ISCU_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ISCU_HUMAN
• UniProt AC: Q9H1K1
• Protein Name: Iron-sulfur cluster assembly enzyme ISCU, mitochondrial
• Gene Name: ISCU
• Organism: Homo sapiens (Human).
• Sequence Length: 167
• Subcellular Localization: Isoform 1: Mitochondrion .; Isoform 2: Cytoplasm. Nucleus .
• Protein Description: Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. [PubMed: 11060020 First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein ISCU. In a second step, the cluster is released from ISCU, transferred to a glutaredoxin GLRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISCU depends on the function of the cysteine desulfurase complex NFS1-LYRM4/ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH (By similarity]
• Protein Sequence: MAAAGAFRLRRAASALLLRSPRLPARELSAPARLYHKKVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQEPKKGEAEKK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7 (in isoform 2)	Phosphorylation	-	8.06	25404012
11 (in isoform 2)	Phosphorylation	-	38.81	20068231
12 (in isoform 2)	Phosphorylation	-	10.19	20068231
14	Phosphorylation	FRLRRAASALLLRSP HHHHHHHHHHHHCCC	20.61	19664994
18 (in isoform 2)	Phosphorylation	-	5.46	20068231
20	Phosphorylation	ASALLLRSPRLPARE HHHHHHCCCCCCHHH	17.84	26055452
29	Phosphorylation	RLPARELSAPARLYH CCCHHHHCCCCHHHC	27.70	30266825
29 (in isoform 2)	Ubiquitination	-	27.70	21890473
32 (in isoform 2)	Ubiquitination	-	17.52	21890473
43	Phosphorylation	HKKVVDHYENPRNVG CHHHHCCCCCCCCCC	16.97	25884760
51	Phosphorylation	ENPRNVGSLDKTSKN CCCCCCCCCCCCCCC	29.16	-
54	Ubiquitination	RNVGSLDKTSKNVGT CCCCCCCCCCCCCCC	61.05	21890473
54 (in isoform 1)	Ubiquitination	-	61.05	21890473
57 (in isoform 2)	Ubiquitination	-	61.97	21890473
57	Ubiquitination	GSLDKTSKNVGTGLV CCCCCCCCCCCCCCC	61.97	21890473
57 (in isoform 1)	Ubiquitination	-	61.97	21890473
66 (in isoform 2)	Ubiquitination	-	4.88	21890473
69	Glutathionylation	GLVGAPACGDVMKLQ CCCCCCCCCCEEEEE	4.68	22555962
73	Sulfoxidation	APACGDVMKLQIQVD CCCCCCEEEEEEEEC	4.22	21406390
82 (in isoform 1)	Ubiquitination	-	62.13	21890473
82	Ubiquitination	LQIQVDEKGKIVDAR EEEEECCCCCEEEEE	62.13	21890473
82	2-Hydroxyisobutyrylation	LQIQVDEKGKIVDAR EEEEECCCCCEEEEE	62.13	-
87 (in isoform 2)	Ubiquitination	-	35.18	21890473
91 (in isoform 1)	Ubiquitination	-	37.07	21890473
91	Ubiquitination	KIVDARFKTFGCGSA CEEEEEEEEECCCHH	37.07	21890473
92	Phosphorylation	IVDARFKTFGCGSAI EEEEEEEEECCCHHH	23.65	21406692
96 (in isoform 2)	Ubiquitination	-	22.08	21890473
97	Phosphorylation	FKTFGCGSAIASSSL EEEECCCHHHHCCHH	22.15	18669648
101	Phosphorylation	GCGSAIASSSLATEW CCCHHHHCCHHCHHH	17.85	18669648
102	Phosphorylation	CGSAIASSSLATEWV CCHHHHCCHHCHHHH	21.98	18669648
103	Phosphorylation	GSAIASSSLATEWVK CHHHHCCHHCHHHHC	21.37	21406692
106	Phosphorylation	IASSSLATEWVKGKT HHCCHHCHHHHCCCC	35.36	21406692
112	Ubiquitination	ATEWVKGKTVEEALT CHHHHCCCCHHHHHH	43.62	21890473
112 (in isoform 1)	Ubiquitination	-	43.62	21890473
121	Ubiquitination	VEEALTIKNTDIAKE HHHHHHCCCCHHHHH	48.86	21890473
121 (in isoform 1)	Ubiquitination	-	48.86	21890473
122 (in isoform 2)	Ubiquitination	-	38.85	21890473
127	Acetylation	IKNTDIAKELCLPPV CCCCHHHHHHCCCCC	52.10	25038526
147	Ubiquitination	MLAEDAIKAALADYK HHHHHHHHHHHHHHH	29.36	21890473
147 (in isoform 1)	Ubiquitination	-	29.36	21890473

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
14	S	Phosphorylation	Kinase	MTOR	P42345	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ISCU_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ISCU_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUP62_HUMAN	NUP62	physical	25416956
NECA2_HUMAN	NECAB2	physical	25416956
BANP_HUMAN	BANP	physical	25416956
ATRAP_HUMAN	AGTRAP	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
CC172_HUMAN	CCDC172	physical	25416956
HSC20_HUMAN	HSCB	physical	24573684
NFS1_HUMAN	NFS1	physical	24573684
NECA2_HUMAN	NECAB2	physical	21516116

Drug and Disease Associations

• Kegg Disease
• OMIM Disease
• 255125: Myopathy with exercise intolerance Swedish type (MEIS)
• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, VARIANT VAL-12, ANDMASS SPECTROMETRY.
PubMed: 19690332

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-14, AND MASSSPECTROMETRY.
PubMed: 18669648