Saccharomyces cerevisiae (S288c)

GSP2

CNR2, Ran GTPase GSP2, L000000737, YOR185C

GTP binding protein (mammalian Ranp homolog); involved in the maintenance of nuclear organization, RNA processing and transport; interacts with Kap121p, Kap123p and Pdr6p (karyophilin betas); not required for viability; protein abundance increases in response to DNA replication stress; GSP2 has a paralog, GSP1, that arose from the whole genome duplication

GO Process (1)

GO Function (1)

GO Component (2)

Gene Ontology Biological Process

nucleus organization [IGI, ISS]

Gene Ontology Molecular Function

GTPase activity [IGI, ISS]

Gene Ontology Cellular Component

integral component of membrane [ISM]

nucleus [IGI, ISS]

SGD Alliance of Genome Resources Entrez Gene RefSeq UniprotKB

Download Curated Data for this Protein

34580

559292

Interactor Statistics

Proteins/Genes

178

Publications

Interactors w/ Physical (HTP) Evidence (140)
Interactors w/ Physical (LTP) Evidence (23)
Interactors w/ Genetic (HTP) Evidence (3)
Interactors w/ More than One Evidence Type (12)

Interactors 114
Interactions 130
Network
PTM Sites 12

Sites with Multi-PTMs

Displaying 1 protein 1 non-assigned with 12 total post translational modifications

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NP_014828

Ran GTPase GSP2

Length: 220

1
MSAPAQNNAE VPTFKLVLVG DGGTGKTTFV KRHLTGEFEK KYIATIGVEV
51
HPLSFYTNFG EIKFDVWDTA GQEKFGGLRD GYYINAQCAI IMFDVTSRIT
101
YKNVPNWHRD LVRVCENIPI VLCGNKVDVK ERKVKAKTIT FHRKKNLQYY
151
DISAKSNYNF EKPFLWLARK LAGNPQLEFV ASPALAPPEV QVDEQLMHQY
201
QQEMDQATAL PLPDEDDADL

Location	PTM	Residue	Source(s)	Note(s)
2	Phosphorylation	S	Helbig AO (2010)	eyJOT1RFUyI6WyJQTUlEIDIxMTI2MzM2OiBQcmVkaWN0ZWQgcHJvdGVpbiBraW5hc2UgPSBSSU0xMSwgYWNjdW11bGF0ZXMgaW4gbmF0MyBjZWxscy4iXX0=
15	Ubiquitination	K	Mayor T (2005)	-
26	Ubiquitination	K	Mayor T (2005)	-
102	Ubiquitination	K	Swaney DL (2013)	-
126	Ubiquitination	K	Beltrao P (2012)	-
			Mayor T (2005)	-
			Swaney DL (2013)	-
130	Ubiquitination	K	Beltrao P (2012)	-
133	Ubiquitination	K	Beltrao P (2012)	-
135	Ubiquitination	K	Beltrao P (2012)	-
137	Ubiquitination	K	Beltrao P (2012)	-
155	Ubiquitination	K	Iesmantavicius V (2014)	-

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Non-Assigned PTMs

Post translational modifications that are currently unassigned to a specific residue location.

Location	PTM	Residue	Source(s)	Note(s)
-	Sumoylation	K	Wohlschlegel JA (2004)	eyJOT1RFUyI6WyJIaXMtdGFnZ2VkIFNtdDNwIChTVU1PKSB3YXMgdXNlZCB0byBpZGVudGlmeSBzdW1veWxhdGVkIHN1YnN0cmF0ZXMuIl0sIlJFTEFUSU9OU0hJUFMiOnsiU01UMyI6IjxzcGFuPjxhIGhyZWY9J2h0dHBzOlwvXC90aGViaW9ncmlkLm9yZ1wvMzI1NjFcL3N1bW1hcnlcL3NhY2NoYXJvbXljZXMtY2VyZXZpc2lhZVwvc210My5odG1sJyBhbHQ9J1NNVDMnPlNNVDM8XC9hPjxcL3NwYW4+In19
-	Ubiquitination	K	Ziv I (2011)	eyJSRUxBVElPTlNISVBTIjp7IlVCSTQiOiI8c3Bhbj48YSBocmVmPSdodHRwczpcL1wvdGhlYmlvZ3JpZC5vcmdcLzMxMjE1XC9zdW1tYXJ5XC9zYWNjaGFyb215Y2VzLWNlcmV2aXNpYWVcL3ViaTQuaHRtbCcgYWx0PSdVQkk0Jz5VQkk0PFwvYT48XC9zcGFuPiJ9fQ==

Relationships

Protein	Relationship	Location	PTM	Residue	Identity	Source(s)
SMT3	Conjugate	-	Sumoylation	K	PTM	Wohlschlegel JA (2004)
UBI4	Conjugate	-	Ubiquitination	K	PTM	Ziv I (2011)

Result Summary