CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012660
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
234TDDEEENKLVKKIKDubiquitination[1]
297RTHMQDLKDVTNNVHubiquitination[1]
394KNLEAQHKELEEKRRubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
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
MSVSARSAAA EERSVNSSTM AQQKNLEGYV GFANLPNQVY RKSVKRGFEF TLMVVGESGL 60
GKSTLINSLF LTDLYSPEYP GPSHRIKKTV QVEQSKVLIK EGGVQLLLTI VDTPGFGDAV 120
DNSNCWQPVI DYIDSKFEDY LNAESRVNRR QMPDNRVQCC LYFIAPSGHG LKPLDIEFMK 180
RLHEKVNIIP LIAKADTLTP EECQQFKKQI MKEIQEHKIK IYEFPETDDE EENKLVKKIK 240
DRLPLAVVGS NTIIEVNGKR VRGRQYPWGV AEVENGEHCD FTILRNMLIR THMQDLKDVT 300
NNVHYENYRS RKLAAVTYNG VDNNKNKGQL TKSPLAQMEE ERREHVAKMK KMEMEMEQVF 360
EMKVKEKVQK LKDSEAELQR RHEQMKKNLE AQHKELEEKR RQFEDEKANW EAQQRILEQQ 420
NSSRTLEKNK KKGKIF 436 
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.