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Protein

Protein polyglycylase TTLL10

Gene

Ttll10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Polyglycylase 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. Polyglycylates alpha-tubulin and beta-tubulin, but is not able to initiate glycylation and only has activity toward monoglycylated tubulin. Has the ability to polyglycylate non-tubulin proteins such as NAP1; in this case it can initiate glycylation and does not require preliminary monoglycylation by another glycylase (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei366 – 3661ATPBy similarity
Binding sitei368 – 3681ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi353 – 3564ATP bindingBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein polyglycylase TTLL10 (EC:6.3.2.-)
Alternative name(s):
Tubulin--tyrosine ligase-like protein 10
Gene namesi
Name:Ttll10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1560839. Ttll10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 679679Protein polyglycylase TTLL10PRO_0000324523Add
BLAST

Proteomic databases

PaxDbiQ5XI57.
PRIDEiQ5XI57.

PTM databases

PhosphoSiteiQ5XI57.

Expressioni

Gene expression databases

ExpressionAtlasiQ5XI57. baseline.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063596.

Structurei

3D structure databases

ProteinModelPortaliQ5XI57.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini172 – 543372TTLPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi592 – 5954Poly-Ser

Sequence similaritiesi

Contains 1 TTL domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2157. Eukaryota.
ENOG410XQDM. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000049156.
HOVERGENiHBG108614.
InParanoidiQ5XI57.
OMAiIMSHCFL.
OrthoDBiEOG7XDBF8.
PhylomeDBiQ5XI57.
TreeFamiTF329363.

Family and domain databases

InterProiIPR004344. TTL/TTLL_fam.
IPR027752. TTLL10.
[Graphical view]
PANTHERiPTHR12241:SF110. PTHR12241:SF110. 1 hit.
PfamiPF03133. TTL. 1 hit.
[Graphical view]
PROSITEiPS51221. TTL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5XI57-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPLHPPARRP HGHRRNGSEA QTEATTQDTG RLSCPRRVGA AVCPIQGLGH
60 70 80 90 100
RAARRPRRGV GTTSASRAPR PGALMPATRN RPRFIHYRVQ PPRTHVSFKR
110 120 130 140 150
PKRSRTHQSH TKVPGWTHEK RMGSSVEEGL RPELSQLEQD ADNLGEEEAA
160 170 180 190 200
RLPVTSLNGL LMEGDRHPNP GQGPFFYIGG TNGASIISNY CESKGWQRTQ
210 220 230 240 250
DSRCEDYKLK WCEIKCRDNY CSFREGQQLL FQLPNNKLLT TKIGLLSALR
260 270 280 290 300
EHARTLSKAR LMPSTQAKVL KMDEFFPETY RLDIRDERQA FFTLFDETQM
310 320 330 340 350
WICKPTASNQ GKGIFLIRSQ EEAAALQAKT QSIEDDPIYR KMPFRAPQAR
360 370 380 390 400
VVQRYVQNPL LLDGKKFDVR SYMLIACAMP YMVFFGHGYA RLTLSLYNPH
410 420 430 440 450
SSDLSGHLTN QFMQKKSPLY MLLKDSTVWS MEHLNRYIND KFRKSKGLPR
460 470 480 490 500
DWVFTTFTKR MQQIMSHCFL AVKSKLECKL GYFDLIGCDF LIDENFKVWL
510 520 530 540 550
LEMNSNPALH TNCEVLKEVI PGVVMETLDL ALETCQKSLH SQKMLPLQSQ
560 570 580 590 600
RRFVLLYNGE TTDLWPRLGS SRPPIRLPYA NSNHARSTCE ISSSSLTSTR
610 620 630 640 650
VTIADRPAAR KSMSSRTAPI CASRKSRLSD SGGVSIEESE TSVCSGLPEG
660 670
SRDAAREPSL GPTEEEREEE QRSTSHRGS
Length:679
Mass (Da):77,081
Last modified:March 18, 2008 - v2
Checksum:i1BA32BE272AD19EF
GO
Isoform 2 (identifier: Q5XI57-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.

Show »
Length:558
Mass (Da):63,453
Checksum:i830DBD11C06C8977
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 121121Missing in isoform 2. 1 PublicationVSP_032266Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03041793 Genomic DNA. No translation available.
BC083833 mRNA. Translation: AAH83833.1.
BC097417 mRNA. Translation: AAH97417.1.
RefSeqiNP_001019929.1. NM_001024758.2. [Q5XI57-2]
NP_001164004.1. NM_001170533.1.
XP_006239624.1. XM_006239562.2. [Q5XI57-2]
XP_008762579.1. XM_008764357.1. [Q5XI57-1]
UniGeneiRn.139876.

Genome annotation databases

EnsembliENSRNOT00000055319; ENSRNOP00000052187; ENSRNOG00000020132. [Q5XI57-2]
GeneIDi298692.
KEGGirno:298692.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03041793 Genomic DNA. No translation available.
BC083833 mRNA. Translation: AAH83833.1.
BC097417 mRNA. Translation: AAH97417.1.
RefSeqiNP_001019929.1. NM_001024758.2. [Q5XI57-2]
NP_001164004.1. NM_001170533.1.
XP_006239624.1. XM_006239562.2. [Q5XI57-2]
XP_008762579.1. XM_008764357.1. [Q5XI57-1]
UniGeneiRn.139876.

3D structure databases

ProteinModelPortaliQ5XI57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063596.

PTM databases

PhosphoSiteiQ5XI57.

Proteomic databases

PaxDbiQ5XI57.
PRIDEiQ5XI57.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000055319; ENSRNOP00000052187; ENSRNOG00000020132. [Q5XI57-2]
GeneIDi298692.
KEGGirno:298692.

Organism-specific databases

CTDi254173.
RGDi1560839. Ttll10.

Phylogenomic databases

eggNOGiKOG2157. Eukaryota.
ENOG410XQDM. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000049156.
HOVERGENiHBG108614.
InParanoidiQ5XI57.
OMAiIMSHCFL.
OrthoDBiEOG7XDBF8.
PhylomeDBiQ5XI57.
TreeFamiTF329363.

Miscellaneous databases

NextBioi644199.
PROiQ5XI57.

Gene expression databases

ExpressionAtlasiQ5XI57. baseline.

Family and domain databases

InterProiIPR004344. TTL/TTLL_fam.
IPR027752. TTLL10.
[Graphical view]
PANTHERiPTHR12241:SF110. PTHR12241:SF110. 1 hit.
PfamiPF03133. TTL. 1 hit.
[Graphical view]
PROSITEiPS51221. TTL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-679 (ISOFORM 1).
    Tissue: Testis.

Entry informationi

Entry nameiTTL10_RAT
AccessioniPrimary (citable) accession number: Q5XI57
Secondary accession number(s): Q4V8F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: May 11, 2016
This is version 82 of the entry and version 2 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. 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.