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Description:
Transitional endoplasmic reticulum ATPase (TER ATPase) (15S Mg(2+)-ATPase p97 subunit) (Valosin-containing protein) (VCP).
Molecular weight: 89191
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) double-strand break repair( GO:0006302 )
Important dates:
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 3.
07-FEB-2006, entry version 53.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein TERA_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AF100752 | AAD43016.1 | - |
| EMBL | AC004472 | AAC07984.1 | - |
| EMBL | Z70768 | CAA94809.1 | - |
| PIR | T02243 | T02243. | |
| HSSP | Q01853 | 1E32 | |
| SMR | P55072 | 17-457.1 | |
| IntAct | P55072 | -.1 | |
| OGP | P55072 | -.1 | |
| Ensembl | ENSG00000165280 | Homo sapiens.1 | |
| H-InvDB | HIX0008010 | -.1 | |
| HGNC | HGNC:12666 | VCP.1 | |
| MIM | 601023 | gene. | |
| GO | GO:0005829 | C:cytosol | IDA. |
| GO | GO:0005783 | C:endoplasmic reticulum | IDA. |
| GO | GO:0005524 | F:ATP binding | IC. |
| GO | GO:0016887 | F:ATPase activity | TAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0030433 | P:ER-associated protein catabolism | TAS. |
| GO | GO:0045184 | P:establishment of protein localization | TAS. |
| GO | GO:0016567 | P:protein ubiquitination | NAS. |
| GO | GO:0030970 | P:retrograde protein transport, ER to cytosol | IDA. |
| GO | GO:0030968 | P:unfolded protein response | TAS. |
| InterPro | IPR003593 | AAA_ATPase. | |
| InterPro | IPR003959 | AAA_ATPase_centr. | |
| InterPro | IPR005938 | AAA_CDC48. | |
| InterPro | IPR003960 | AAA_sub. | |
| InterPro | IPR003338 | ATPaseVAT_N. | |
| Pfam | PF00004 | AAA | 2. |
| Pfam | PF02359 | CDC48_N | 1. |
| SMART | SM00382 | AAA | 2. |
| TIGRFAMs | TIGR01243 | CDC48 | 1. |
| PROSITE | PS00674 | AAA | 2. |
Keywords:
Acetylation; ATP-binding; Direct protein sequencing; Endoplasmic reticulum; Golgi stack; Lipid-binding; Nuclear protein; Nucleotide-binding; Phosphorylation; Repeat; Transport; Ubl conjugation pathway.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX MEDLINE=20402571; PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lamerdin J.E., McCready P.M., Skowronski E., Adamson A.W.,
RA Burkhart-Schultz K., Gordon L., Kyle A., Ramirez M., Stilwagen S.,
RA Phan H., Velasco N., Garnes J., Danganan L., Poundstone P.,
RA Christensen M., Georgescu A., Avila J., Liu S., Attix C., Andreise T.,
RA Trankheim M., Amico-Keller G., Coefield J., Duarte S., Lucas S.,
RA Bruce R., Thomas P., Quan G., Kronmiller B., Arellano A.,
RA Montgomery M., Ow D., Nolan M., Trong S., Kobayashi A., Olsen A.O.,
RA Carrano A.V.;
RT "Sequence analysis of a human P1 clone containing the XRCC9 DNA repair
RT gene.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-24.
RC TISSUE=Platelet;
RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [4]
RP PROTEIN SEQUENCE OF 1-17; 147-154; 277-286; 295-311; 365-376; 465-486;
RP 586-598; 638-650 AND 668-676, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION SITE ALA-1, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Unpublished observations (NOV-2005).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 387-482.
RC TISSUE=Brain;
RA Dmitrenko V.V., Garifulin O.M., Kavsan V.M.;
RT "Characterization of different mRNA types expressed in human brain.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH VIMP.
RX PubMed=15215856; DOI=10.1038/nature02656;
RA Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A.;
RT "A membrane protein complex mediates retro-translocation from the ER
RT lumen into the cytosol.";
RL Nature 429:841-847(2004).
RN [7]
RP PHOSPHORYLATION SITE TYR-804, AND MASS SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
Feature:
INIT_MET 0 0
CHAIN 1 805 Transitional endoplasmic reticulum
ATPase.
/FTId=PRO_0000084572.
NP_BIND 244 251 ATP (By similarity).
NP_BIND 517 524 ATP (By similarity).
MOD_RES 1 1 N-acetylalanine.
MOD_RES 804 804 Phosphotyrosine.
Comments:
-!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
mitosis and for their reassembly after mitosis. Involved in the
formation of the transitional endoplasmic reticulum (tER). The
transfer of membranes from the endoplasmic reticulum to the Golgi
apparatus occurs via 50-70 nm transition vesicles which derive
from part-rough, part-smooth transitional elements of the
endoplasmic reticulum (tER). Vesicle budding from the tER is an
ATP-dependent process. The ternary complex containing UFD1L, VCP
and NPL4 binds ubiquitinated proteins and is necessary for the
export of misfolded proteins from the ER to the cytoplasm, where
they are degraded by the proteasome. The NPL4-UFD1L-VCP complex
regulates spindle disassembly at the end of mitosis and is
necessary for the formation of a closed nuclear envelope (By
similarity).
-!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm
diameter, that displays 6-fold radial symmetry. Part of a ternary
complex containing STX5A, NSFL1C and VCP. NSFL1C forms a
homotrimer that binds to one end of a VCP homohexamer. The complex
binds to membranes enriched in phosphatidylethanolamine-containing
lipids. Interaction with VCIP135 leads to dissociation of the
complex via ATP hydrolysis by VCP. Part of a ternary complex
containing NPL4, UFD1L and VCP (By similarity). Interacts with
SELS/VIMP, and indirectly with DER1; which probably transfer
misfolded proteins from the ER to VCP. Interacts with SVIP (By
similarity).
-!- INTERACTION:
Q14191:WRN; NbExp=1; IntAct=EBI-355164, EBI-368417;
-!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
-!- PTM: Phosphorylated by tyrosine kinases in response to T-cell
antigen receptor activation (By similarity).
-!- SIMILARITY: Belongs to the AAA ATPase family.
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Sequence length: 805
ASGADSKGDD LSTAILKQKN RPNRLIVDEA INEDNSVVSL SQPKMDELQL FRGDTVLLKG
KKRREAVCIV LSDDTCSDEK IRMNRVVRNN LRVRLGDVIS IQPCPDVKYG KRIHVLPIDD
TVEGITGNLF EVYLKPYFLE AYRPIRKGDI FLVRGGMRAV EFKVVETDPS PYCIVAPDTV
IHCEGEPIKR EDEEESLNEV GYDDIGGCRK QLAQIKEMVE LPLRHPALFK AIGVKPPRGI
LLYGPPGTGK TLIARAVANE TGAFFFLING PEIMSKLAGE SESNLRKAFE EAEKNAPAII
FIDELDAIAP KREKTHGEVE RRIVSQLLTL MDGLKQRAHV IVMAATNRPN SIDPALRRFG
RFDREVDIGI PDATGRLEIL QIHTKNMKLA DDVDLEQVAN ETHGHVGADL AALCSEAALQ
AIRKKMDLID LEDETIDAEV MNSLAVTMDD FRWALSQSNP SALRETVVEV PQVTWEDIGG
LEDVKRELQE LVQYPVEHPD KFLKFGMTPS KGVLFYGPPG CGKTLLAKAI ANECQANFIS
IKGPELLTMW FGESEANVRE IFDKARQAAP CVLFFDELDS IAKARGGNIG DGGGAADRVI
NQILTEMDGM STKKNVFIIG ATNRPDIIDP AILRPGRLDQ LIYIPLPDEK SRVAILKANL
RKSPVAKDVD LEFLAKMTNG FSGADLTEIC QRACKLAIRE SIESEIRRER ERQTNPSAME
VEEDDPVPEI RRDHFEEAMR FARRSVSDND IRKYEMFAQT LQQSRGFGSF RFPSGNQGGA
GPSQGSGGGT GGSVYTEDND DDLYG