. 2018 Oct 10;41(10):889–899. doi: 10.14348/molcells.2018.0192

Table 1.

A list of MU-type IDPs/IDRs containing PreSMos

Name	Number of residues	P/R^b	Location of PreSMo residues^c	Population^d (%)	Role/Binding	References
FlgM	97	P	60–73	50±10	σ²⁸	Daughdrill et al., 1997
			83–90	50±10
			42–50	20
KID	60	R	119–129	>50	KIX	Radhakrishnan et al., 1998
KID			134–143	~10		Hua et al., 1998
GBD/CRIB in WASP W7	68	R	252–264	~14	Cdc42/Rac	Rudolph et al., 1998
GBD/CRIB in WASP W7	(201–268)
HIV-1 Nef	56	R	14–22 : helix I	18		Geyer et al., 1999
HIV-1 Nef	(2–57)		35–41 : helix II (Hα only)
Synaptobrevin-2	96	R	78–91	45	core complex forming	Hazzard et al., 1999
APPC	47	R	20–23	30	X11	Ramelot et al., 2000
	(649–695)		27–35	20
			37–45 (Hα only)	30
p53 TAD	73	R	18–26 : helix	20	Mdm2	Lee et al., 2000
			40–44 : turn I	5	RPA, TFEII
			48–53 : turn II	15
RPS4	200	P	12–15	8	rRNA, ribosomal proteins	Sayers et al., 2000
RPS4			30–33: β?	23
α-Synuclein	140	P	18–31	~10	amyloid-forming	Eliezer et al., 2001
α-Synuclein						Murrali et al., 2018
N-term. Tmod 1	92	R	24–35	NA	tropomyosin	Greenfield et al., 2005
VP16 TAD	79		443–447	25	hTAF_II31 PC4	Jonker et al., 2005
VP16 TAD	(412–490)	R	469–483	15
VP16 TAD	79	R	424–433/442–446, 465–467/472–479 (Hα only)	60/40	hTAF_II31 PC4	Kim et al., 2009
VP16 TAD	(412–490)		424–433/442–446, 465–467/472–479 (Hα only)	10/20
Dynein interm. chain	40	R	223–228	NA	light chains	Benison et al., 2006
Dynein interm. chain	(198–237)					Benison et al., 2007
γ-Synuclein	127	P	49–99	~15		Marsh et al., 2006
HMGA1	107	P	3–9	8	20 different proteins	Buchko et al., 2007
HMGA1			64–67
CFTR	185	R	α-helix		interaction between R region and NT-binding domain 1	Baker et al., 2007
	(654–838)		654–668, 759–764, 766–776, 801–817	>5
			654–668, 759–764, 766–776, 801–817	>5
			β-strand
			744–753	>5
NS5A-D2 (HCV)	93	R	L48-V57	20	-	Liang et al., 2007
NS5A-D2 (HCV)	(250–342)		L86-E96 (Hα only)	25
preS1 of HBV	119	R	32–36, 41–45	~10	hepatocyte receptor-binding	Chi et al., 2007
			11–18, 22–25, 37–40, 46–50. (Hα only)	~10	hepatocyte receptor-binding
			11–18, 22–25, 37–40, 46–50. (Hα only)	~10
β-synuclein	134	P	NA	~20	-	Sung et al., 2007
Securin	202	P	150–159 : helix	45	-	Csizmok et al., 2008
			113–127 (β)	15
			174–178	20
C-XPC^e	126	R	818–843: helix	~30	Centri2	Miron et al., 2008
	(815–940)		847–860: helix	~30	TFIIH
			891–901: helix	NA
			908–915: helix	NA
			923–930: helix	NA
MSP2	237	P	14–21	35	-	Zhang et al., 2008
			140–150	35
			197–211	20
DARPP-32	118	R	22–29	50	PP1	Dancheck et al., 2008
DARPP-32			103–114	25
I-2	156	R	36–42	30	PP1	Dancheck et al., 2008
	(9–164)		96–106	48 (70)
			127–154	67 (90)
			132–138	>98
ENSA	121	P	32–36	40	-	Boettcher et al., 2008
			48–50	10		Boettcher et al., 2007
			65–70	30
ODD/HIF-1α	74	R	438–440	~10	-	Kim et al., 2009
ODD/HIF-1α	(404–477)		467–477
Sml1	104	P	4–14: helix	~20	RNR binding	Zhao et al., 2000
Sml1	(1–104)		61–80: helix	~70	Dimer forming
Myb25	25	R	295–309 : helix	25~30	KIX	Zor et al., 2002
Myb25	(291–315)
N tail	125	R	488–499 : helix	NA	phosphoprotein P	Bourhis et al., 2004
Measles virus nucleoprotein	(401–525)
dSLBP	92	R	28–45 : helix	NA	mRNA	Thapar et al., 2004
	(17–108)		50–57 : helix		stem-loop
			66–75 : helix
			91–96 : helix
Tβ-4	43	P	5–16 : helix	NA	Ca ATP	Domanski et al., 2004
Tβ-4	(1–43)				G-actin
N tail	82	R	479–484	36	phosphoprotein P	Jensen et al., 2008
Sendai Virus nucleoprotein	(443–524)		476–488	38
Sendai Virus nucleoprotein			478–492	11
Sic1	90	R	20–30	20	Cdc4	Mittag et al., 2008
Sic1	(1–90)		63–68
c-Myc	88	R	26–34 : helix	40	Bin-SH3 domain	Andresen et al., 2012
	(1–88)		47–52 : helix	25	24–31(TRRAP binding)
			20–23 : β-turn
ExsE	88	P	42–51: helix	NA	ExsC	Zheng et al., 2012
ExsE	(1–88)		61–65: helix
NS5A	415	R	401–412 : helix	NA	Bin1-SH3	Braeuning, 2013
HCV	(33–447)		427–445 : helix
NS5A	179	R	205–221 : helix I	38	Bin1-SH3	Feuerstein et al., 2012
HCV	(191–369)		251–266 : helix II	38		Solyom et al., 2015
HCV			292–306 : helix III	51
4EBP2	120	P	1–5	15~37	eIF4E	Lukhele et al., 2013
	(1–120)		33–37
			50–64
			86–89
			96–105
E7	40	R	8–13 : helix	NA	E2	Noval et al., 2013
HPV	(1–40)		17–29 : helix
HPV			33–38 : PPII
4EBP1	70	R	56–63 : helix	20	eIF4E	Kim et al., 2015
4EBP1	(49–118)
Myb32	32	R	290–310 : helix	~70	KIX	Arai et al., 2015
Myb32	(284–315)
E7	46	R	7–14 : helix	10	E2	Lee et al., 2016
HPV	(1–46)		20–26 : helix	20
CBP-ID4	207	R	1852–1875: helix	~60	-	Piai et al., 2016
CBP-ID4	(1851–2057)		1951–1978: helix
HIV-1 Tat	121	P	27–32: helix	~20	Fab’	To et al., 2016
	(1–121)^a		41–59: helix	~30	P-TEFb
			70–81: β sheet	~25	TAR-cyclin T1
			93–99: β sheet	~25
			105–112: β sheet	~10
SUSP4	100	R	263–291 : helix	~30	mdm2	Kim et al., 2017
	(201–300)		265–270 : helix	~10
			281–291 : helix
hGRtau1c	64	R	185–202: helix	20~30	TAZ2	Kim et al., 2017
	(181–244)		206–225: helix
			232–244: helix
Huntingtin Httex1 25Q	95	P	18–42: helix	NA	Cytotoxic	Newcombe et al., 2018
	(1–95)				Membrane binding
					Aggregation

The numbering includes a 20-residue N-terminal tag.

An IDP (P) versus an IDR (R).

Residue numbers are taken from the original report.

Population of PreSMos are read from the mid-point of the SSP scores that are calculated from chemical shifts in BMRB or literature. Shown in bold are the populations described in the original report. When the populations described in the original report without SSP scores differed significantly from the calculated SSP scores, the SSP scores are provided in parenthesis.

NA = not available.

Determined by SAXS.