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Q9C0C2

- TB182_HUMAN

UniProt

Q9C0C2 - TB182_HUMAN

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Protein

182 kDa tankyrase-1-binding protein

Gene
TNKS1BP1, KIAA1741, TAB182
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ankyrin binding Source: UniProtKB
  2. enzyme binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA metabolic process Source: Reactome
  3. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  4. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. telomere maintenance via telomerase Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_20514. Deadenylation of mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
182 kDa tankyrase-1-binding protein
Gene namesi
Synonyms:KIAA1741, TAB182
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:19081. TNKS1BP1.

Subcellular locationi

Nucleus. Cytoplasmcytoskeleton. Chromosome
Note: Colocalizes with chromosomes during mitosis, and in the cytoplasm with cortical actin.

GO - Cellular componenti

  1. CCR4-NOT complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-SubCell
  4. cytosol Source: Reactome
  5. nuclear telomeric heterochromatin Source: UniProtKB
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38789.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17291729182 kDa tankyrase-1-binding proteinPRO_0000072437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781Phosphoserine2 Publications
Modified residuei221 – 2211Phosphoserine1 Publication
Modified residuei239 – 2391Phosphothreonine1 Publication
Modified residuei429 – 4291Phosphoserine4 Publications
Modified residuei435 – 4351Phosphoserine2 Publications
Modified residuei437 – 4371Phosphoserine1 Publication
Modified residuei494 – 4941Phosphoserine2 Publications
Modified residuei498 – 4981Phosphoserine1 Publication
Modified residuei601 – 6011Phosphoserine4 Publications
Modified residuei672 – 6721Phosphoserine4 Publications
Modified residuei691 – 6911Phosphoserine6 Publications
Modified residuei695 – 6951Phosphoserine1 Publication
Modified residuei712 – 7121Phosphoserine1 Publication
Modified residuei744 – 7441Phosphoserine1 Publication
Modified residuei762 – 7621Phosphoserine2 Publications
Modified residuei833 – 8331Phosphothreonine1 Publication
Modified residuei836 – 8361Phosphoserine7 Publications
Modified residuei851 – 8511Phosphoserine1 Publication
Modified residuei872 – 8721Phosphoserine3 Publications
Modified residuei877 – 8771Phosphoserine1 Publication
Modified residuei882 – 8821Phosphoserine1 Publication
Modified residuei893 – 8931Phosphoserine3 Publications
Modified residuei899 – 8991Phosphoserine1 Publication
Modified residuei920 – 9201Phosphoserine1 Publication
Modified residuei936 – 9361Phosphoserine1 Publication
Modified residuei979 – 9791Phosphothreonine1 Publication
Modified residuei983 – 9831Phosphoserine1 Publication
Modified residuei987 – 9871Phosphoserine2 Publications
Modified residuei1008 – 10081Phosphoserine2 Publications
Modified residuei1024 – 10241Phosphoserine1 Publication
Modified residuei1029 – 10291Phosphoserine1 Publication
Modified residuei1054 – 10541Phosphoserine1 Publication
Modified residuei1103 – 11031Phosphoserine4 Publications
Modified residuei1133 – 11331Phosphoserine2 Publications
Modified residuei1138 – 11381Phosphoserine4 Publications
Modified residuei1178 – 11781Phosphoserine1 Publication
Modified residuei1248 – 12481Phosphoserine2 Publications
Modified residuei1253 – 12531Phosphoserine1 Publication
Modified residuei1282 – 12821Phosphothreonine1 Publication
Modified residuei1297 – 12971Phosphoserine2 Publications
Modified residuei1328 – 13281Phosphoserine1 Publication
Modified residuei1331 – 13311Phosphoserine2 Publications
Modified residuei1383 – 13831Phosphoserine2 Publications
Modified residuei1385 – 13851Phosphoserine3 Publications
Modified residuei1439 – 14391Phosphoserine1 Publication
Modified residuei1533 – 15331Phosphoserine3 Publications
Modified residuei1545 – 15451Phosphoserine2 Publications
Modified residuei1558 – 15581Phosphoserine1 Publication
Modified residuei1563 – 15631Phosphothreonine1 Publication
Modified residuei1620 – 16201Phosphoserine5 Publications
Modified residuei1621 – 16211Phosphoserine5 Publications
Modified residuei1631 – 16311Phosphoserine1 Publication
Modified residuei1652 – 16521Phosphoserine2 Publications
Modified residuei1666 – 16661Phosphoserine6 Publications
Modified residuei1715 – 17151Phosphoserine1 Publication

Post-translational modificationi

ADP-ribosylated by TNKS1 (in vitro).

Keywords - PTMi

ADP-ribosylation, Phosphoprotein

Proteomic databases

MaxQBiQ9C0C2.
PaxDbiQ9C0C2.
PRIDEiQ9C0C2.

PTM databases

PhosphoSiteiQ9C0C2.

Expressioni

Tissue specificityi

Detected in testis, ovary, lung, skeletal muscle, heart, prostate and pancreas, and at very low levels in brain and peripheral blood leukocytes.

Gene expression databases

ArrayExpressiQ9C0C2.
BgeeiQ9C0C2.
CleanExiHS_TNKS1BP1.
GenevestigatoriQ9C0C2.

Organism-specific databases

HPAiHPA037929.
HPA037930.

Interactioni

Subunit structurei

Binds to the ANK repeat domain of TNKS1 and TNKS2.

Protein-protein interaction databases

BioGridi124540. 20 interactions.
IntActiQ9C0C2. 12 interactions.
MINTiMINT-4538987.
STRINGi9606.ENSP00000350990.

Structurei

3D structure databases

ProteinModelPortaliQ9C0C2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 15721363AcidicAdd
BLAST
Regioni1450 – 154293Tankyrase-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1629 – 16357Nuclear localization signal Reviewed prediction
Motifi1723 – 17297Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 103102Arg/Glu/Lys/Pro-rich (charged)Add
BLAST
Compositional biasi127 – 767641Pro-richAdd
BLAST
Compositional biasi1010 – 1340331Gly-richAdd
BLAST
Compositional biasi1572 – 1729158Arg/Glu/Lys-rich (charged)Add
BLAST

Phylogenomic databases

eggNOGiNOG46995.
HOGENOMiHOG000001569.
HOVERGENiHBG080593.
InParanoidiQ9C0C2.
OMAiQDQEKLG.
OrthoDBiEOG7DC23N.
PhylomeDBiQ9C0C2.
TreeFamiTF336029.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9C0C2-1) [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

MKVSTLRESS AMASPLPREM EEELVPTGSE PGDTRAKPPV KPKPRALPAK     50
PALPAKPSLL VPVGPRPPRG PLAELPSARK MNMLAGPQPY GGSKRPLPFA 100
PRPAVEASTG GEATQETGKE EAGKEEPPPL TPPARCAAPG GVRKAPAPFR 150
PASERFAATT VEEILAKMEQ PRKEVLASPD RLWGSRLTFN HDGSSRYGPR 200
TYGTTTAPRD EDGSTLFRGW SQEGPVKSPA ECREEHSKTP EERSLPSDLA 250
FNGDLAKAAS SELPADISKP WIPSSPAPSS ENGGPASPGL PAEASGSGPG 300
SPHLHPPDKS SPCHSQLLEA QTPEASQASP CPAVTPSAPS AALPDEGSRH 350
TPSPGLPAEG APEAPRPSSP PPEVLEPHSL DQPPATSPRP LIEVGELLDL 400
TRTFPSGGEE EAKGDAHLRP TSLVQRRFSE GVLQSPSQDQ EKLGGSLAAL 450
PQGQGSQLAL DRPFGAESNW SLSQSFEWTF PTRPSGLGVW RLDSPPPSPI 500
TEASEAAEAA EAGNLAVSSR EEGVSQQGQG AGSAPSGSGS SWVQGDDPSM 550
SLTQKGDGES QPQFPAVPLE PLPTTEGTPG LPLQQAEERY ESQEPLAGQE 600
SPLPLATREA ALPILEPVLG QEQPAAPDQP CVLFADAPEP GQALPVEEEA 650
VTLARAETTQ ARTEAQDLCR ASPEPPGPES SSRWLDDLLA SPPPSGGGAR 700
RGAGAELKDT QSPSTCSEGL LGWSQKDLQS EFGITGDPQP SSFSPSSWCQ 750
GASQDYGLGG ASPRGDPGLG ERDWTSKYGQ GAGEGSTREW ASRCGIGQEE 800
MEASSSQDQS KVSAPGVLTA QDRVVGKPAQ LGTQRSQEAD VQDWEFRKRD 850
SQGTYSSRDA ELQDQEFGKR DSLGTYSSRD VSLGDWEFGK RDSLGAYASQ 900
DANEQGQDLG KRDHHGRYSS QDADEQDWEF QKRDVSLGTY GSRAAEPQEQ 950
EFGKSAWIRD YSSGGSSRTL DAQDRSFGTR PLSSGFSPEE AQQQDEEFEK 1000
KIPSVEDSLG EGSRDAGRPG ERGSGGLFSP STAHVPDGAL GQRDQSSWQN 1050
SDASQEVGGH QERQQAGAQG PGSADLEDGE MGKRGWVGEF SLSVGPQREA 1100
AFSPGQQDWS RDFCIEASER SYQFGIIGND RVSGAGFSPS SKMEGGHFVP 1150
PGKTTAGSVD WTDQLGLRNL EVSSCVGSGG SSEARESAVG QMGWSGGLSL 1200
RDMNLTGCLE SGGSEEPGGI GVGEKDWTSD VNVKSKDLAE VGEGGGHSQA 1250
RESGVGQTDW SGVEAGEFLK SRERGVGQAD WTPDLGLRNM APGAVCSPGE 1300
SKELGVGQMD WGNNLGLRDL EVTCDPDSGG SQGLRGCGVG QMDWTQDLAP 1350
QNVELFGAPS EAREHGVGGV SQCPEPGLRH NGSLSPGLEA RDPLEARELG 1400
VGETSGPETQ GEDYSSSSLE PHPADPGMET GEALSFGASP GRCPARPPPS 1450
GSQGLLEEML AASSSKAVAR RESAASGLGG LLEEEGAGAG AAQEEVLEPG 1500
RDSPPSWRPQ PDGEASQTED VDGTWGSSAA RWSDQGPAQT SRRPSQGPPA 1550
RSPSQDFSFI EDTEILDSAM YRSRANLGRK RGHRAPVIRP GGTLGLSEAA 1600
DSDAHLFQDS TEPRASRVPS SDEEVVEEPQ SRRTRMSLGT KGLKVNLFPG 1650
LSPSALKAKL RPRNRSAEEG ELAESKSSQK ESAVQRSKSC KVPGLGKPLT 1700
LPPKPEKSSG SEGSSPNWLQ ALKLKKKKV 1729
Length:1,729
Mass (Da):181,796
Last modified:January 11, 2011 - v4
Checksum:i561FA5C27C923036
GO
Isoform 2 (identifier: Q9C0C2-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:778
Mass (Da):82,677
Checksum:iA08CC80D7372B25D
GO

Sequence cautioni

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.
The sequence BAB21832.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti322 – 3221T → S.1 Publication
Corresponds to variant rs4939134 [ dbSNP | Ensembl ].
VAR_028141
Natural varianti714 – 7141S → N.
Corresponds to variant rs34203865 [ dbSNP | Ensembl ].
VAR_032615

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 549549Missing in isoform 2. VSP_026000Add
BLAST
Alternative sequencei1275 – 132753GVGQA…TCDPD → LGRHIYALCITLRTPPTPSL PWISSLVVEGFVPSSPPSLS LSASSSSLPWVFF in isoform 2. VSP_026001Add
BLAST
Alternative sequencei1328 – 1729402Missing in isoform 2. VSP_026002Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841L → P in AAM15531. 1 Publication
Sequence conflicti388 – 3881P → S in AAM15531. 1 Publication
Sequence conflicti554 – 5541Q → H in BAB84939. 1 Publication
Sequence conflicti604 – 6041P → S in AAM15531. 1 Publication
Sequence conflicti1450 – 14501S → F in AAM15531. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7951.1. [Q9C0C2-1]
RefSeqiNP_203754.2. NM_033396.2. [Q9C0C2-1]
XP_006718788.1. XM_006718725.1. [Q9C0C2-1]
UniGeneiHs.530730.

Genome annotation databases

EnsembliENST00000358252; ENSP00000350990; ENSG00000149115. [Q9C0C2-1]
ENST00000532437; ENSP00000437271; ENSG00000149115. [Q9C0C2-1]
GeneIDi85456.
KEGGihsa:85456.
UCSCiuc001njr.3. human. [Q9C0C2-1]

Polymorphism databases

DMDMi317373547.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS7951.1. [Q9C0C2-1 ]
RefSeqi NP_203754.2. NM_033396.2. [Q9C0C2-1 ]
XP_006718788.1. XM_006718725.1. [Q9C0C2-1 ]
UniGenei Hs.530730.

3D structure databases

ProteinModelPortali Q9C0C2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124540. 20 interactions.
IntActi Q9C0C2. 12 interactions.
MINTi MINT-4538987.
STRINGi 9606.ENSP00000350990.

PTM databases

PhosphoSitei Q9C0C2.

Polymorphism databases

DMDMi 317373547.

Proteomic databases

MaxQBi Q9C0C2.
PaxDbi Q9C0C2.
PRIDEi Q9C0C2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358252 ; ENSP00000350990 ; ENSG00000149115 . [Q9C0C2-1 ]
ENST00000532437 ; ENSP00000437271 ; ENSG00000149115 . [Q9C0C2-1 ]
GeneIDi 85456.
KEGGi hsa:85456.
UCSCi uc001njr.3. human. [Q9C0C2-1 ]

Organism-specific databases

CTDi 85456.
GeneCardsi GC11M057067.
HGNCi HGNC:19081. TNKS1BP1.
HPAi HPA037929.
HPA037930.
MIMi 607104. gene.
neXtProti NX_Q9C0C2.
PharmGKBi PA38789.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46995.
HOGENOMi HOG000001569.
HOVERGENi HBG080593.
InParanoidi Q9C0C2.
OMAi QDQEKLG.
OrthoDBi EOG7DC23N.
PhylomeDBi Q9C0C2.
TreeFami TF336029.

Enzyme and pathway databases

Reactomei REACT_20514. Deadenylation of mRNA.

Miscellaneous databases

ChiTaRSi TNKS1BP1. human.
GeneWikii TNKS1BP1.
GenomeRNAii 85456.
NextBioi 76085.
PROi Q9C0C2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9C0C2.
Bgeei Q9C0C2.
CleanExi HS_TNKS1BP1.
Genevestigatori Q9C0C2.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Hippocampus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1729 (ISOFORM 1).
    Tissue: Spleen.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; THR-833; SER-836; SER-1383; SER-1385 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-691; SER-695; SER-836; SER-1103; SER-1138; SER-1620; SER-1621 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-836; SER-1248 AND SER-1331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-691; SER-836 AND SER-1103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; THR-239; SER-429; SER-435; SER-494; SER-498; SER-601; SER-672; SER-712; SER-744; SER-762; SER-872; SER-877; SER-893; SER-920; SER-936; THR-979; SER-983; SER-987; SER-1008; SER-1029; SER-1103; SER-1133; SER-1138; SER-1178; SER-1297; SER-1328; SER-1331; SER-1439; SER-1533; SER-1545; SER-1558; THR-1563; SER-1620; SER-1621; SER-1652 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-429; SER-494; SER-691; SER-836; SER-1620; SER-1621 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "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-178; SER-221; SER-429; SER-435; SER-437; SER-601; SER-672; SER-691; SER-762; SER-836; SER-872; SER-882; SER-893; SER-987; SER-1008; SER-1024; SER-1103; SER-1133; SER-1138; SER-1248; SER-1253; THR-1282; SER-1297; SER-1383; SER-1385; SER-1533; SER-1620; SER-1621; SER-1652; SER-1666 AND SER-1715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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-429; SER-601; SER-672; SER-691; SER-836; SER-851; SER-872; SER-893; SER-899; SER-1054; SER-1138; SER-1385; SER-1533; SER-1545; SER-1620; SER-1621; SER-1631 AND SER-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTB182_HUMAN
AccessioniPrimary (citable) accession number: Q9C0C2
Secondary accession number(s): A7E2F8, Q6PJ35, Q6ZV74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 119 of the entry and version 4 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 11
    Human chromosome 11: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

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