dbPTM

MVP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MVP_HUMAN
UniProt AC	Q14764
Protein Name	Major vault protein
Gene Name	MVP
Organism	Homo sapiens (Human).
Sequence Length	893
Subcellular Localization	Cytoplasm . Nucleus, nuclear pore complex . Cytoplasm, perinuclear region . 5% found in the nuclear pore complex (PubMed:15133037). Translocates from the nucleus to the cytoplasm upon EGF treatment (PubMed:16441665).
Protein Description	Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases..
Protein Sequence	MATEEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQVRLRHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVVEIIQATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRDFRGVSRRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLEQGIQDVYVLSEQQGLLLRALQPLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRAVIGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLADRGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYREKRARVVFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKDPQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGFETSEAKGPDGMALPRPRDQAVFPQNGLVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEALSMAVESTGTAKAEAESRAEAARIEGEGSVLQAKLKAQALAIETEAELQRVQKVRELELVYARAQLELEVSKAQQLAEVEVKKFKQMTEAIGPSTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLGMGPEGQPLGRRVASGPSPGEGISPQSAQAPQAPGDNHVVPVLR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATEEFIIR ------CCCCEEEEE	24.58	22223895
13	Phosphorylation	FIIRIPPYHYIHVLD EEEECCCCEEEEEEE	11.25	20090780
15	Phosphorylation	IRIPPYHYIHVLDQN EECCCCEEEEEEECC	6.20	28152594
52	Phosphorylation	FAPMRMVTVPPRHYC EEEEEEEECCCHHEE	20.25	-
58	Phosphorylation	VTVPPRHYCTVANPV EECCCHHEEEECCCC	7.35	28152594
59	S-nitrosylation	TVPPRHYCTVANPVS ECCCHHEEEECCCCC	1.70	2212679
60	Phosphorylation	VPPRHYCTVANPVSR CCCHHEEEECCCCCC	18.58	28450419
107	Ubiquitination	YPGEVLEKDITPLQV CCCCEECCCCCCCEE	50.71	-
132	Ubiquitination	ALLDFEDKDGDKVVA HHCCCCCCCCCEEEE	57.31	-
136	Ubiquitination	FEDKDGDKVVAGDEW CCCCCCCEEEECCEE	44.10	-
150	Phosphorylation	WLFEGPGTYIPRKEV EEEECCCEECCCCCE	22.78	24719451
299	2-Hydroxyisobutyrylation	GKNQLGQKRVVKGEK CCCCCCCEEEECCCC	45.41	-
348	Ubiquitination	EEGEDEEKVSHQAGD CCCCCHHHHCCCCCC	47.17	-
370	Ubiquitination	LEYVPSAKVEVVEER CEECCCCEEEEEEEE	43.18	21890473
389	Phosphorylation	LDENEGIYVQDVKTG CCCCCCEEEEECCCC	11.69	-
394	Ubiquitination	GIYVQDVKTGKVRAV CEEEEECCCCCEEEE	60.90	-
397	Ubiquitination	VQDVKTGKVRAVIGS EEECCCCCEEEEECC	33.50	-
404	Phosphorylation	KVRAVIGSTYMLTQD CEEEEECCEEECCCC	12.77	28348404
405	Phosphorylation	VRAVIGSTYMLTQDE EEEEECCEEECCCCC	14.03	28348404
407	Sulfoxidation	AVIGSTYMLTQDEVL EEECCEEECCCCCCH	3.10	30846556
429	Ubiquitination	GVEELLNKGQDPLAD CHHHHHHCCCCCCCC	58.90	-
440	Ubiquitination	PLADRGEKDTAKSLQ CCCCCCCCCCHHHCC	64.30	-
442	Phosphorylation	ADRGEKDTAKSLQPL CCCCCCCCHHHCCCC	47.23	26699800
444	Ubiquitination	RGEKDTAKSLQPLAP CCCCCCHHHCCCCCC	54.51	21890473
444	Sumoylation	RGEKDTAKSLQPLAP CCCCCCHHHCCCCCC	54.51	28112733
445	Phosphorylation	GEKDTAKSLQPLAPR CCCCCHHHCCCCCCC	29.76	23911959
455	Phosphorylation	PLAPRNKTRVVSYRV CCCCCCCCEEEEEEC	32.04	24719451
459	Phosphorylation	RNKTRVVSYRVPHNA CCCCEEEEEECCCCC	12.36	23403867
460	Phosphorylation	NKTRVVSYRVPHNAA CCCEEEEEECCCCCE	12.20	23403867
471	Phosphorylation	HNAAVQVYDYREKRA CCCEEEEEECCHHHE	7.08	28152594
473	Phosphorylation	AAVQVYDYREKRARV CEEEEEECCHHHEEE	11.72	28152594
560	Ubiquitination	KDPQETAKLFSVPDF CCHHHHHHHCCCCHH	58.44	-
573	2-Hydroxyisobutyrylation	DFVGDACKAIASRVR HHHHHHHHHHHHHHH	44.54	-
585	Phosphorylation	RVRGAVASVTFDDFH HHHCCEEEEECHHHC	18.32	28348404
587	Phosphorylation	RGAVASVTFDDFHKN HCCEEEEECHHHCHH	20.89	28348404
593	Ubiquitination	VTFDDFHKNSARIIR EECHHHCHHCHHHHH	53.22	-
601	Phosphorylation	NSARIIRTAVFGFET HCHHHHHEEECCCCC	19.43	20068231
608	Phosphorylation	TAVFGFETSEAKGPD EEECCCCCCCCCCCC	29.61	20068231
609	Phosphorylation	AVFGFETSEAKGPDG EECCCCCCCCCCCCC	28.49	20068231
617	Sulfoxidation	EAKGPDGMALPRPRD CCCCCCCCCCCCCCC	4.51	30846556
636	Phosphorylation	PQNGLVVSSVDVQSV CCCCEEEEEEEECCC	19.71	-
637	Phosphorylation	QNGLVVSSVDVQSVE CCCEEEEEEEECCCC	15.66	-
674	Ubiquitination	NSQEAAAKHEAQRLE CCHHHHHHHHHHHHH	36.93	21890473
692	Ubiquitination	RGRLERQKILDQSEA HHHHHHHHHCCHHHH	52.00	-
701	Ubiquitination	LDQSEAEKARKELLE CCHHHHHHHHHHHHH	61.61	-
701	2-Hydroxyisobutyrylation	LDQSEAEKARKELLE CCHHHHHHHHHHHHH	61.61	-
704	Sumoylation	SEAEKARKELLELEA HHHHHHHHHHHHHHH	58.54	28112733
714	Sulfoxidation	LELEALSMAVESTGT HHHHHHHHHHHCCCC	5.14	30846556
745	Acetylation	EGSVLQAKLKAQALA CCHHHHHHHHHHHHH	37.24	27178108
745	Ubiquitination	EGSVLQAKLKAQALA CCHHHHHHHHHHHHH	37.24	-
747	Ubiquitination	SVLQAKLKAQALAIE HHHHHHHHHHHHHHH	37.43	2190698
755	Phosphorylation	AQALAIETEAELQRV HHHHHHHCHHHHHHH	34.09	-
772	Phosphorylation	VRELELVYARAQLEL HHHHHHHHHHHHHHH	11.73	26267517
793	Ubiquitination	QLAEVEVKKFKQMTE HHHHHHHHHHHHHHH	38.70	-
796	Malonylation	EVEVKKFKQMTEAIG HHHHHHHHHHHHHHC	48.30	26320211
805	Phosphorylation	MTEAIGPSTIRDLAV HHHHHCHHHHHHHHH	31.11	-
806	Phosphorylation	TEAIGPSTIRDLAVA HHHHCHHHHHHHHHH	24.14	-
817	Sulfoxidation	LAVAGPEMQVKLLQS HHHHCHHHHHHHHHH	6.63	30846556
829	Phosphorylation	LQSLGLKSTLITDGS HHHCCCCCEEECCCC	33.22	20068231
830	Phosphorylation	QSLGLKSTLITDGST HHCCCCCEEECCCCC	22.16	20068231
833	Phosphorylation	GLKSTLITDGSTPIN CCCCEEECCCCCCCH	37.10	20068231
836	Phosphorylation	STLITDGSTPINLFN CEEECCCCCCCHHHH	33.54	28348404
837	Phosphorylation	TLITDGSTPINLFNT EEECCCCCCCHHHHH	33.45	28348404
844	Phosphorylation	TPINLFNTAFGLLGM CCCHHHHHHHHHCCC	18.94	20068231
851	Sulfoxidation	TAFGLLGMGPEGQPL HHHHHCCCCCCCCCC	9.03	30846556
864	Phosphorylation	PLGRRVASGPSPGEG CCCCCCCCCCCCCCC	48.67	27273156
867	Phosphorylation	RRVASGPSPGEGISP CCCCCCCCCCCCCCH	49.41	30266825
873	Phosphorylation	PSPGEGISPQSAQAP CCCCCCCCHHHCCCC	27.95	29255136
876	Phosphorylation	GEGISPQSAQAPQAP CCCCCHHHCCCCCCC	26.23	30266825

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of MVP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MVP_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of MVP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR1_HUMAN	ESR1	physical	9628887
PTEN_HUMAN	PTEN	physical	12177006
RFWD2_HUMAN	RFWD2	physical	15994960
TEP1_HUMAN	TEP1	physical	10551828
NNTM_HUMAN	NNT	physical	21988832
PLS1_HUMAN	PLSCR1	physical	21988832
MVP_HUMAN	MVP	physical	21988832
POTE1_HUMAN	POT1	physical	21988832
SAP_HUMAN	PSAP	physical	22863883
MVP_HUMAN	MVP	physical	24722188
PLS1_HUMAN	PLSCR1	physical	24722188
RIMB1_HUMAN	BZRAP1	physical	24722188
DISC1_HUMAN	DISC1	physical	24722188
DLX2_HUMAN	DLX2	physical	24722188
ATL4_HUMAN	ADAMTSL4	physical	24722188
AES_HUMAN	AES	physical	24722188
BANP_HUMAN	BANP	physical	24722188
CA094_HUMAN	C1orf94	physical	24722188
CACO2_HUMAN	CALCOCO2	physical	24722188
KCC2B_HUMAN	CAMK2B	physical	24722188
IHO1_HUMAN	CCDC36	physical	24722188
SAXO1_HUMAN	FAM154A	physical	24722188
FA46C_HUMAN	FAM46C	physical	24722188
GOGA2_HUMAN	GOLGA2	physical	24722188
KCTD9_HUMAN	KCTD9	physical	24722188
IMA4_HUMAN	KPNA3	physical	24722188
MDFI_HUMAN	MDFI	physical	24722188
MEOX1_HUMAN	MEOX1	physical	24722188
MEOX2_HUMAN	MEOX2	physical	24722188
TRIM1_HUMAN	MID2	physical	24722188
MKL1_HUMAN	MKL1	physical	24722188
NT2NL_HUMAN	NOTCH2NL	physical	24722188
STN1_HUMAN	OBFC1	physical	24722188
PIHD2_HUMAN	PIH1D2	physical	24722188
PPIP1_HUMAN	PSTPIP1	physical	24722188
RAB3I_HUMAN	RAB3IP	physical	24722188
RBPMS_HUMAN	RBPMS	physical	24722188
REL_HUMAN	REL	physical	24722188
RHXF2_HUMAN	RHOXF2	physical	24722188
RIM3A_HUMAN	RIMBP3	physical	24722188
RN111_HUMAN	RNF111	physical	24722188
SRTD1_HUMAN	SERTAD1	physical	24722188
SKIL_HUMAN	SKIL	physical	24722188
ITF2_HUMAN	TCF4	physical	24722188
TFCP2_HUMAN	TFCP2	physical	24722188
P53_HUMAN	TP53	physical	24722188
TRAF2_HUMAN	TRAF2	physical	24722188
TRI27_HUMAN	TRIM27	physical	24722188
TRI42_HUMAN	TRIM42	physical	24722188
PCH2_HUMAN	TRIP13	physical	24722188
TRIP6_HUMAN	TRIP6	physical	24722188
VAC14_HUMAN	VAC14	physical	24722188
ZBT32_HUMAN	ZBTB32	physical	24722188
ZMIZ2_HUMAN	ZMIZ2	physical	24722188
MVP_HUMAN	MVP	physical	25416956
PARP4_HUMAN	PARP4	physical	28514442
GOPC_HUMAN	GOPC	physical	28514442
RCOR3_HUMAN	RCOR3	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MVP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, AND MASSSPECTROMETRY.	15592455 [Abstract]
"The major vault protein is a novel substrate for the tyrosinephosphatase SHP-2 and scaffold protein in epidermal growth factorsignaling."; Kolli S., Zito C.I., Mossink M.H., Wiemer E.A.C., Bennett A.M.; J. Biol. Chem. 279:29374-29385(2004). Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES, MASS SPECTROMETRY, INTERACTIONWITH PTPN11, SUBCELLULAR LOCATION, AND FUNCTION.	15133037 [Abstract]