UniProt Accession

 SEPT7_HUMAN; Q16181; Q52M76; Q6NX50 

Genbank Protein ID

 S72008; BC067264; BC093640; BC093642 

Genbank Nucleotide ID

 AAB31337.1; AAH67264.2; AAH93640.2; AAH93642.2 

Protein Name

 Septin-7 

Protein Synonyms/Alias

 CDC10 protein homolog 

Gene Name

 SEPT7 

Gene Synonyms/Alias

 CDC10 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
88	PGPSHRIKKTVQVEQ	ubiquitination	[1]
89	GPSHRIKKTVQVEQS	ubiquitination	[1]
97	TVQVEQSKVLIKEGG	acetylation	[2]
97	TVQVEQSKVLIKEGG	ubiquitination	[1, 3]
181	PLDIEFMKRLHEKVN	acetylation	[2]
186	FMKRLHEKVNIIPLI	acetylation	[2]
186	FMKRLHEKVNIIPLI	ubiquitination	[1, 3]
195	NIIPLIAKADTLTPE	ubiquitination	[1]
208	PEECQQFKKQIMKEI	ubiquitination	[1]
209	EECQQFKKQIMKEIQ	ubiquitination	[4]
213	QFKKQIMKEIQEHKI	acetylation	[2]
213	QFKKQIMKEIQEHKI	ubiquitination	[1]
235	TDDEEENKLVKKIKD	ubiquitination	[1]
238	EEENKLVKKIKDRLP	ubiquitination	[1]
239	EENKLVKKIKDRLPL	ubiquitination	[1]
298	RTHMQDLKDVTNNVH	ubiquitination	[1, 3, 4]
313	YENYRSRKLAAVTYN	ubiquitination	[1]
328	GVDNNKNKGQLTKSP	ubiquitination	[1]
333	KNKGQLTKSPLAQME	ubiquitination	[1]
373	KEKVQKLKDSEAELQ	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. 

Sequence Annotation

 NP_BIND 57 64 GTP.
 NP_BIND 195 203 GTP (By similarity).
 BINDING 90 90 GTP (By similarity).
 BINDING 116 116 GTP; via amide nitrogen (By similarity).
 BINDING 250 250 GTP; via amide nitrogen and carbonyl
 BINDING 265 265 GTP (By similarity).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 30 30 Phosphotyrosine (By similarity).
 MOD_RES 228 228 Phosphothreonine (By similarity).
 MOD_RES 334 334 Phosphoserine.
 MOD_RES 424 424 Phosphoserine.
 MOD_RES 426 426 Phosphothreonine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division; Cell projection; Centromere; Chromosome; Cilium; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; Kinetochore; Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 437 AA 

Protein Sequence

Gene Ontology

 GO:0043679; C:axon terminus; IEA:Compara.
 GO:0035085; C:cilium axoneme; ISS:UniProtKB.
 GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0031105; C:septin complex; IEA:InterPro.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0045202; C:synapse; IEA:Compara.
 GO:0005525; F:GTP binding; TAS:ProtInc.
 GO:0005198; F:structural molecule activity; TAS:ProtInc.
 GO:0060271; P:cilium morphogenesis; ISS:UniProtKB.
 GO:0000910; P:cytokinesis; TAS:ProtInc.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
 GO:0016476; P:regulation of embryonic cell shape; ISS:UniProtKB. 

Interpro

 IPR000038; Cell_div_GTP-bd.
 IPR027417; P-loop_NTPase.
 IPR016491; Septin.
 IPR008115; Septin7. 

Pfam

 PF00735; Septin 

SMART

  

PROSITE

  

PRINTS

 PR01742; SEPTIN7.