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Protein

TBC1 domain family member 15

Gene

TBC1D15

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

Functioni

Acts as a GTPase activating protein for RAB7A. Does not act on RAB4, RAB5 or RAB6 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 15
Alternative name(s):
GTPase-activating protein RAB7
Short name:
GAP for RAB7
Short name:
Rab7-GAP
Gene namesi
Name:TBC1D15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:25694. TBC1D15.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endomembrane system Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • intracellular Source: GO_Central
  • mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134946839.

Polymorphism and mutation databases

BioMutaiTBC1D15.
DMDMi143811467.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 691690TBC1 domain family member 15PRO_0000208042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei70 – 701PhosphoserineCombined sources
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei274 – 2741PhosphoserineCombined sources
Modified residuei640 – 6401PhosphoserineCombined sources
Modified residuei675 – 6751PhosphoserineCombined sources
Modified residuei689 – 6891PhosphothreonineCombined sources
Isoform 2 (identifier: Q8TC07-2)
Modified residuei205 – 2051PhosphoserineCombined sources
Isoform 3 (identifier: Q8TC07-3)
Modified residuei213 – 2131PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8TC07.
MaxQBiQ8TC07.
PaxDbiQ8TC07.
PeptideAtlasiQ8TC07.
PRIDEiQ8TC07.

PTM databases

iPTMnetiQ8TC07.
PhosphoSiteiQ8TC07.

Expressioni

Gene expression databases

BgeeiQ8TC07.
CleanExiHS_TBC1D15.
ExpressionAtlasiQ8TC07. baseline and differential.
GenevisibleiQ8TC07. HS.

Organism-specific databases

HPAiHPA013388.
HPA015592.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCOCO1Q9P1Z23EBI-1048247,EBI-749920
CEP63Q96MT85EBI-1048247,EBI-741977
GABARAPO951665EBI-1048247,EBI-712001
GABARAPL1Q9H0R82EBI-1048247,EBI-746969
GABARAPL2P605202EBI-1048247,EBI-720116
MAP1LC3BQ9GZQ82EBI-1048247,EBI-373144
OPTNQ96CV93EBI-1048247,EBI-748974

GO - Molecular functioni

Protein-protein interaction databases

BioGridi122296. 56 interactions.
IntActiQ8TC07. 13 interactions.
STRINGi9606.ENSP00000448182.

Structurei

3D structure databases

ProteinModelPortaliQ8TC07.
SMRiQ8TC07. Positions 346-613.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini346 – 556211Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Rab-GAP TBC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2197. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00550000074386.
HOGENOMiHOG000012710.
HOVERGENiHBG057668.
InParanoidiQ8TC07.
KOiK20168.
OMAiDVEDVLC.
OrthoDBiEOG7HTHHR.
PhylomeDBiQ8TC07.
TreeFamiTF314296.

Family and domain databases

InterProiIPR021935. DUF3548.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF12068. DUF3548. 1 hit.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TC07-1) [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
MAAAGVVSGK IIYEQEGVYI HSSCGKTNDQ DGLISGILRV LEKDAEVIVD
60 70 80 90 100
WRPLDDALDS SSILYARKDS SSVVEWTQAP KERGHRGSEH LNSYEAEWDM
110 120 130 140 150
VNTVSFKRKP HTNGDAPSHR NGKSKWSFLF SLTDLKSIKQ NKEGMGWSYL
160 170 180 190 200
VFCLKDDVVL PALHFHQGDS KLLIESLEKY VVLCESPQDK RTLLVNCQNK
210 220 230 240 250
SLSQSFENLL DEPAYGLIQA GLLDRRKLLW AIHHWKKIKK DPYTATMIGF
260 270 280 290 300
SKVTNYIFDS LRGSDPSTHQ RPPSEMADFL SDAIPGLKIN QQEEPGFEVI
310 320 330 340 350
TRIDLGERPV VQRREPVSLE EWTKNIDSEG RILNVDNMKQ MIFRGGLSHA
360 370 380 390 400
LRKQAWKFLL GYFPWDSTKE ERTQLQKQKT DEYFRMKLQW KSISQEQEKR
410 420 430 440 450
NSRLRDYRSL IEKDVNRTDR TNKFYEGQDN PGLILLHDIL MTYCMYDFDL
460 470 480 490 500
GYVQGMSDLL SPLLYVMENE VDAFWCFASY MDQMHQNFEE QMQGMKTQLI
510 520 530 540 550
QLSTLLRLLD SGFCSYLESQ DSGYLYFCFR WLLIRFKREF SFLDILRLWE
560 570 580 590 600
VMWTELPCTN FHLLLCCAIL ESEKQQIMEK HYGFNEILKH INELSMKIDV
610 620 630 640 650
EDILCKAEAI SLQMVKCKEL PQAVCEILGL QGSEVTTPDS DVGEDENVVM
660 670 680 690
TPCPTSAFQS NALPTLSASG ARNDSPTQIP VSSDVCRLTP A
Length:691
Mass (Da):79,491
Last modified:April 3, 2007 - v2
Checksum:iD880DBE4D5758EC7
GO
Isoform 2 (identifier: Q8TC07-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     220-236: Missing.

Show »
Length:674
Mass (Da):77,395
Checksum:iA40A9F8838A2EB9E
GO
Isoform 3 (identifier: Q8TC07-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MAAAGVVSGK → MCPGLYPYSSLLEYGRSM
     220-236: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:682
Mass (Da):78,572
Checksum:i02F379CC94953EA9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521R → G in BAB13971 (PubMed:19077034).Curated
Sequence conflicti298 – 2981E → G in BAG60001 (PubMed:14702039).Curated
Sequence conflicti498 – 4981Q → R in BAG60001 (PubMed:14702039).Curated
Sequence conflicti541 – 5411S → G in AAH28352 (PubMed:16541075).Curated
Sequence conflicti633 – 6331S → G in BAB13971 (PubMed:19077034).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1010MAAAGVVSGK → MCPGLYPYSSLLEYGRSM in isoform 3. 1 PublicationVSP_046402
Alternative sequencei220 – 23617Missing in isoform 2 and isoform 3. 2 PublicationsVSP_023094Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB449901 mRNA. Translation: BAH16644.1.
AK022147 mRNA. Translation: BAB13971.1.
AK297626 mRNA. Translation: BAG60001.1.
AC089984 Genomic DNA. No translation available.
AC090109 Genomic DNA. No translation available.
BC028352 mRNA. Translation: AAH28352.1.
CCDSiCCDS31858.1. [Q8TC07-1]
CCDS53814.1. [Q8TC07-2]
CCDS55849.1. [Q8TC07-3]
RefSeqiNP_001139685.2. NM_001146213.1. [Q8TC07-2]
NP_001139686.1. NM_001146214.1. [Q8TC07-3]
NP_073608.4. NM_022771.4. [Q8TC07-1]
UniGeneiHs.284630.

Genome annotation databases

EnsembliENST00000319106; ENSP00000318262; ENSG00000121749. [Q8TC07-3]
ENST00000485960; ENSP00000420678; ENSG00000121749. [Q8TC07-2]
ENST00000550746; ENSP00000448182; ENSG00000121749. [Q8TC07-1]
GeneIDi64786.
KEGGihsa:64786.
UCSCiuc001swu.4. human. [Q8TC07-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB449901 mRNA. Translation: BAH16644.1.
AK022147 mRNA. Translation: BAB13971.1.
AK297626 mRNA. Translation: BAG60001.1.
AC089984 Genomic DNA. No translation available.
AC090109 Genomic DNA. No translation available.
BC028352 mRNA. Translation: AAH28352.1.
CCDSiCCDS31858.1. [Q8TC07-1]
CCDS53814.1. [Q8TC07-2]
CCDS55849.1. [Q8TC07-3]
RefSeqiNP_001139685.2. NM_001146213.1. [Q8TC07-2]
NP_001139686.1. NM_001146214.1. [Q8TC07-3]
NP_073608.4. NM_022771.4. [Q8TC07-1]
UniGeneiHs.284630.

3D structure databases

ProteinModelPortaliQ8TC07.
SMRiQ8TC07. Positions 346-613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122296. 56 interactions.
IntActiQ8TC07. 13 interactions.
STRINGi9606.ENSP00000448182.

PTM databases

iPTMnetiQ8TC07.
PhosphoSiteiQ8TC07.

Polymorphism and mutation databases

BioMutaiTBC1D15.
DMDMi143811467.

Proteomic databases

EPDiQ8TC07.
MaxQBiQ8TC07.
PaxDbiQ8TC07.
PeptideAtlasiQ8TC07.
PRIDEiQ8TC07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319106; ENSP00000318262; ENSG00000121749. [Q8TC07-3]
ENST00000485960; ENSP00000420678; ENSG00000121749. [Q8TC07-2]
ENST00000550746; ENSP00000448182; ENSG00000121749. [Q8TC07-1]
GeneIDi64786.
KEGGihsa:64786.
UCSCiuc001swu.4. human. [Q8TC07-1]

Organism-specific databases

CTDi64786.
GeneCardsiTBC1D15.
HGNCiHGNC:25694. TBC1D15.
HPAiHPA013388.
HPA015592.
MIMi612662. gene.
neXtProtiNX_Q8TC07.
PharmGKBiPA134946839.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2197. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00550000074386.
HOGENOMiHOG000012710.
HOVERGENiHBG057668.
InParanoidiQ8TC07.
KOiK20168.
OMAiDVEDVLC.
OrthoDBiEOG7HTHHR.
PhylomeDBiQ8TC07.
TreeFamiTF314296.

Miscellaneous databases

ChiTaRSiTBC1D15. human.
GenomeRNAii64786.
PROiQ8TC07.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TC07.
CleanExiHS_TBC1D15.
ExpressionAtlasiQ8TC07. baseline and differential.
GenevisibleiQ8TC07. HS.

Family and domain databases

InterProiIPR021935. DUF3548.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF12068. DUF3548. 1 hit.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that possesses Rab3A-GAP activity."
    Ishibashi K., Kanno E., Itoh T., Fukuda M.
    Genes Cells 14:41-52(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  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] (ISOFORMS 2 AND 3).
    Tissue: Brain and Embryo.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Testis.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-675 AND THR-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-70, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-274 AND SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-640 AND SER-675, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTBC15_HUMAN
AccessioniPrimary (citable) accession number: Q8TC07
Secondary accession number(s): B4DMT9
, B9A6L6, J3KNI9, Q9HA83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: April 3, 2007
Last modified: July 6, 2016
This is version 118 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.