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Protein

Tubulin polyglutamylase TTLL4

Gene

TTLL4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glutamylase which preferentially modifies beta-tubulin and non-tubulin proteins, such as NAP1L1, NAP1L4 and CGAS/MB21D1. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Involved in formation of short side-chains. Mediates initiation of polyglutamylation of nucleosome assembly proteins NAP1L1 and NAP1L4. Also acts as a monoglutamylase: generates monoglutamylation of CGAS/MB21D1, leading to impair the nucleotidyltransferase activity of CGAS/MB21D1.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei762 – 7621ATPBy similarity
Binding sitei764 – 7641ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi749 – 7524ATP bindingBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein-glutamic acid ligase activity Source: UniProtKB
  • tubulin binding Source: UniProtKB

GO - Biological processi

  • peptidyl-glutamic acid modification Source: UniProtKB
  • protein polyglutamylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin polyglutamylase TTLL4 (EC:6.-.-.-)
Alternative name(s):
Tubulin--tyrosine ligase-like protein 4
Gene namesi
Name:TTLL4
Synonyms:KIAA0173
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:28976. TTLL4.

Subcellular locationi

  • Cell projectioncilium By similarity
  • Cytoplasmcytoskeletoncilium basal body By similarity

  • Note: Located in cilia. In some cells, also found in basal bodies.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi978 – 9814KMKK → EMEE: Decreased binding to microtubules and polyglutamylase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134935712.

Polymorphism and mutation databases

BioMutaiTTLL4.
DMDMi143811470.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11991199Tubulin polyglutamylase TTLL4PRO_0000212442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei691 – 6911PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14679.
MaxQBiQ14679.
PaxDbiQ14679.
PeptideAtlasiQ14679.
PRIDEiQ14679.

PTM databases

iPTMnetiQ14679.
PhosphoSiteiQ14679.

Expressioni

Gene expression databases

BgeeiQ14679.
CleanExiHS_TTLL4.
ExpressionAtlasiQ14679. baseline and differential.
GenevisibleiQ14679. HS.

Organism-specific databases

HPAiHPA027091.
HPA050252.

Interactioni

GO - Molecular functioni

  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115012. 7 interactions.
IntActiQ14679. 2 interactions.
STRINGi9606.ENSP00000258398.

Structurei

3D structure databases

ProteinModelPortaliQ14679.
SMRiQ14679. Positions 658-912.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini604 – 947344TTLPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni918 – 1029112c-MTBD region1 PublicationAdd
BLAST

Domaini

The flexible c-MTBD (cationic microtubule binding domain) region mediates binding to microtubules. It is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding.By similarity1 Publication

Sequence similaritiesi

Belongs to the tubulin--tyrosine ligase family.Curated
Contains 1 TTL domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2156. Eukaryota.
ENOG410XTI2. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000154712.
HOVERGENiHBG058942.
InParanoidiQ14679.
KOiK16601.
OMAiYKPMLNN.
PhylomeDBiQ14679.
TreeFamiTF313087.

Family and domain databases

InterProiIPR004344. TTL/TTLL_fam.
IPR027748. TTLL-4.
[Graphical view]
PANTHERiPTHR12241:SF9. PTHR12241:SF9. 2 hits.
PfamiPF03133. TTL. 1 hit.
[Graphical view]
PROSITEiPS51221. TTL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14679-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAGTQHYS IGLRQKNSFK QSGPSGTVPA TPPEKPSEGR VWPQAHQQVK
60 70 80 90 100
PIWKLEKKQV ETLSAGLGPG LLGVPPQPAY FFCPSTLCSS GTTAVIAGHS
110 120 130 140 150
SSCYLHSLPD LFNSTLLYRR SSYRQKPYQQ LESFCLRSSP SEKSPFSLPQ
160 170 180 190 200
KSLPVSLTAN KATSSMVFSM AQPMASSSTE PYLCLAAAGE NPSGKSLASA
210 220 230 240 250
ISGKIPSPLS SSYKPMLNNN SFMWPNSTPV PLLQTTQGLK PVSPPKIQPV
260 270 280 290 300
SWHHSGGTGD CAPQPVDHKV PKSIGTVPAD ASAHIALSTA SSHDTSTTSV
310 320 330 340 350
ASSWYNRNNL AMRAEPLSCA LDDSSDSQDP TKEIRFTEAV RKLTARGFEK
360 370 380 390 400
MPRQGCQLEQ SSFLNPSFQW NVLNRSRRWK PPAVNQQFPQ EDAGSVRRVL
410 420 430 440 450
PGASDTLGLD NTVFCTKRIS IHLLASHASG LNHNPACESV IDSSAFGEGK
460 470 480 490 500
APGPPFPQTL GIANVATRLS SIQLGQSEKE RPEEARELDS SDRDISSATD
510 520 530 540 550
LQPDQAETED TEEELVDGLE DCCSRDENEE EEGDSECSSL SAVSPSESVA
560 570 580 590 600
MISRSCMEIL TKPLSNHEKV VRPALIYSLF PNVPPTIYFG TRDERVEKLP
610 620 630 640 650
WEQRKLLRWK MSTVTPNIVK QTIGRSHFKI SKRNDDWLGC WGHHMKSPSF
660 670 680 690 700
RSIREHQKLN HFPGSFQIGR KDRLWRNLSR MQSRFGKKEF SFFPQSFILP
710 720 730 740 750
QDAKLLRKAW ESSSRQKWIV KPPASARGIG IQVIHKWSQL PKRRPLLVQR
760 770 780 790 800
YLHKPYLISG SKFDLRIYVY VTSYDPLRIY LFSDGLVRFA SCKYSPSMKS
810 820 830 840 850
LGNKFMHLTN YSVNKKNAEY QANADEMACQ GHKWALKALW NYLSQKGVNS
860 870 880 890 900
DAIWEKIKDV VVKTIISSEP YVTSLLKMYV RRPYSCHELF GFDIMLDENL
910 920 930 940 950
KPWVLEVNIS PSLHSSSPLD ISIKGQMIRD LLNLAGFVLP NAEDIISSPS
960 970 980 990 1000
SCSSSTTSLP TSPGDKCRMA PEHVTAQKMK KAYYLTQKIP DQDFYASVLD
1010 1020 1030 1040 1050
VLTPDDVRIL VEMEDEFSRR GQFERIFPSH ISSRYLRFFE QPRYFNILTT
1060 1070 1080 1090 1100
QWEQKYHGNK LKGVDLLRSW CYKGFHMGVV SDSAPVWSLP TSLLTISKDD
1110 1120 1130 1140 1150
VILNAFSKSE TSKLGKQSSC EVSLLLSEDG TTPKSKKTQA GLSPYPQKPS
1160 1170 1180 1190
SSKDSEDTSK EPSLSTQTLP VIKCSGQTSR LSASSTFQSI SDSLLAVSP
Length:1,199
Mass (Da):133,378
Last modified:April 3, 2007 - v2
Checksum:i9B95597237588956
GO

Sequence cautioni

The sequence BAA11490.2 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171N → S.1 Publication
Corresponds to variant rs11542786 [ dbSNP | Ensembl ].
VAR_031464
Natural varianti34 – 341E → Q.1 Publication
Corresponds to variant rs3731877 [ dbSNP | Ensembl ].
VAR_031465
Natural varianti364 – 3641L → P.
Corresponds to variant rs3731875 [ dbSNP | Ensembl ].
VAR_031466
Natural varianti418 – 4181R → H.
Corresponds to variant rs2114664 [ dbSNP | Ensembl ].
VAR_013140
Natural varianti518 – 5181G → S.1 Publication
Corresponds to variant rs17851914 [ dbSNP | Ensembl ].
VAR_031467
Natural varianti524 – 5241S → G.1 Publication
Corresponds to variant rs17851915 [ dbSNP | Ensembl ].
VAR_031468
Natural varianti852 – 8521A → S.1 Publication
Corresponds to variant rs17856640 [ dbSNP | Ensembl ].
VAR_031469
Natural varianti1138 – 11381T → I.
Corresponds to variant rs9989776 [ dbSNP | Ensembl ].
VAR_057315

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D79995 mRNA. Translation: BAA11490.2. Different initiation.
AK291770 mRNA. Translation: BAF84459.1.
CH471063 Genomic DNA. Translation: EAW70651.1.
BC021707 mRNA. Translation: AAH21707.1.
CCDSiCCDS2422.1.
RefSeqiNP_055455.3. NM_014640.4.
XP_005247034.1. XM_005246977.2.
XP_006712936.1. XM_006712873.2.
XP_011510516.1. XM_011512214.1.
UniGeneiHs.471405.

Genome annotation databases

EnsembliENST00000258398; ENSP00000258398; ENSG00000135912.
ENST00000392102; ENSP00000375951; ENSG00000135912.
GeneIDi9654.
KEGGihsa:9654.
UCSCiuc002viy.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D79995 mRNA. Translation: BAA11490.2. Different initiation.
AK291770 mRNA. Translation: BAF84459.1.
CH471063 Genomic DNA. Translation: EAW70651.1.
BC021707 mRNA. Translation: AAH21707.1.
CCDSiCCDS2422.1.
RefSeqiNP_055455.3. NM_014640.4.
XP_005247034.1. XM_005246977.2.
XP_006712936.1. XM_006712873.2.
XP_011510516.1. XM_011512214.1.
UniGeneiHs.471405.

3D structure databases

ProteinModelPortaliQ14679.
SMRiQ14679. Positions 658-912.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115012. 7 interactions.
IntActiQ14679. 2 interactions.
STRINGi9606.ENSP00000258398.

PTM databases

iPTMnetiQ14679.
PhosphoSiteiQ14679.

Polymorphism and mutation databases

BioMutaiTTLL4.
DMDMi143811470.

Proteomic databases

EPDiQ14679.
MaxQBiQ14679.
PaxDbiQ14679.
PeptideAtlasiQ14679.
PRIDEiQ14679.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258398; ENSP00000258398; ENSG00000135912.
ENST00000392102; ENSP00000375951; ENSG00000135912.
GeneIDi9654.
KEGGihsa:9654.
UCSCiuc002viy.4. human.

Organism-specific databases

CTDi9654.
GeneCardsiTTLL4.
H-InvDBHIX0002837.
HGNCiHGNC:28976. TTLL4.
HPAiHPA027091.
HPA050252.
neXtProtiNX_Q14679.
PharmGKBiPA134935712.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2156. Eukaryota.
ENOG410XTI2. LUCA.
GeneTreeiENSGT00760000118951.
HOGENOMiHOG000154712.
HOVERGENiHBG058942.
InParanoidiQ14679.
KOiK16601.
OMAiYKPMLNN.
PhylomeDBiQ14679.
TreeFamiTF313087.

Miscellaneous databases

GenomeRNAii9654.
PROiQ14679.

Gene expression databases

BgeeiQ14679.
CleanExiHS_TTLL4.
ExpressionAtlasiQ14679. baseline and differential.
GenevisibleiQ14679. HS.

Family and domain databases

InterProiIPR004344. TTL/TTLL_fam.
IPR027748. TTLL-4.
[Graphical view]
PANTHERiPTHR12241:SF9. PTHR12241:SF9. 2 hits.
PfamiPF03133. TTL. 1 hit.
[Graphical view]
PROSITEiPS51221. TTL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
    DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-34.
    Tissue: Bone marrow.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS SER-17; SER-518; GLY-524 AND SER-852.
    Tissue: Testis.
  5. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "Multivalent microtubule recognition by tubulin tyrosine ligase-like family glutamylases."
    Garnham C.P., Vemu A., Wilson-Kubalek E.M., Yu I., Szyk A., Lander G.C., Milligan R.A., Roll-Mecak A.
    Cell 161:1112-1123(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF 978-LYS--LYS-981.

Entry informationi

Entry nameiTTLL4_HUMAN
AccessioniPrimary (citable) accession number: Q14679
Secondary accession number(s): A8K6V5, Q8WW29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: April 3, 2007
Last modified: July 6, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. 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.