA4Q9F1.
SOURCEiSearch...

Gene expression databases

BgeeiA4Q9F1.
CleanExiMM_TTLL8.
ExpressionAtlasiA4Q9F1. baseline.

Family and domain databases

InterProiIPR004344. TTL/TTLL_fam.
[Graphical view]
PfamiPF03133. TTL. 1 hit.
[Graphical view]
PROSITEiPS51221. TTL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A targeted multienzyme mechanism for selective microtubule polyglutamylation."
    van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.
    Mol. Cell 26:437-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6JImported.
    Tissue: TestisImported.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: TestisImported.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-832.
  4. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
    Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  5. "TTLL10 can perform tubulin glycylation when co-expressed with TTLL8."
    Ikegami K., Setou M.
    FEBS Lett. 583:1957-1963(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTTLL8_MOUSE
AccessioniPrimary (citable) accession number: A4Q9F1
Secondary accession number(s): Q14B76, Q8C0N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 15, 2007
Last modified: May 11, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.