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Protein

Anaphase-promoting complex subunit 1

Gene

ANAPC1

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

Functioni

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit 1
Short name:
APC1
Alternative name(s):
Cyclosome subunit 1
Mitotic checkpoint regulator
Testis-specific gene 24 protein
Gene namesi
Name:ANAPC1
Synonyms:TSG24
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:19988. ANAPC1.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134907013.

Polymorphism and mutation databases

BioMutaiANAPC1.
DMDMi37537845.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19441944Anaphase-promoting complex subunit 1PRO_0000215871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511PhosphoserineCombined sources
Modified residuei60 – 601PhosphoserineCombined sources
Modified residuei202 – 2021Phosphoserine1 Publication
Modified residuei286 – 2861Phosphoserine1 Publication
Modified residuei291 – 2911PhosphothreonineCombined sources1 Publication
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei355 – 3551PhosphoserineCombined sources1 Publication
Modified residuei362 – 3621PhosphoserineCombined sources
Modified residuei373 – 3731Phosphoserine1 Publication
Modified residuei377 – 3771PhosphoserineCombined sources1 Publication
Modified residuei537 – 5371Phosphothreonine1 Publication
Modified residuei547 – 5471PhosphoserineCombined sources
Modified residuei555 – 5551PhosphoserineCombined sources
Modified residuei571 – 5711Phosphotyrosine1 Publication
Modified residuei686 – 6861PhosphoserineCombined sources
Modified residuei688 – 6881PhosphoserineCombined sources1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation on Ser-355 occurs specifically during mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H1A4.
MaxQBiQ9H1A4.
PaxDbiQ9H1A4.
PRIDEiQ9H1A4.

PTM databases

iPTMnetiQ9H1A4.
PhosphoSiteiQ9H1A4.

Expressioni

Gene expression databases

BgeeiQ9H1A4.
CleanExiHS_ANAPC1.
ExpressionAtlasiQ9H1A4. baseline and differential.
GenevisibleiQ9H1A4. HS.

Organism-specific databases

HPAiHPA036329.
HPA036330.
HPA042998.

Interactioni

Subunit structurei

The mammalian APC/C is composed of 14 distinct subunits that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa.1 Publication

Protein-protein interaction databases

BioGridi122229. 75 interactions.
DIPiDIP-32940N.
IntActiQ9H1A4. 43 interactions.
MINTiMINT-2817292.
STRINGi9606.ENSP00000339109.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60A1-1944[»]
5A31electron microscopy4.30A11-1897[»]
ProteinModelPortaliQ9H1A4.
SMRiQ9H1A4. Positions 11-295, 398-513, 581-670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1297 – 132529PC 1Add
BLAST
Repeati1366 – 140439PC 2Add
BLAST
Repeati1467 – 150135PC 3Add
BLAST
Repeati1520 – 155233PC 4Add
BLAST

Sequence similaritiesi

Belongs to the APC1 family.Curated
Contains 4 PC repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1858. Eukaryota.
ENOG410XQ83. LUCA.
GeneTreeiENSGT00390000016757.
HOGENOMiHOG000231934.
HOVERGENiHBG045326.
InParanoidiQ9H1A4.
KOiK03348.
OMAiAEWMQPP.
PhylomeDBiQ9H1A4.
TreeFamiTF105441.

Family and domain databases

InterProiIPR024990. Apc1.
[Graphical view]
PANTHERiPTHR12827. PTHR12827. 1 hit.
PfamiPF12859. ANAPC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H1A4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNFYEERTT MIAARDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS
60 70 80 90 100
SDGAAGLVGS LQEVTIHEKQ KESWQLRKGV SEIGEDVDYD EELYVAGNMV
110 120 130 140 150
IWSKGSKSQA LAVYKAFTVD SPVQQALWCD FIISQDKSEK AYSSNEVEKC
160 170 180 190 200
ICILQSSCIN MHSIEGKDYI ASLPFQVANV WPTKYGLLFE RSASSHEVPP
210 220 230 240 250
GSPREPLPTM FSMLHPLDEI TPLVCKSGSL FGSSRVQYVV DHAMKIVFLN
260 270 280 290 300
TDPSIVMTYD AVQNVHSVWT LRRVKSEEEN VVLKFSEQGG TPQNVATSSS
310 320 330 340 350
LTAHLRSLSK GDSPVTSPFQ NYSSIHSQSR STSSPSLHSR SPSISNMAAL
360 370 380 390 400
SRAHSPALGV HSFSGVQRFN ISSHNQSPKR HSISHSPNSN SNGSFLAPET
410 420 430 440 450
EPIVPELCID HLWTETITNI REKNSQASKV FITSDLCGQK FLCFLVESQL
460 470 480 490 500
QLRCVKFQES NDKTQLIFGS VTNIPAKDAA PVEKIDTMLV LEGSGNLVLY
510 520 530 540 550
TGVVRVGKVF IPGLPAPSLT MSNTMPRPST PLDGVSTPKP LSKLLGSLDE
560 570 580 590 600
VVLLSPVPEL RDSSKLHDSL YNEDCTFQQL GTYIHSIRDP VHNRVTLELS
610 620 630 640 650
NGSMVRITIP EIATSELVQT CLQAIKFILP KEIAVQMLVK WYNVHSAPGG
660 670 680 690 700
PSYHSEWNLF VTCLMNMMGY NTDRLAWTRN FDFEGSLSPV IAPKKARPSE
710 720 730 740 750
TGSDDDWEYL LNSDYHQNVE SHLLNRSLCL SPSEASQMKD EDFSQNLSLD
760 770 780 790 800
SSTLLFTHIP AIFFVLHLVY EELKLNTLMG EGICSLVELL VQLARDLKLG
810 820 830 840 850
PYVDHYYRDY PTLVRTTGQV CTIDPGQTGF MHHPSFFTSE PPSIYQWVSS
860 870 880 890 900
CLKGEGMPPY PYLPGICERS RLVVLSIALY ILGDESLVSD ESSQYLTRIT
910 920 930 940 950
IAPQKLQVEQ EENRFSFRHS TSVSSLAERL VVWMTNVGFT LRDLETLPFG
960 970 980 990 1000
IALPIRDAIY HCREQPASDW PEAVCLLIGR QDLSKQACEG NLPKGKSVLS
1010 1020 1030 1040 1050
SDVPSGTETE EEDDGMNDMN HEVMSLIWSE DLRVQDVRRL LQSAHPVRVN
1060 1070 1080 1090 1100
VVQYPELSDH EFIEEKENRL LQLCQRTMAL PVGRGMFTLF SYHPVPTEPL
1110 1120 1130 1140 1150
PIPKLNLTGR APPRNTTVDL NSGNIDVPPN MTSWASFHNG VAAGLKIAPA
1160 1170 1180 1190 1200
SQIDSAWIVY NKPKHAELAN EYAGFLMALG LNGHLTKLAT LNIHDYLTKG
1210 1220 1230 1240 1250
HEMTSIGLLL GVSAAKLGTM DMSITRLLSI HIPALLPPTS TELDVPHNVQ
1260 1270 1280 1290 1300
VAAVVGIGLV YQGTAHRHTA EVLLAEIGRP PGPEMEYCTD RESYSLAAGL
1310 1320 1330 1340 1350
ALGMVCLGHG SNLIGMSDLN VPEQLYQYMV GGHRRFQTGM HREKHKSPSY
1360 1370 1380 1390 1400
QIKEGDTINV DVTCPGATLA LAMIYLKTNN RSIADWLRAP DTMYLLDFVK
1410 1420 1430 1440 1450
PEFLLLRTLA RCLILWDDIL PNSKWVDSNV PQIIRENSIS LSEIELPCSE
1460 1470 1480 1490 1500
DLNLETLSQA HVYIIAGACL SLGFRFAGSE NLSAFNCLHK FAKDFMTYLS
1510 1520 1530 1540 1550
APNASVTGPH NLETCLSVVL LSLAMVMAGS GNLKVLQLCR FLHMKTGGEM
1560 1570 1580 1590 1600
NYGFHLAHHM ALGLLFLGGG RYSLSTSNSS IAALLCALYP HFPAHSTDNR
1610 1620 1630 1640 1650
YHLQALRHLY VLAAEPRLLV PVDVDTNTPC YALLEVTYKG TQWYEQTKEE
1660 1670 1680 1690 1700
LMAPTLLPEL HLLKQIKVKG PRYWELLIDL SKGTQHLKSI LSKDGVLYVK
1710 1720 1730 1740 1750
LRAGQLSYKE DPMGWQSLLA QTVANRNSEA RAFKPETISA FTSDPALLSF
1760 1770 1780 1790 1800
AEYFCKPTVN MGQKQEILDL FSSVLYECVT QETPEMLPAY IAMDQAIRRL
1810 1820 1830 1840 1850
GRREMSETSE LWQIKLVLEF FSSRSHQERL QNHPKRGLFM NSEFLPVVKC
1860 1870 1880 1890 1900
TIDNTLDQWL QVGGDMCVHA YLSGQPLEES QLSMLACFLV YHSVPAPQHL
1910 1920 1930 1940
PPIGLEGSTS FAELLFKFKQ LKMPVRALLR LAPLLLGNPQ PMVM
Length:1,944
Mass (Da):216,500
Last modified:March 1, 2001 - v1
Checksum:iE08B1FE3FC28917E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti604 – 6041M → V in BAB14687 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278357 mRNA. Translation: CAC19484.1.
BC005089 mRNA. Translation: AAH05089.1.
BC104902 mRNA. Translation: AAI04903.1.
BC104904 mRNA. Translation: AAI04905.1.
AK023807 mRNA. Translation: BAB14687.1.
CCDSiCCDS2093.1.
RefSeqiNP_073153.1. NM_022662.3.
UniGeneiHs.436527.

Genome annotation databases

EnsembliENST00000341068; ENSP00000339109; ENSG00000153107.
GeneIDi64682.
KEGGihsa:64682.
UCSCiuc002thi.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278357 mRNA. Translation: CAC19484.1.
BC005089 mRNA. Translation: AAH05089.1.
BC104902 mRNA. Translation: AAI04903.1.
BC104904 mRNA. Translation: AAI04905.1.
AK023807 mRNA. Translation: BAB14687.1.
CCDSiCCDS2093.1.
RefSeqiNP_073153.1. NM_022662.3.
UniGeneiHs.436527.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UI9electron microscopy3.60A1-1944[»]
5A31electron microscopy4.30A11-1897[»]
ProteinModelPortaliQ9H1A4.
SMRiQ9H1A4. Positions 11-295, 398-513, 581-670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122229. 75 interactions.
DIPiDIP-32940N.
IntActiQ9H1A4. 43 interactions.
MINTiMINT-2817292.
STRINGi9606.ENSP00000339109.

PTM databases

iPTMnetiQ9H1A4.
PhosphoSiteiQ9H1A4.

Polymorphism and mutation databases

BioMutaiANAPC1.
DMDMi37537845.

Proteomic databases

EPDiQ9H1A4.
MaxQBiQ9H1A4.
PaxDbiQ9H1A4.
PRIDEiQ9H1A4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341068; ENSP00000339109; ENSG00000153107.
GeneIDi64682.
KEGGihsa:64682.
UCSCiuc002thi.4. human.

Organism-specific databases

CTDi64682.
GeneCardsiANAPC1.
H-InvDBHIX0002242.
HIX0161603.
HGNCiHGNC:19988. ANAPC1.
HPAiHPA036329.
HPA036330.
HPA042998.
MIMi608473. gene.
neXtProtiNX_Q9H1A4.
PharmGKBiPA134907013.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1858. Eukaryota.
ENOG410XQ83. LUCA.
GeneTreeiENSGT00390000016757.
HOGENOMiHOG000231934.
HOVERGENiHBG045326.
InParanoidiQ9H1A4.
KOiK03348.
OMAiAEWMQPP.
PhylomeDBiQ9H1A4.
TreeFamiTF105441.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176407. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiANAPC1. human.
GeneWikiiANAPC1.
GenomeRNAii64682.
NextBioi66605.
PROiQ9H1A4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H1A4.
CleanExiHS_ANAPC1.
ExpressionAtlasiQ9H1A4. baseline and differential.
GenevisibleiQ9H1A4. HS.

Family and domain databases

InterProiIPR024990. Apc1.
[Graphical view]
PANTHERiPTHR12827. PTHR12827. 1 hit.
PfamiPF12859. ANAPC1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterisation of the human APC1, the largest subunit of the anaphase-promoting complex."
    Joergensen P.M., Graeslund S., Betz R., Stahl S., Larsson C., Hoeoeg C.
    Gene 262:51-59(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Colon and Ovary.
  3. "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] OF 510-1944.
    Tissue: Placenta.
  4. "Mitotic regulation of the human anaphase-promoting complex by phosphorylation."
    Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.
    EMBO J. 22:6598-6609(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-202; SER-286; THR-291; SER-355; SER-373; SER-377; THR-537; TYR-571 AND SER-688.
  5. "Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
    Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
    Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE APC/C.
  6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-377; SER-547 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-60; THR-291; SER-341; SER-355; SER-362 AND SER-547, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-60; SER-547; SER-555 AND SER-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-60; THR-291; SER-341; SER-355; SER-377; SER-547; SER-555; SER-686 AND SER-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-377 AND SER-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C."
    Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A., Engel A., Peters J.-M., Stark H.
    Mol. Cell 20:867-879(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF THE APC/C.
  16. "Molecular architecture and mechanism of the anaphase-promoting complex."
    Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.
    Nature 513:388-393(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, SUBUNIT.

Entry informationi

Entry nameiAPC1_HUMAN
AccessioniPrimary (citable) accession number: Q9H1A4
Secondary accession number(s): Q2M3H8, Q9BSE6, Q9H8D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 137 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.