Q9C0C2 (TB182_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
182 kDa tankyrase-1-binding protein

Gene names

Name:	TNKS1BP1
Synonyms:	KIAA1741, TAB182

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1729 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Binds to the ANK repeat domain of TNKS1 and TNKS2.
Subcellular location	Nucleus. Cytoplasm › cytoskeleton. Chromosome. Note: Colocalizes with chromosomes during mitosis, and in the cytoplasm with cortical actin.
Tissue specificity	Detected in testis, ovary, lung, skeletal muscle, heart, prostate and pancreas, and at very low levels in brain and peripheral blood leukocytes.
Post-translational modification	ADP-ribosylated by TNKS1 (in vitro). Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23
Sequence caution	The sequence BAB21832.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB84939.1 differs from that shown. Reason: Frameshift at positions 1070, 1098 and 1466. The sequence BAB84939.1 differs from that shown. Reason: Frameshift at positions 1071, 1097 and 1467.

Ontologies

Keywords
Cellular component	Chromosome Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	ADP-ribosylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nuclear-transcribed mRNA poly(A) tail shortening Traceable author statement. Source: Reactome telomere maintenance via telomerase Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome nuclear telomeric heterochromatin Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	ankyrin binding Non-traceable author statement Ref.1. Source: UniProtKB enzyme binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9C0C2-1)

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.

Isoform 2 (identifier: Q9C0C2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-549: Missing.
     1275-1327: GVGQADWTPD...RDLEVTCDPD → LGRHIYALCI...SSSSLPWVFF
     1328-1729: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1729	1729	182 kDa tankyrase-1-binding protein		PRO_0000072437
Regions
	Region	210 – 1572	1363	Acidic
	Region	1450 – 1542	93	Tankyrase-binding
	Motif	1629 – 1635	7	Nuclear localization signal Potential
	Motif	1723 – 1729	7	Nuclear localization signal Potential
	Compositional bias	2 – 103	102	Arg/Glu/Lys/Pro-rich (charged)
	Compositional bias	127 – 767	641	Pro-rich
	Compositional bias	1010 – 1340	331	Gly-rich
	Compositional bias	1572 – 1729	158	Arg/Glu/Lys-rich (charged)
Amino acid modifications
	Modified residue	178	1	Phosphoserine Ref.19
	Modified residue	221	1	Phosphoserine Ref.15 Ref.19
	Modified residue	228	1	Phosphoserine Ref.11 Ref.19
	Modified residue	239	1	Phosphothreonine Ref.19
	Modified residue	287	1	Phosphoserine Ref.19
	Modified residue	301	1	Phosphoserine Ref.19
	Modified residue	429	1	Phosphoserine Ref.19 Ref.23
	Modified residue	435	1	Phosphoserine Ref.19 Ref.21
	Modified residue	437	1	Phosphoserine Ref.18
	Modified residue	494	1	Phosphoserine Ref.19 Ref.23
	Modified residue	498	1	Phosphoserine Ref.19
	Modified residue	504	1	Phosphoserine Ref.22
	Modified residue	518	1	Phosphoserine Ref.22
	Modified residue	601	1	Phosphoserine Ref.9 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23
	Modified residue	672	1	Phosphoserine Ref.9 Ref.11 Ref.12 Ref.16 Ref.18 Ref.19 Ref.21
	Modified residue	691	1	Phosphoserine Ref.9 Ref.12 Ref.16 Ref.18 Ref.19 Ref.22 Ref.23
	Modified residue	695	1	Phosphoserine Ref.12 Ref.19
	Modified residue	712	1	Phosphoserine Ref.19 Ref.21
	Modified residue	714	1	Phosphoserine Ref.21
	Modified residue	744	1	Phosphoserine Ref.19
	Modified residue	762	1	Phosphoserine Ref.19
	Modified residue	806	1	Phosphoserine Ref.15
	Modified residue	833	1	Phosphothreonine Ref.11
	Modified residue	836	1	Phosphoserine Ref.11 Ref.12 Ref.15 Ref.18 Ref.19 Ref.21 Ref.23
	Modified residue	872	1	Phosphoserine Ref.11 Ref.19
	Modified residue	893	1	Phosphoserine Ref.19
	Modified residue	920	1	Phosphoserine Ref.19
	Modified residue	936	1	Phosphoserine Ref.11 Ref.19
	Modified residue	976	1	Phosphoserine Ref.19
	Modified residue	979	1	Phosphothreonine Ref.19
	Modified residue	983	1	Phosphoserine Ref.19
	Modified residue	987	1	Phosphoserine Ref.19
	Modified residue	1008	1	Phosphoserine Ref.19
	Modified residue	1024	1	Phosphoserine Ref.17
	Modified residue	1029	1	Phosphoserine Ref.17 Ref.19
	Modified residue	1093	1	Phosphoserine Ref.11
	Modified residue	1103	1	Phosphoserine Ref.12 Ref.18 Ref.19
	Modified residue	1133	1	Phosphoserine Ref.19
	Modified residue	1138	1	Phosphoserine Ref.9 Ref.12 Ref.19 Ref.21 Ref.23
	Modified residue	1141	1	Phosphoserine Ref.18 Ref.21
	Modified residue	1178	1	Phosphoserine Ref.19
	Modified residue	1181	1	Phosphoserine Ref.19
	Modified residue	1248	1	Phosphoserine Ref.15
	Modified residue	1282	1	Phosphothreonine Ref.19 Ref.21
	Modified residue	1297	1	Phosphoserine Ref.19
	Modified residue	1328	1	Phosphoserine Ref.19
	Modified residue	1331	1	Phosphoserine Ref.15 Ref.19
	Modified residue	1383	1	Phosphoserine Ref.9 Ref.11 Ref.19
	Modified residue	1385	1	Phosphoserine Ref.9 Ref.11 Ref.19
	Modified residue	1405	1	Phosphoserine Ref.19
	Modified residue	1439	1	Phosphoserine Ref.19
	Modified residue	1452	1	Phosphoserine Ref.15
	Modified residue	1473	1	Phosphoserine Ref.19
	Modified residue	1476	1	Phosphoserine Ref.19
	Modified residue	1533	1	Phosphoserine Ref.19
	Modified residue	1545	1	Phosphoserine Ref.19
	Modified residue	1552	1	Phosphoserine Ref.19
	Modified residue	1554	1	Phosphoserine Ref.15
	Modified residue	1558	1	Phosphoserine Ref.19
	Modified residue	1563	1	Phosphothreonine Ref.19
	Modified residue	1616	1	Phosphoserine Ref.21
	Modified residue	1620	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.19 Ref.20 Ref.21 Ref.23
	Modified residue	1621	1	Phosphoserine Ref.9 Ref.11 Ref.12 Ref.13 Ref.19 Ref.20 Ref.21 Ref.23
	Modified residue	1652	1	Phosphoserine Ref.18 Ref.19 Ref.21
	Modified residue	1654	1	Phosphoserine Ref.14
	Modified residue	1666	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.19 Ref.22 Ref.23
	Modified residue	1715	1	Phosphoserine Ref.21
Natural variations
	Alternative sequence	1 – 549	549	Missing in isoform 2.		VSP_026000
	Alternative sequence	1275 – 1327	53	GVGQA…TCDPD → LGRHIYALCITLRTPPTPSL PWISSLVVEGFVPSSPPSLS LSASSSSLPWVFF in isoform 2.		VSP_026001
	Alternative sequence	1328 – 1729	402	Missing in isoform 2.		VSP_026002
	Natural variant	322	1	T → S. Ref.1 Corresponds to variant rs4939134 [ dbSNP | Ensembl ].		VAR_028141
	Natural variant	714	1	S → N. Corresponds to variant rs34203865 [ dbSNP | Ensembl ].		VAR_032615
Experimental info
	Sequence conflict	84	1	L → P in AAM15531. Ref.1
	Sequence conflict	388	1	P → S in AAM15531. Ref.1
	Sequence conflict	554	1	Q → H in BAB84939. Ref.7
	Sequence conflict	604	1	P → S in AAM15531. Ref.1
	Sequence conflict	1450	1	S → F in AAM15531. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: 561FA5C27C923036	FASTA	1,729	181,796
	10 20 30 40 50 60 MKVSTLRESS AMASPLPREM EEELVPTGSE PGDTRAKPPV KPKPRALPAK PALPAKPSLL 70 80 90 100 110 120 VPVGPRPPRG PLAELPSARK MNMLAGPQPY GGSKRPLPFA PRPAVEASTG GEATQETGKE 130 140 150 160 170 180 EAGKEEPPPL TPPARCAAPG GVRKAPAPFR PASERFAATT VEEILAKMEQ PRKEVLASPD 190 200 210 220 230 240 RLWGSRLTFN HDGSSRYGPR TYGTTTAPRD EDGSTLFRGW SQEGPVKSPA ECREEHSKTP 250 260 270 280 290 300 EERSLPSDLA FNGDLAKAAS SELPADISKP WIPSSPAPSS ENGGPASPGL PAEASGSGPG 310 320 330 340 350 360 SPHLHPPDKS SPCHSQLLEA QTPEASQASP CPAVTPSAPS AALPDEGSRH TPSPGLPAEG 370 380 390 400 410 420 APEAPRPSSP PPEVLEPHSL DQPPATSPRP LIEVGELLDL TRTFPSGGEE EAKGDAHLRP 430 440 450 460 470 480 TSLVQRRFSE GVLQSPSQDQ EKLGGSLAAL PQGQGSQLAL DRPFGAESNW SLSQSFEWTF 490 500 510 520 530 540 PTRPSGLGVW RLDSPPPSPI TEASEAAEAA EAGNLAVSSR EEGVSQQGQG AGSAPSGSGS 550 560 570 580 590 600 SWVQGDDPSM SLTQKGDGES QPQFPAVPLE PLPTTEGTPG LPLQQAEERY ESQEPLAGQE 610 620 630 640 650 660 SPLPLATREA ALPILEPVLG QEQPAAPDQP CVLFADAPEP GQALPVEEEA VTLARAETTQ 670 680 690 700 710 720 ARTEAQDLCR ASPEPPGPES SSRWLDDLLA SPPPSGGGAR RGAGAELKDT QSPSTCSEGL 730 740 750 760 770 780 LGWSQKDLQS EFGITGDPQP SSFSPSSWCQ GASQDYGLGG ASPRGDPGLG ERDWTSKYGQ 790 800 810 820 830 840 GAGEGSTREW ASRCGIGQEE MEASSSQDQS KVSAPGVLTA QDRVVGKPAQ LGTQRSQEAD 850 860 870 880 890 900 VQDWEFRKRD SQGTYSSRDA ELQDQEFGKR DSLGTYSSRD VSLGDWEFGK RDSLGAYASQ 910 920 930 940 950 960 DANEQGQDLG KRDHHGRYSS QDADEQDWEF QKRDVSLGTY GSRAAEPQEQ EFGKSAWIRD 970 980 990 1000 1010 1020 YSSGGSSRTL DAQDRSFGTR PLSSGFSPEE AQQQDEEFEK KIPSVEDSLG EGSRDAGRPG 1030 1040 1050 1060 1070 1080 ERGSGGLFSP STAHVPDGAL GQRDQSSWQN SDASQEVGGH QERQQAGAQG PGSADLEDGE 1090 1100 1110 1120 1130 1140 MGKRGWVGEF SLSVGPQREA AFSPGQQDWS RDFCIEASER SYQFGIIGND RVSGAGFSPS 1150 1160 1170 1180 1190 1200 SKMEGGHFVP PGKTTAGSVD WTDQLGLRNL EVSSCVGSGG SSEARESAVG QMGWSGGLSL 1210 1220 1230 1240 1250 1260 RDMNLTGCLE SGGSEEPGGI GVGEKDWTSD VNVKSKDLAE VGEGGGHSQA RESGVGQTDW 1270 1280 1290 1300 1310 1320 SGVEAGEFLK SRERGVGQAD WTPDLGLRNM APGAVCSPGE SKELGVGQMD WGNNLGLRDL 1330 1340 1350 1360 1370 1380 EVTCDPDSGG SQGLRGCGVG QMDWTQDLAP QNVELFGAPS EAREHGVGGV SQCPEPGLRH 1390 1400 1410 1420 1430 1440 NGSLSPGLEA RDPLEARELG VGETSGPETQ GEDYSSSSLE PHPADPGMET GEALSFGASP 1450 1460 1470 1480 1490 1500 GRCPARPPPS GSQGLLEEML AASSSKAVAR RESAASGLGG LLEEEGAGAG AAQEEVLEPG 1510 1520 1530 1540 1550 1560 RDSPPSWRPQ PDGEASQTED VDGTWGSSAA RWSDQGPAQT SRRPSQGPPA RSPSQDFSFI 1570 1580 1590 1600 1610 1620 EDTEILDSAM YRSRANLGRK RGHRAPVIRP GGTLGLSEAA DSDAHLFQDS TEPRASRVPS 1630 1640 1650 1660 1670 1680 SDEEVVEEPQ SRRTRMSLGT KGLKVNLFPG LSPSALKAKL RPRNRSAEEG ELAESKSSQK 1690 1700 1710 1720 ESAVQRSKSC KVPGLGKPLT LPPKPEKSSG SEGSSPNWLQ ALKLKKKKV
	Isoform 2 [UniParc]. Checksum: A08CC80D7372B25D	FASTA	778	82,677
	10 20 30 40 50 60 MSLTQKGDGE SQPQFPAVPL EPLPTTEGTP GLPLQQAEER YESQEPLAGQ ESPLPLATRE 70 80 90 100 110 120 AALPILEPVL GQEQPAAPDQ PCVLFADAPE PGQALPVEEE AVTLARAETT QARTEAQDLC 130 140 150 160 170 180 RASPEPPGPE SSSRWLDDLL ASPPPSGGGA RRGAGAELKD TQSPSTCSEG LLGWSQKDLQ 190 200 210 220 230 240 SEFGITGDPQ PSSFSPSSWC QGASQDYGLG GASPRGDPGL GERDWTSKYG QGAGEGSTRE 250 260 270 280 290 300 WASRCGIGQE EMEASSSQDQ SKVSAPGVLT AQDRVVGKPA QLGTQRSQEA DVQDWEFRKR 310 320 330 340 350 360 DSQGTYSSRD AELQDQEFGK RDSLGTYSSR DVSLGDWEFG KRDSLGAYAS QDANEQGQDL 370 380 390 400 410 420 GKRDHHGRYS SQDADEQDWE FQKRDVSLGT YGSRAAEPQE QEFGKSAWIR DYSSGGSSRT 430 440 450 460 470 480 LDAQDRSFGT RPLSSGFSPE EAQQQDEEFE KKIPSVEDSL GEGSRDAGRP GERGSGGLFS 490 500 510 520 530 540 PSTAHVPDGA LGQRDQSSWQ NSDASQEVGG HQERQQAGAQ GPGSADLEDG EMGKRGWVGE 550 560 570 580 590 600 FSLSVGPQRE AAFSPGQQDW SRDFCIEASE RSYQFGIIGN DRVSGAGFSP SSKMEGGHFV 610 620 630 640 650 660 PPGKTTAGSV DWTDQLGLRN LEVSSCVGSG GSSEARESAV GQMGWSGGLS LRDMNLTGCL 670 680 690 700 710 720 ESGGSEEPGG IGVGEKDWTS DVNVKSKDLA EVGEGGGHSQ ARESGVGQTD WSGVEAGEFL 730 740 750 760 770 KSRERLGRHI YALCITLRTP PTPSLPWISS LVVEGFVPSS PPSLSLSASS SSLPWVFF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)." Seimiya H., Smith S. J. Biol. Chem. 277:14116-14126(2002) [PubMed: 11854288] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-322. Tissue: Placenta and Testis.
[2]	"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O. DNA Res. 7:347-355(2000) [PubMed: 11214970] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Hippocampus.
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[8]	"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones." Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O. DNA Res. 10:49-57(2003) [PubMed: 12693554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1729 (ISOFORM 1). Tissue: Spleen.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-672; SER-691; SER-1138; SER-1383; SER-1385 AND SER-1621, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1666, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; SER-672; THR-833; SER-836; SER-872; SER-936; SER-1093; SER-1383; SER-1385; SER-1620; SER-1621 AND SER-1666, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; SER-691; SER-695; SER-836; SER-1103; SER-1138; SER-1620; SER-1621 AND SER-1666, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1620 AND SER-1621, MASS SPECTROMETRY. Tissue: Prostate cancer.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1654, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; SER-806; SER-836; SER-1248; SER-1331; SER-1452 AND SER-1554, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-672 AND SER-691, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1024 AND SER-1029, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437; SER-601; SER-672; SER-691; SER-836; SER-1103; SER-1141 AND SER-1652, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-221; SER-228; THR-239; SER-287; SER-301; SER-429; SER-435; SER-494; SER-498; SER-601; SER-672; SER-691; SER-695; SER-712; SER-744; SER-762; SER-836; SER-872; SER-893; SER-920; SER-936; SER-976; THR-979; SER-983; SER-987; SER-1008; SER-1029; SER-1103; SER-1133; SER-1138; SER-1178; SER-1181; THR-1282; SER-1297; SER-1328; SER-1331; SER-1383; SER-1385; SER-1405; SER-1439; SER-1473; SER-1476; SER-1533; SER-1545; SER-1552; SER-1558; THR-1563; SER-1620; SER-1621; SER-1652 AND SER-1666, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1620 AND SER-1621, MASS SPECTROMETRY. Tissue: Liver.
[21]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-601; SER-672; SER-712; SER-714; SER-836; SER-1138; SER-1141; THR-1282; SER-1616; SER-1620; SER-1621; SER-1652 AND SER-1715, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[22]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504; SER-518; SER-601; SER-691 AND SER-1666, MASS SPECTROMETRY.
[23]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-494; SER-601; SER-691; SER-836; SER-1138; SER-1620; SER-1621 AND SER-1666, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[24]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF441771 mRNA. Translation: AAM15531.1. AB051528 mRNA. Translation: BAB21832.2. Different initiation. AK124903 mRNA. Translation: BAC85989.1. AP000781 Genomic DNA. No translation available. CH471076 Genomic DNA. Translation: EAW73731.1. BC023622 mRNA. Translation: AAH23622.1. BC150333 mRNA. Translation: AAI50334.1. AK074113 mRNA. Translation: BAB84939.1. Frameshift.
IPI	IPI00304589. IPI00847646.
RefSeq	NP_203754.2. NM_033396.2.
UniGene	Hs.530730.
3D structure databases
ProteinModelPortal	Q9C0C2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9C0C2. 5 interactions.
STRING	Q9C0C2.
PTM databases
PhosphoSite	Q9C0C2.
Polymorphism databases
DMDM	116242814.
Proteomic databases
PRIDE	Q9C0C2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358252; ENSP00000350990; ENSG00000149115.
GeneID	85456.
KEGG	hsa:85456.
UCSC	uc009ymd.1. human.
Organism-specific databases
CTD	85456.
GeneCards	GC11M057067.
HGNC	HGNC:19081. TNKS1BP1.
HPA	HPA037929.
MIM	607104. gene.
neXtProt	NX_Q9C0C2.
PharmGKB	PA38789.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18729.
GeneTree	ENSGT00530000064083.
HOGENOM	HBG282914.
HOVERGEN	HBG080593.
InParanoid	Q9C0C2.
OMA	GVWRLDS.
PhylomeDB	Q9C0C2.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9C0C2.
Bgee	Q9C0C2.
CleanEx	HS_TNKS1BP1.
Genevestigator	Q9C0C2.
GermOnline	ENSG00000149115. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other
NextBio	76085.
SOURCE	Search...

Entry information

Entry name

TB182_HUMAN

Accession

Primary (citable) accession number: Q9C0C2
Secondary accession number(s): A7E2F8, Q6PJ35, Q6ZV74

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 94 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.