Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenomatous polyposis coli protein

Gene

Apc

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

Functioni

Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Adenomatous polyposis coli protein
Short name:
Protein APC
Gene namesi
Name:Apc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2123. Apc.

Subcellular locationi

  • Cell junctionadherens junction By similarity
  • Cytoplasmcytoskeleton By similarity
  • Cell projectionlamellipodium By similarity
  • Cell projectionruffle membrane By similarity
  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Associated with the microtubule network at the growing distal tip of microtubules. Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane.By similarity

GO - Cellular componenti

  • adherens junction Source: UniProtKB-SubCell
  • axonal growth cone Source: RGD
  • beta-catenin destruction complex Source: UniProtKB
  • cell body fiber Source: RGD
  • cell cortex Source: RGD
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • dendrite Source: RGD
  • growth cone Source: RGD
  • kinetochore Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • microtubule Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection terminus Source: RGD
  • nuclear membrane Source: RGD
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • protein complex Source: RGD
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi523 – 5231C → R in an IQ-induced colon tumor. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 28422841Adenomatous polyposis coli proteinPRO_0000064629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei105 – 1051PhosphoserineBy similarity
Modified residuei109 – 1091PhosphoserineBy similarity
Modified residuei742 – 7421PhosphoserineCombined sources
Modified residuei778 – 7781PhosphoserineCombined sources
Modified residuei985 – 9851PhosphoserineCombined sources
Modified residuei1036 – 10361PhosphoserineBy similarity
Modified residuei1040 – 10401PhosphoserineCombined sources
Modified residuei1357 – 13571PhosphoserineBy similarity
Modified residuei1368 – 13681PhosphoserineCombined sources
Modified residuei1389 – 13891PhosphoserineBy similarity
Modified residuei1392 – 13921PhosphoserineBy similarity
Modified residuei1435 – 14351PhosphothreonineBy similarity
Modified residuei1565 – 15651PhosphoserineCombined sources
Modified residuei1714 – 17141PhosphoserineCombined sources
Modified residuei1772 – 17721PhosphoserineBy similarity
Modified residuei1859 – 18591PhosphoserineCombined sources
Modified residuei1861 – 18611PhosphoserineBy similarity
Modified residuei1862 – 18621PhosphoserineBy similarity
Modified residuei1969 – 19691PhosphoserineBy similarity
Modified residuei1971 – 19711PhosphoserineBy similarity
Modified residuei2087 – 20871PhosphoserineCombined sources
Modified residuei2092 – 20921PhosphoserineCombined sources
Modified residuei2125 – 21251PhosphoserineBy similarity
Modified residuei2129 – 21291PhosphoserineCombined sources
Modified residuei2130 – 21301PhosphoserineCombined sources
Modified residuei2132 – 21321PhosphoserineCombined sources
Modified residuei2151 – 21511PhosphothreonineBy similarity
Modified residuei2260 – 22601PhosphoserineBy similarity
Modified residuei2270 – 22701PhosphoserineBy similarity
Modified residuei2283 – 22831PhosphoserineBy similarity
Modified residuei2473 – 24731PhosphoserineBy similarity
Modified residuei2535 – 25351PhosphoserineBy similarity
Modified residuei2671 – 26711PhosphoserineBy similarity
Modified residuei2674 – 26741PhosphoserineBy similarity
Modified residuei2679 – 26791PhosphothreonineBy similarity
Modified residuei2710 – 27101PhosphoserineCombined sources
Modified residuei2723 – 27231PhosphoserineBy similarity
Modified residuei2788 – 27881PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by GSK3B.By similarity
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP70478.
PRIDEiP70478.

PTM databases

iPTMnetiP70478.
PhosphoSiteiP70478.

Interactioni

Subunit structurei

Forms homooligomers and heterooligomers with APC2. Interacts with DIAPH1 and DIAPH2. Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with ARHGEF4 (via N-terminus). Interacts with MAPRE1 (via C-terminus); probably required for APC targeting to the growing microtubule plus ends. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells. Interacts with SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3 domain). Interacts at the cell membrane with AMER1 and AMER2 (via ARM repeats) (By similarity). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4P310162EBI-631663,EBI-375655

GO - Molecular functioni

Protein-protein interaction databases

BioGridi246393. 6 interactions.
IntActiP70478. 1 interaction.
STRINGi10116.ENSRNOP00000027691.

Structurei

3D structure databases

ProteinModelPortaliP70478.
SMRiP70478. Positions 2-55, 128-237, 1467-1528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati451 – 49343ARM 1Add
BLAST
Repeati503 – 54543ARM 2Add
BLAST
Repeati546 – 58944ARM 3Add
BLAST
Repeati590 – 63647ARM 4Add
BLAST
Repeati637 – 68145ARM 5Add
BLAST
Repeati682 – 72342ARM 6Add
BLAST
Repeati724 – 76542ARM 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1864 – 189128Highly chargedAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 6261Sequence analysisAdd
BLAST
Coiled coili125 – 260136Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2802 – 28054Microtubule tip localization signal
Motifi2840 – 28423PDZ-bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 728728Leu-richAdd
BLAST
Compositional biasi739 – 28312093Ser-richAdd
BLAST
Compositional biasi1130 – 115526Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi1556 – 157520Asp/Glu-rich (acidic)Add
BLAST

Domaini

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.By similarity

Sequence similaritiesi

Contains 7 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG2122. Eukaryota.
ENOG410XR2V. LUCA.
HOGENOMiHOG000033986.
HOVERGENiHBG004264.
InParanoidiP70478.
KOiK02085.
PhylomeDBiP70478.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR026836. APC.
IPR009240. APC_15aa_rpt.
IPR009234. APC_basic_dom.
IPR026831. APC_dom.
IPR026818. Apc_fam.
IPR032038. APC_N.
IPR009223. APC_rpt.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR009232. EB1-bd.
IPR009224. SAMP.
[Graphical view]
PANTHERiPTHR12607. PTHR12607. 2 hits.
PTHR12607:SF11. PTHR12607:SF11. 2 hits.
PfamiPF05972. APC_15aa. 3 hits.
PF05956. APC_basic. 1 hit.
PF05923. APC_crr. 7 hits.
PF16689. APC_N_CC. 1 hit.
PF00514. Arm. 2 hits.
PF05937. EB1_binding. 1 hit.
PF05924. SAMP. 3 hits.
[Graphical view]
SMARTiSM00185. ARM. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF58050. SSF58050. 1 hit.
SSF82931. SSF82931. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P70478-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTELETE ASNMKEVLKQ
60 70 80 90 100
LQGSIEDETM TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS
110 120 130 140 150
VSSRSGECSP VPMGSFPRRA FVNGSRESTG YLEELEKERS LLLADLDKEE
160 170 180 190 200
KEKDWYYAQL QNLTKRIDSL PLTENFSLQT DMTRRQLEYE ARQIRAAMEE
210 220 230 240 250
QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA ERSSQSKHET
260 270 280 290 300
ASHEAERQLE GQGVAESNLA TSGSGQSSAA RVDHETAGVL SSSGTHSAPR
310 320 330 340 350
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC
360 370 380 390 400
LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR
410 420 430 440 450
EIRVLHLLEQ IRAYCETCWE WQEAHEQGMD QDKNPMPAPV EHQICPAVCV
460 470 480 490 500
LMKLSFDEEH RHAMNELGGL QAIAELLQVD CEMHGLTDDH YSVTLRRYAG
510 520 530 540 550
MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ VIASVLRNLS
560 570 580 590 600
WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
610 620 630 640 650
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH
660 670 680 690 700
RQILRENNCL QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG
710 720 730 740 750
AVSMLKNLIH SKHKMIAMGS AAALRNLMAN RPAKYKDANI MSPGSSLPSL
760 770 780 790 800
HVRKQKALEA ELDAQHLSET FDNIDNLSPK ASHRSKQRHK QNLYGDYVFD
810 820 830 840 850
ASRHDDNRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD SSRSEKDRSL
860 870 880 890 900
ERERGIGLST YHSATENPGT SSKRGLQLSA TAAQIAKVME EVSALHTSQD
910 920 930 940 950
DRSPASAAEL HCVAEERTAA RRSSASHTHP NTHNFAKSES SNRTCSMPYA
960 970 980 990 1000
KVEYKRSSND SLNSVTSSDG YGKRGQMKPS VESYSEDDEG KFCSYGQYPA
1010 1020 1030 1040 1050
DLAHKIHSAN HMDDNGGELD TPINYSLKYS DEQLNSGRQS PSQNERWARP
1060 1070 1080 1090 1100
KHVIEDEIKQ NEQRQSRSQN TNFPVYSENT DDKHLKFQQH FGQQECVSPY
1110 1120 1130 1140 1150
RSRGTNGSET NRMGSSHAVN QNVNQSLCQE DDYEDDKPTN YSERYSEEEQ
1160 1170 1180 1190 1200
HEEEERPTNY SIKYNEEKHH VDQPIDYSLK YATDISSSQK PSFSFSKTPS
1210 1220 1230 1240 1250
VQGTKTEHNS PSSEAASAPS SNAKRQSQLH PSSAQRNGQT PKGTACKVPS
1260 1270 1280 1290 1300
INQETMQTYC VEDTPICFSR CSSLSSLSSA EDEIGCDQTT QEADSANTLQ
1310 1320 1330 1340 1350
IAEIKENDVT RSAQDPASDV PAVSQSTRTK PSRLQASGLA SESARHKAVE
1360 1370 1380 1390 1400
FSSGAKSPSK SGAQTPKSPP EHYVQETPLV FSRCTSVSSL DSFESRSIAS
1410 1420 1430 1440 1450
SVQSEPCSGM VSGIVSPSDL PDSPGQTMPP SRSKTPPPPP PPQPVQTKRE
1460 1470 1480 1490 1500
VPKTKVPAAE QREGGPKQTA VSAAVQRVQV LPDADTLLHF ATESTPDGFS
1510 1520 1530 1540 1550
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETEPEQ PEESNENQDK
1560 1570 1580 1590 1600
EVEKPDSEKD LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP
1610 1620 1630 1640 1650
PPVARKPSQL PVYKLLPSQS RLQAQKHVSF TPGDDVPRVY CVEGTPINFS
1660 1670 1680 1690 1700
TATSLSDLTI ESPPNELAAG DGVRASVQSG EFEKRDTIPT EGRSTDEAQR
1710 1720 1730 1740 1750
GKVSSIAIPD LDGSKAEEGD ILAECINSAL PKGRSHKPFR VKKIMDQVQQ
1760 1770 1780 1790 1800
ASMTSSGTNK NQIDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
1810 1820 1830 1840 1850
ETFSDNKDSK KQSLKNNPKD LNDKLPDNED RVRGGFTFDS PHHYAPIEGT
1860 1870 1880 1890 1900
PYCFSRNDSL SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCHTEPSS
1910 1920 1930 1940 1950
SQQSARKAQA STKHPVNRGP SKPLLQEQPT FPQSSKDVPD RGAATDEKLQ
1960 1970 1980 1990 2000
NFAIENTPVC FSRNSSLSSL SDVDQENNNN EETGPVRDAE PANAQGQPGK
2010 2020 2030 2040 2050
PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLRE CISSAMPKKR
2060 2070 2080 2090 2100
RPSRLKGEGE WQSPRKVGSV LAEDLTLDLK DIQRPESEHG LSPDSENFDW
2110 2120 2130 2140 2150
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GVSLGSPFHL
2160 2170 2180 2190 2200
TPDQEEKPFT SHKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT
2210 2220 2230 2240 2250
GKIRSNSEIS SQMKQPLQTN MPSISRGRTM IHIPGVRNSS SSTSPVSKKG
2260 2270 2280 2290 2300
PPLKTPASKS PSEGPVATTS PRGTKPAVKS ELSPITRQTS HISGSNKGPS
2310 2320 2330 2340 2350
RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISTPN KLSQLPRTSS
2360 2370 2380 2390 2400
PSTASTKSSG SGKMSYTSPG RQLSQQNLSK QTGLSKNASS IPRSESASKG
2410 2420 2430 2440 2450
LNQMNNSNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP
2460 2470 2480 2490 2500
TLRRKLEESA SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ
2510 2520 2530 2540 2550
AGGWRKLPPN LSPTIEYSDG RPSKRHDIAR SHSESPSRLP VNRAGTWKRE
2560 2570 2580 2590 2600
HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDEK HVNSVPGPRQ
2610 2620 2630 2640 2650
MKENQVPTKG TWRKIKESEI SPTNTVSQTT SSGAASGAES KTLIYQMAPA
2660 2670 2680 2690 2700
VSRTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSISEKG NPSIKDSKDT
2710 2720 2730 2740 2750
QGKQSVGSGS PVQTVGLENR LNSFIQVEAP EQKGTETKAG QGSPAPVAET
2760 2770 2780 2790 2800
GETCMAERTP FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR
2810 2820 2830 2840
PSQIPTPVGS STKKRDSKTD STESSGAQSP KRHSGSYLVT SV
Length:2,842
Mass (Da):310,533
Last modified:February 1, 1997 - v1
Checksum:i3CBB2EA8A34E8F47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38629 mRNA. Translation: BAA07609.1.
RefSeqiNP_036631.1. NM_012499.1.
UniGeneiRn.156346.
Rn.88057.

Genome annotation databases

GeneIDi24205.
KEGGirno:24205.
UCSCiRGD:2123. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38629 mRNA. Translation: BAA07609.1.
RefSeqiNP_036631.1. NM_012499.1.
UniGeneiRn.156346.
Rn.88057.

3D structure databases

ProteinModelPortaliP70478.
SMRiP70478. Positions 2-55, 128-237, 1467-1528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246393. 6 interactions.
IntActiP70478. 1 interaction.
STRINGi10116.ENSRNOP00000027691.

PTM databases

iPTMnetiP70478.
PhosphoSiteiP70478.

Proteomic databases

PaxDbiP70478.
PRIDEiP70478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24205.
KEGGirno:24205.
UCSCiRGD:2123. rat.

Organism-specific databases

CTDi324.
RGDi2123. Apc.

Phylogenomic databases

eggNOGiKOG2122. Eukaryota.
ENOG410XR2V. LUCA.
HOGENOMiHOG000033986.
HOVERGENiHBG004264.
InParanoidiP70478.
KOiK02085.
PhylomeDBiP70478.

Miscellaneous databases

NextBioi602593.
PROiP70478.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR026836. APC.
IPR009240. APC_15aa_rpt.
IPR009234. APC_basic_dom.
IPR026831. APC_dom.
IPR026818. Apc_fam.
IPR032038. APC_N.
IPR009223. APC_rpt.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR009232. EB1-bd.
IPR009224. SAMP.
[Graphical view]
PANTHERiPTHR12607. PTHR12607. 2 hits.
PTHR12607:SF11. PTHR12607:SF11. 2 hits.
PfamiPF05972. APC_15aa. 3 hits.
PF05956. APC_basic. 1 hit.
PF05923. APC_crr. 7 hits.
PF16689. APC_N_CC. 1 hit.
PF00514. Arm. 2 hits.
PF05937. EB1_binding. 1 hit.
PF05924. SAMP. 3 hits.
[Graphical view]
SMARTiSM00185. ARM. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF58050. SSF58050. 1 hit.
SSF82931. SSF82931. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of the rat APC gene and assignment to chromosome 18."
    Toyota M., Ushijima T., Kakiuchi H., Watanabe M., Imai K., Yachi A., Sugimura T., Nagao M.
    Mamm. Genome 6:746-748(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344/N.
    Tissue: Brain.
  2. "Specific 5'-GGGA-3'-->5'-GGA-3' mutation of the Apc gene in rat colon tumors induced by 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine."
    Kakiuchi H., Watanabe M., Ushijima T., Toyota M., Imai K., Weisburger J.H., Sugimura T., Nagao M.
    Proc. Natl. Acad. Sci. U.S.A. 92:910-914(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
    Strain: Fischer 344/N and Sprague-Dawley.
  3. "The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway."
    Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.
    Genes Dev. 20:1933-1945(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH MACF1; CTNNB1; AXIN1 AND GSK3B.
  4. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742; SER-778; SER-985; SER-1040; SER-1368; SER-1565; SER-1859; SER-2087; SER-2092; SER-2129; SER-2130; SER-2132 AND SER-2710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAPC_RAT
AccessioniPrimary (citable) accession number: P70478
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 1, 1997
Last modified: May 11, 2016
This is version 139 of the entry and version 1 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.