dbPTM

IMB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IMB1_HUMAN
UniProt AC	Q14974
Protein Name	Importin subunit beta-1
Gene Name	KPNB1
Organism	Homo sapiens (Human).
Sequence Length	876
Subcellular Localization	Cytoplasm . Nucleus envelope .
Protein Description	Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports SNAI1 and PRKCI into the nucleus..
Protein Sequence	MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDPSVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MELITILE -------CCCCHHHH	9.49	19413330
1	Sulfoxidation	-------MELITILE -------CCCCHHHH	9.49	28183972
5	Phosphorylation	---MELITILEKTVS ---CCCCHHHHHCCC	31.94	20068231
10	Phosphorylation	LITILEKTVSPDRLE CCHHHHHCCCCCHHH	19.48	23927012
12	Phosphorylation	TILEKTVSPDRLELE HHHHHCCCCCHHHHH	26.72	23927012
15	Methylation	EKTVSPDRLELEAAQ HHCCCCCHHHHHHHH	33.18	115481407
23	Ubiquitination	LELEAAQKFLERAAV HHHHHHHHHHHHHHH	47.38	21890473
23	2-Hydroxyisobutyrylation	LELEAAQKFLERAAV HHHHHHHHHHHHHHH	47.38	-
23	Ubiquitination	LELEAAQKFLERAAV HHHHHHHHHHHHHHH	47.38	21890473
23	Acetylation	LELEAAQKFLERAAV HHHHHHHHHHHHHHH	47.38	21466224
23	Ubiquitination	LELEAAQKFLERAAV HHHHHHHHHHHHHHH	47.38	21890473
41	Phosphorylation	PTFLVELSRVLANPG CHHHHHHHHHHCCCC	13.56	21712546
46	Ubiquitination	ELSRVLANPGNSQVA HHHHHHCCCCCHHHH	40.63	-
50	Phosphorylation	VLANPGNSQVARVAA HHCCCCCHHHHHHHH	31.76	21712546
61	Ubiquitination	RVAAGLQIKNSLTSK HHHHCCEECCCCCCC	5.69	-
62	Ubiquitination	VAAGLQIKNSLTSKD HHHCCEECCCCCCCC	27.76	21906983
62	Ubiquitination	VAAGLQIKNSLTSKD HHHCCEECCCCCCCC	27.76	21890473
62	Ubiquitination	VAAGLQIKNSLTSKD HHHCCEECCCCCCCC	27.76	21890473
66	Acetylation	LQIKNSLTSKDPDIK CEECCCCCCCCCCHH	33.29	-
66	Ubiquitination	LQIKNSLTSKDPDIK CEECCCCCCCCCCHH	33.29	-
68	Ubiquitination	IKNSLTSKDPDIKAQ ECCCCCCCCCCHHHH	68.96	-
68	2-Hydroxyisobutyrylation	IKNSLTSKDPDIKAQ ECCCCCCCCCCHHHH	68.96	-
68	Acetylation	IKNSLTSKDPDIKAQ ECCCCCCCCCCHHHH	68.96	26051181
68	Succinylation	IKNSLTSKDPDIKAQ ECCCCCCCCCCHHHH	68.96	23954790
73	Ubiquitination	TSKDPDIKAQYQQRW CCCCCCHHHHHHHHH	36.50	-
73	2-Hydroxyisobutyrylation	TSKDPDIKAQYQQRW CCCCCCHHHHHHHHH	36.50	-
73	Acetylation	TSKDPDIKAQYQQRW CCCCCCHHHHHHHHH	36.50	26051181
76	Phosphorylation	DPDIKAQYQQRWLAI CCCHHHHHHHHHHHH	16.09	19702290
170	Phosphorylation	PEQLQDKSNEILTAI HHHHHHHHHHHHHHH	48.24	20068231
175	Phosphorylation	DKSNEILTAIIQGMR HHHHHHHHHHHHHHC	22.82	20068231
181	Sulfoxidation	LTAIIQGMRKEEPSN HHHHHHHHCCCCCCC	2.95	21406390
191	Acetylation	EEPSNNVKLAATNAL CCCCCHHHHHHHHHH	34.23	25953088
191	Ubiquitination	EEPSNNVKLAATNAL CCCCCHHHHHHHHHH	34.23	-
201	Phosphorylation	ATNALLNSLEFTKAN HHHHHHHHHHHHHHC	29.28	24719451
206	Ubiquitination	LNSLEFTKANFDKES HHHHHHHHHCCCCHH	46.80	21906983
206	2-Hydroxyisobutyrylation	LNSLEFTKANFDKES HHHHHHHHHCCCCHH	46.80	-
206	Ubiquitination	LNSLEFTKANFDKES HHHHHHHHHCCCCHH	46.80	21890473
206	Ubiquitination	LNSLEFTKANFDKES HHHHHHHHHCCCCHH	46.80	21890473
211	Acetylation	FTKANFDKESERHFI HHHHCCCCHHHHHHH	60.03	19608861
211	Ubiquitination	FTKANFDKESERHFI HHHHCCCCHHHHHHH	60.03	19608861
226	Phosphorylation	MQVVCEATQCPDTRV HHHHHHHHCCCCHHH	14.38	-
231	Acetylation	EATQCPDTRVRVAAL HHHCCCCHHHHHHHH	19.06	-
231	Ubiquitination	EATQCPDTRVRVAAL HHHCCCCHHHHHHHH	19.06	-
246	Phosphorylation	QNLVKIMSLYYQYME HHHHHHHHHHHHHHH	19.38	25867546
248	Phosphorylation	LVKIMSLYYQYMETY HHHHHHHHHHHHHHH	4.92	25867546
249	Phosphorylation	VKIMSLYYQYMETYM HHHHHHHHHHHHHHH	9.84	25867546
251	Phosphorylation	IMSLYYQYMETYMGP HHHHHHHHHHHHHHH	4.84	25867546
254	Phosphorylation	LYYQYMETYMGPALF HHHHHHHHHHHHHHH	11.41	25867546
255	Phosphorylation	YYQYMETYMGPALFA HHHHHHHHHHHHHHH	6.18	25867546
264	Phosphorylation	GPALFAITIEAMKSD HHHHHHHHHHHHHCC	14.88	25867546
372	Ubiquitination	PHVLPFIKEHIKNPD HHHHHHHHHHCCCCC	43.55	-
376	Ubiquitination	PFIKEHIKNPDWRYR HHHHHHCCCCCCHHH	65.42	21890473
376	Acetylation	PFIKEHIKNPDWRYR HHHHHHCCCCCCHHH	65.42	25953088
376	Ubiquitination	PFIKEHIKNPDWRYR HHHHHHCCCCCCHHH	65.42	21890473
376	Ubiquitination	PFIKEHIKNPDWRYR HHHHHHCCCCCCHHH	65.42	21890473
392	Ubiquitination	AAVMAFGCILEGPEP HHHHHHHHHHCCCCH	2.31	-
396	Ubiquitination	AFGCILEGPEPSQLK HHHHHHCCCCHHHCH	28.55	-
404	Ubiquitination	PEPSQLKPLVIQAMP CCHHHCHHHHHHHHH	40.21	-
421	Phosphorylation	IELMKDPSVVVRDTA HHHHCCCCEEECCCH	37.36	23403867
448	Phosphorylation	EAAINDVYLAPLLQC HHHHCCHHHHHHHHH	10.46	-
449	Ubiquitination	AAINDVYLAPLLQCL HHHCCHHHHHHHHHH	3.88	-
506	Ubiquitination	LSSSFELIVQKLLET HHHHHHHHHHHHHHC	2.13	-
513	Phosphorylation	IVQKLLETTDRPDGH HHHHHHHCCCCCCCC	33.69	24275569
526	Phosphorylation	GHQNNLRSSAYESLM CCCCCHHHHHHHHHH	23.61	28152594
527	Phosphorylation	HQNNLRSSAYESLME CCCCHHHHHHHHHHH	28.56	28152594
529	Phosphorylation	NNLRSSAYESLMEIV CCHHHHHHHHHHHHH	14.16	28796482
531	Phosphorylation	LRSSAYESLMEIVKN HHHHHHHHHHHHHHH	21.97	28152594
533	Sulfoxidation	SSAYESLMEIVKNSA HHHHHHHHHHHHHCH	4.62	30846556
537	Ubiquitination	ESLMEIVKNSAKDCY HHHHHHHHHCHHHCH	51.34	21906983
537	Ubiquitination	ESLMEIVKNSAKDCY HHHHHHHHHCHHHCH	51.34	21890473
537	Acetylation	ESLMEIVKNSAKDCY HHHHHHHHHCHHHCH	51.34	25953088
537	Ubiquitination	ESLMEIVKNSAKDCY HHHHHHHHHCHHHCH	51.34	21890473
539	Phosphorylation	LMEIVKNSAKDCYPA HHHHHHHCHHHCHHH	30.86	24275569
541	Ubiquitination	EIVKNSAKDCYPAVQ HHHHHCHHHCHHHHH	48.42	21906983
541	2-Hydroxyisobutyrylation	EIVKNSAKDCYPAVQ HHHHHCHHHCHHHHH	48.42	-
544	Phosphorylation	KNSAKDCYPAVQKTT HHCHHHCHHHHHHHH	12.36	20068231
549	Ubiquitination	DCYPAVQKTTLVIME HCHHHHHHHHHHHHH	36.56	21906983
564	Sulfoxidation	RLQQVLQMESHIQST HHHHHHHHHHHHCCC	5.09	21406390
565	Ubiquitination	LQQVLQMESHIQSTS HHHHHHHHHHHCCCC	26.63	-
566	Phosphorylation	QQVLQMESHIQSTSD HHHHHHHHHHCCCCC	22.13	22210691
585	Ubiquitination	NDLQSLLCATLQNVL HHHHHHHHHHHHHHH	3.09	-
587	Phosphorylation	LQSLLCATLQNVLRK HHHHHHHHHHHHHHH	28.07	-
594	Ubiquitination	TLQNVLRKVQHQDAL HHHHHHHHCCCCCHH	41.93	-
614	Sulfoxidation	VMASLLRMFQSTAGS HHHHHHHHHHHCCCC	3.46	30846556
617	Phosphorylation	SLLRMFQSTAGSGGV HHHHHHHHCCCCCCC	14.68	22210691
618	Phosphorylation	LLRMFQSTAGSGGVQ HHHHHHHCCCCCCCH	25.01	22210691
621	Phosphorylation	MFQSTAGSGGVQEDA HHHHCCCCCCCHHHH	29.88	23532336
630	Sulfoxidation	GVQEDALMAVSTLVE CCHHHHHHHHHHHHH	3.57	30846556
632	Ubiquitination	QEDALMAVSTLVEVL HHHHHHHHHHHHHHH	2.53	-
646	Phosphorylation	LGGEFLKYMEAFKPF HCHHHHHHHHHHCCH	11.44	20860994
651	Ubiquitination	LKYMEAFKPFLGIGL HHHHHHHCCHHCCCC	41.74	21890473
651	Ubiquitination	LKYMEAFKPFLGIGL HHHHHHHCCHHCCCC	41.74	21890473
651	Acetylation	LKYMEAFKPFLGIGL HHHHHHHCCHHCCCC	41.74	26051181
651	Ubiquitination	LKYMEAFKPFLGIGL HHHHHHHCCHHCCCC	41.74	21890473
690	Acetylation	SNIIPFCDEVMQLLL CCCHHHHHHHHHHHH	52.48	-
690	Ubiquitination	SNIIPFCDEVMQLLL CCCHHHHHHHHHHHH	52.48	-
710	Ubiquitination	ENVHRSVKPQILSVF CCHHHCCCHHHHHHH	32.24	21906983
714	Ubiquitination	RSVKPQILSVFGDIA HCCCHHHHHHHHHHH	2.77	-
722	Acetylation	SVFGDIALAIGGEFK HHHHHHHHHHCCHHH	3.49	-
722	Ubiquitination	SVFGDIALAIGGEFK HHHHHHHHHHCCHHH	3.49	-
726	Ubiquitination	DIALAIGGEFKKYLE HHHHHHCCHHHHHHH	30.93	-
730	Ubiquitination	AIGGEFKKYLEVVLN HHCCHHHHHHHHHHH	61.46	21890473
730	Ubiquitination	AIGGEFKKYLEVVLN HHCCHHHHHHHHHHH	61.46	21890473
730	Ubiquitination	AIGGEFKKYLEVVLN HHCCHHHHHHHHHHH	61.46	21890473
738	Phosphorylation	YLEVVLNTLQQASQA HHHHHHHHHHHHHHH	23.06	-
743	Phosphorylation	LNTLQQASQAQVDKS HHHHHHHHHHCCCCC	23.01	-
750	Phosphorylation	SQAQVDKSDYDMVDY HHHCCCCCHHHHHHH	36.62	29978859
752	Phosphorylation	AQVDKSDYDMVDYLN HCCCCCHHHHHHHHH	17.03	28796482
754	Sulfoxidation	VDKSDYDMVDYLNEL CCCCHHHHHHHHHHH	1.69	30846556
757	Phosphorylation	SDYDMVDYLNELRES CHHHHHHHHHHHHHH	10.46	-
777	Ubiquitination	TGIVQGLKGDQENVH HHHHHHHCCCCCCCC	68.23	21906983
788	Sulfoxidation	ENVHPDVMLVQPRVE CCCCCCEEEECCCHH	3.85	21406390
835	Acetylation	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	19608861
835	Ubiquitination	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	21890473
835	2-Hydroxyisobutyrylation	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	-
835	Malonylation	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	26320211
835	Ubiquitination	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	21890473
835	Ubiquitination	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	21890473
842	Sulfoxidation	KLVEARPMIHELLTE HHHHHHHHHHHHHHC	3.99	21406390
853	Phosphorylation	LLTEGRRSKTNKAKT HHHCCCCCCCCHHHH	42.33	22817900
855	Phosphorylation	TEGRRSKTNKAKTLA HCCCCCCCCHHHHHH	43.10	22817900
859	Ubiquitination	RSKTNKAKTLATWAT CCCCCHHHHHHHHHH	45.76	-
867	Acetylation	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	19608861
867	Ubiquitination	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	21890473
867	2-Hydroxyisobutyrylation	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	-
867	Malonylation	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	26320211
867	Ubiquitination	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	21890473
867	Ubiquitination	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	21890473
871	Ubiquitination	WATKELRKLKNQA-- HHHHHHHHHHHCC--	76.16	-

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 IMB1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IMB1_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 IMB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRBP2_HUMAN	SREBF2	physical	11283257
IMA1_HUMAN	KPNA2	physical	11283257
NU153_HUMAN	NUP153	physical	10202161
NUP50_HUMAN	NUP50	physical	12176322
SMAD3_HUMAN	SMAD3	physical	10846168
SMAD4_HUMAN	SMAD4	physical	10846168
IPO7_HUMAN	IPO7	physical	9214382
IPO8_HUMAN	IPO8	physical	9214382
NU153_HUMAN	NUP153	physical	10749866
MTG8_HUMAN	RUNX1T1	physical	10951564
NUP62_HUMAN	NUP62	physical	11266456
NUP54_HUMAN	NUP54	physical	11266456
NU153_HUMAN	NUP153	physical	11266456
RBP2_HUMAN	RANBP2	physical	11266456
RAN_HUMAN	RAN	physical	9135132
NUP62_HUMAN	NUP62	physical	9102465
NTF2_HUMAN	NUTF2	physical	9102465
IMA5_HUMAN	KPNA1	physical	9102465
RAN_HUMAN	RAN	physical	9102465
RANG_HUMAN	RANBP1	physical	10779340
RAN_HUMAN	RAN	physical	10779340
NUP98_HUMAN	NUP98	physical	9144189
SRY_HUMAN	SRY	physical	15297880
RCC1_HUMAN	RCC1	physical	17855385
RAN_HUMAN	RAN	physical	20658144
RANG_HUMAN	RANBP1	physical	20658144
NU153_HUMAN	NUP153	physical	20658144
IMB1_HUMAN	KPNB1	physical	21832065
AMFR_HUMAN	AMFR	physical	21832065
DERL1_HUMAN	DERL1	physical	21832065
SELS_HUMAN	VIMP	physical	21832065
CUL4B_HUMAN	CUL4B	physical	19801544
RAN_HUMAN	RAN	physical	10037787
RANG_HUMAN	RANBP1	physical	10037787
EXO1_HUMAN	EXO1	physical	22222486
TBA1A_HUMAN	TUBA1A	physical	21278340
RBP2_HUMAN	RANBP2	physical	8909533
RANG_HUMAN	RANBP1	physical	8909533
RAN_HUMAN	RAN	physical	8909533
PIAS4_HUMAN	PIAS4	physical	15383276
PTN_HUMAN	PTN	physical	15383276
NXF1_HUMAN	NXF1	physical	21965294
DCAF8_HUMAN	DCAF8	physical	22500989
RAE1L_HUMAN	RAE1	physical	15851029
RAN_HUMAN	RAN	physical	9045717
RANG_HUMAN	RANBP1	physical	9045717
RAN_HUMAN	RAN	physical	22939629
IPO5_HUMAN	IPO5	physical	22939629
IPO9_HUMAN	IPO9	physical	22939629
ERBB2_HUMAN	ERBB2	physical	16314522
RASF5_HUMAN	RASSF5	physical	23538446
RAN_HUMAN	RAN	physical	9214382
NU100_YEAST	NUP100	physical	25562883
NU116_YEAST	NUP116	physical	25562883
NUP98_HUMAN	NUP98	physical	25562883
NU98B_ARATH	AT1G59660	physical	25562883
NUP98_CAEEL	npp-10	physical	25562883
SMAP_HUMAN	C11orf58	physical	26344197
XPO2_HUMAN	CSE1L	physical	26344197
EXOS2_HUMAN	EXOSC2	physical	26344197
IPO4_HUMAN	IPO4	physical	26344197
IPO8_HUMAN	IPO8	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
NUCL_HUMAN	NCL	physical	26344197
NUP98_HUMAN	NUP98	physical	26344197
RAN_HUMAN	RAN	physical	26344197
RNBP6_HUMAN	RANBP6	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
AL3A2_HUMAN	ALDH3A2	physical	26496610
RCC1_HUMAN	RCC1	physical	26496610
ERF1_HUMAN	ETF1	physical	26496610
GLE1_HUMAN	GLE1	physical	26496610
ECHB_HUMAN	HADHB	physical	26496610
SP110_HUMAN	SP110	physical	26496610
KIFC1_HUMAN	KIFC1	physical	26496610
IMA5_HUMAN	KPNA1	physical	26496610
IMA1_HUMAN	KPNA2	physical	26496610
IMA4_HUMAN	KPNA3	physical	26496610
IMA3_HUMAN	KPNA4	physical	26496610
NSF_HUMAN	NSF	physical	26496610
NUP88_HUMAN	NUP88	physical	26496610
NUP98_HUMAN	NUP98	physical	26496610
RAN_HUMAN	RAN	physical	26496610
RANG_HUMAN	RANBP1	physical	26496610
RBP2_HUMAN	RANBP2	physical	26496610
RAGP1_HUMAN	RANGAP1	physical	26496610
TAF4B_HUMAN	TAF4B	physical	26496610
TAF11_HUMAN	TAF11	physical	26496610
UBC9_HUMAN	UBE2I	physical	26496610
SUMO1_HUMAN	SUMO1	physical	26496610
R113A_HUMAN	RNF113A	physical	26496610
NU214_HUMAN	NUP214	physical	26496610
AAAS_HUMAN	AAAS	physical	26496610
RAE1L_HUMAN	RAE1	physical	26496610
CCNK_HUMAN	CCNK	physical	26496610
NU155_HUMAN	NUP155	physical	26496610
NUP93_HUMAN	NUP93	physical	26496610
DLGP5_HUMAN	DLGAP5	physical	26496610
RUSC2_HUMAN	RUSC2	physical	26496610
MED24_HUMAN	MED24	physical	26496610
NU153_HUMAN	NUP153	physical	26496610
NXF1_HUMAN	NXF1	physical	26496610
IPO7_HUMAN	IPO7	physical	26496610
NUP50_HUMAN	NUP50	physical	26496610
S27A2_HUMAN	SLC27A2	physical	26496610
NUPL2_HUMAN	NUPL2	physical	26496610
NU205_HUMAN	NUP205	physical	26496610
PO210_HUMAN	NUP210	physical	26496610
NU160_HUMAN	NUP160	physical	26496610
NEMP1_HUMAN	TMEM194A	physical	26496610
NU188_HUMAN	NUP188	physical	26496610
IMA7_HUMAN	KPNA6	physical	26496610
VIR_HUMAN	KIAA1429	physical	26496610
QCR9_HUMAN	UQCR10	physical	26496610
SENP1_HUMAN	SENP1	physical	26496610
CERS2_HUMAN	CERS2	physical	26496610
NUSAP_HUMAN	NUSAP1	physical	26496610
TM214_HUMAN	TMEM214	physical	26496610
CEP55_HUMAN	CEP55	physical	26496610
NSMA3_HUMAN	SMPD4	physical	26496610
NDC1_HUMAN	NDC1	physical	26496610
NU133_HUMAN	NUP133	physical	26496610
NU107_HUMAN	NUP107	physical	26496610
THOC2_HUMAN	THOC2	physical	26496610
CHD8_HUMAN	CHD8	physical	26496610
NUP37_HUMAN	NUP37	physical	26496610
ZC3HE_HUMAN	ZC3H14	physical	26496610
NUP85_HUMAN	NUP85	physical	26496610
SEH1_HUMAN	SEH1L	physical	26496610
PKHA8_HUMAN	PLEKHA8	physical	26496610
TM209_HUMAN	TMEM209	physical	26496610
SPB12_HUMAN	SERPINB12	physical	26496610
YTDC1_HUMAN	YTHDC1	physical	26496610
CMTD1_HUMAN	COMTD1	physical	26496610
NUP53_HUMAN	NUP35	physical	26496610
CDCA2_HUMAN	CDCA2	physical	26496610
NUP43_HUMAN	NUP43	physical	26496610
RGPD8_HUMAN	RGPD8	physical	26496610
STOM_HUMAN	STOM	physical	27173435

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 IMB1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211; LYS-835 AND LYS-867,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.	18691976 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-211, AND MASSSPECTROMETRY.	17370265 [Abstract]