Q16181 (SEPT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Septin-7

Alternative name(s):
CDC10 protein homolog

Gene names

Name:	SEPT7
Synonyms:	CDC10

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.13
Subunit structure	Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Within the trimer, directly interacts with SEPT6, while interaction with SEPT2 seems indirect. In the absence of SEPT6, forms homodimers. Interacts directly with CENPE and links CENPE to septin filaments composed of SEPT2, SEPT6 and SEPT7. Interacts with SEPT5 and SEPT8 By similarity. Interacts with SEPT9 and SEPT11. Ref.3 Ref.8 Ref.13 Ref.16 Ref.19
Subcellular location	Cytoplasm. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › spindle. Cleavage furrow. Midbody. Cytoplasm › cytoskeleton › cilium axoneme By similarity. Note: Distributed throughout the cytoplasm in prometaphase cells. Associated with the spindle during metaphase. Associated with the central spindle and at the cleavage furrow in anaphase cells. Detected at the midbody in telophase. Associated with actin stress fibers By similarity. Ref.13
Tissue specificity	Widely expressed. Ref.4
Miscellaneous	Coordinated expression with SEPT2 and SEPT6.
Sequence similarities	Belongs to the septin family.
Sequence caution	The sequence AAB31337.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH67264.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH93640.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH93642.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cell projection Centromere Chromosome Cilium Cytoplasm Cytoskeleton Kinetochore
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cilium morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB cytokinesis Traceable author statement. Source: ProtInc mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein heterooligomerization Inferred from direct assay Ref.3. Source: UniProtKB regulation of embryonic cell shape Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cilium axoneme Inferred from sequence or structural similarity. Source: UniProtKB cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA septin complex Inferred from electronic annotation. Source: InterPro spindle Inferred from electronic annotation. Source: UniProtKB-SubCell stress fiber Inferred from direct assay Ref.3. Source: UniProtKB
Molecular function	GTP binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.3. Source: UniProtKB structural molecule activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16181-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q16181-2)

The sequence of this isoform differs from the canonical sequence as follows:
     21-21: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 437

437

Septin-7

PRO_0000173528

Regions

Nucleotide binding

57 – 64

8

GTP

Nucleotide binding

195 – 203

9

GTP By similarity

Coiled coil

332 – 437

106

Potential

Sites

Binding site

90

1

GTP By similarity

Binding site

116

1

GTP; via amide nitrogen By similarity

Binding site

250

1

GTP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

265

1

GTP By similarity

Amino acid modifications

Modified residue

30

1

Phosphotyrosine Ref.10

Modified residue

186

1

N6-acetyllysine Ref.17

Modified residue

213

1

N6-acetyllysine Ref.17

Modified residue

228

1

Phosphothreonine By similarity

Modified residue

319

1

Phosphotyrosine Ref.6

Modified residue

334

1

Phosphoserine Ref.7 Ref.12 Ref.14

Modified residue

423

1

Phosphoserine Ref.11

Modified residue

424

1

Phosphoserine Ref.14

Modified residue

426

1

Phosphothreonine Ref.11 Ref.14 Ref.15

Natural variations

Alternative sequence

21

1

Missing in isoform 2.

VSP_022202

Experimental info

Sequence conflict

271

1

V → I in AAB31337. Ref.1

Sequence conflict

289

1

L → K in AAB31337. Ref.1

Secondary structure

1

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437

Helix Strand Turn

Details...

Turn

40 – 44

5

Beta strand

51 – 56

6

Helix

64 – 70

7

Beta strand

92 – 97

6

Beta strand

107 – 113

7

Helix

128 – 141

14

Turn

142 – 144

3

Beta strand

160 – 164

5

Helix

174 – 183

10

Turn

184 – 186

3

Beta strand

187 – 195

9

Helix

201 – 218

18

Beta strand

246 – 248

3

Turn

281 – 283

3

Helix

284 – 290

7

Helix

294 – 304

11

Helix

306 – 313

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2005. Version 2. Checksum: 946A08C54B7124FF	FASTA	437	50,680
	10 20 30 40 50 60 MSVSARSAAA EERSVNSSTM VAQQKNLEGY VGFANLPNQV YRKSVKRGFE FTLMVVGESG 70 80 90 100 110 120 LGKSTLINSL FLTDLYSPEY PGPSHRIKKT VQVEQSKVLI KEGGVQLLLT IVDTPGFGDA 130 140 150 160 170 180 VDNSNCWQPV IDYIDSKFED YLNAESRVNR RQMPDNRVQC CLYFIAPSGH GLKPLDIEFM 190 200 210 220 230 240 KRLHEKVNII PLIAKADTLT PEECQQFKKQ IMKEIQEHKI KIYEFPETDD EEENKLVKKI 250 260 270 280 290 300 KDRLPLAVVG SNTIIEVNGK RVRGRQYPWG VAEVENGEHC DFTILRNMLI RTHMQDLKDV 310 320 330 340 350 360 TNNVHYENYR SRKLAAVTYN GVDNNKNKGQ LTKSPLAQME EERREHVAKM KKMEMEMEQV 370 380 390 400 410 420 FEMKVKEKVQ KLKDSEAELQ RRHEQMKKNL EAQHKELEEK RRQFEDEKAN WEAQQRILEQ 430 QNSSRTLEKN KKKGKIF
	Isoform 2 [UniParc]. Checksum: 803345D98374253B	FASTA	436	50,581
	10 20 30 40 50 60 MSVSARSAAA EERSVNSSTM AQQKNLEGYV GFANLPNQVY RKSVKRGFEF TLMVVGESGL 70 80 90 100 110 120 GKSTLINSLF LTDLYSPEYP GPSHRIKKTV QVEQSKVLIK EGGVQLLLTI VDTPGFGDAV 130 140 150 160 170 180 DNSNCWQPVI DYIDSKFEDY LNAESRVNRR QMPDNRVQCC LYFIAPSGHG LKPLDIEFMK 190 200 210 220 230 240 RLHEKVNIIP LIAKADTLTP EECQQFKKQI MKEIQEHKIK IYEFPETDDE EENKLVKKIK 250 260 270 280 290 300 DRLPLAVVGS NTIIEVNGKR VRGRQYPWGV AEVENGEHCD FTILRNMLIR THMQDLKDVT 310 320 330 340 350 360 NNVHYENYRS RKLAAVTYNG VDNNKNKGQL TKSPLAQMEE ERREHVAKMK KMEMEMEQVF 370 380 390 400 410 420 EMKVKEKVQK LKDSEAELQR RHEQMKKNLE AQHKELEEKR RQFEDEKANW EAQQRILEQQ 430 NSSRTLEKNK KKGKIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a novel human cDNA homologous to CDC10 in Saccharomyces cerevisiae." Nakatsuru S., Sudo K., Nakamura Y. Biochem. Biophys. Res. Commun. 202:82-87(1994) [PubMed: 8037772] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-437 (ISOFORM 1). Tissue: Fetal lung.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-437 (ISOFORMS 1 AND 2). Tissue: Brain and Uterus.
[3]	"Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11." Nagata K., Asano T., Nozawa Y., Inagaki M. J. Biol. Chem. 279:55895-55904(2004) [PubMed: 15485874] [Abstract] Cited for: INTERACTION WITH SEPT9 AND SEPT11.
[4]	"Expression profiling the human septin gene family." Hall P.A., Jung K., Hillan K.J., Russell S.E.H. J. Pathol. 206:269-278(2005) [PubMed: 15915442] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4." Kremer B.E., Haystead T., Macara I.G. Mol. Biol. Cell 16:4648-4659(2005) [PubMed: 16093351] [Abstract] Cited for: COORDINATED EXPRESSION WITH SEPT2 AND SEPT6.
[6]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-319, MASS SPECTROMETRY.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Structural analysis of septin 2, 6, and 7 complexes." Low C., Macara I.G. J. Biol. Chem. 281:30697-30706(2006) [PubMed: 16914550] [Abstract] Cited for: INTERACTION WITH SEPT2 AND SEPT6, HOMODIMERIZATION.
[9]	"Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7." Kremer B.E., Adang L.A., Macara I.G. Cell 130:837-850(2007) [PubMed: 17803907] [Abstract] Cited for: FUNCTION.
[10]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND THR-426, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Septin 7 interacts with centromere-associated protein E and is required for its kinetochore localization." Zhu M., Wang F., Yan F., Yao P.Y., Du J., Gao X., Wang X., Wu Q., Ward T., Li J., Kioko S., Hu R., Xie W., Ding X., Yao X. J. Biol. Chem. 283:18916-18925(2008) [PubMed: 18460473] [Abstract] Cited for: INTERACTION WITH CENPE, SUBCELLULAR LOCATION, FUNCTION.
[14]	"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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-424 AND THR-426, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-426, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Septins regulate bacterial entry into host cells." Mostowy S., Nam Tham T., Danckaert A., Guadagnini S., Boisson-Dupuis S., Pizarro-Cerda J., Cossart P. PLoS ONE 4:E4196-E4196(2009) [PubMed: 19145258] [Abstract] Cited for: INTERACTION WITH SEPT9.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-186 AND LYS-213, MASS SPECTROMETRY.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Structural insight into filament formation by mammalian septins." Sirajuddin M., Farkasovsky M., Hauer F., Kuehlmann D., Macara I.G., Weyand M., Stark H., Wittinghofer A. Nature 449:311-315(2007) [PubMed: 17637674] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 20-437 IN COMPLEX WITH GDP, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S72008 mRNA. Translation: AAB31337.1. Different initiation.
BC067264 mRNA. Translation: AAH67264.2. Different initiation.
BC093640 mRNA. Translation: AAH93640.2. Different initiation.
BC093642 mRNA. Translation: AAH93642.2. Different initiation.

IPI

IPI00816201.
IPI00941534.

PIR

JC2352.

RefSeq

NP_001779.3. NM_001788.5.

UniGene

Hs.191346.
Hs.632906.
Hs.642540.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QAG	X-ray	4.00	C	20-437	[»]
3T5D	X-ray	3.30	A/C	48-316	[»]
3TW4	X-ray	3.35	A/B	48-317	[»]

ProteinModelPortal

Q16181.

SMR

Q16181. Positions 49-316.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16181. 8 interactions.

STRING

Q16181.

PTM databases

PhosphoSite

Q16181.

Polymorphism databases

DMDM

67472677.

2D gel databases

OGP

Q16181.

UCD-2DPAGE

Q16181.

Proteomic databases

PRIDE

Q16181.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000399034; ENSP00000381992; ENSG00000122545.

GeneID

989.

KEGG

hsa:989.

Organism-specific databases

CTD

989.

GeneCards

GC07P035807.

H-InvDB

HIX0032379.

HGNC

HGNC:1717. SEPT7.

HPA

HPA023309.
HPA029524.

MIM

603151. gene.

neXtProt

NX_Q16181.

PharmGKB

PA26253.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG715249.

HOVERGEN

HBG065093.

InParanoid

Q16181.

PhylomeDB

Q16181.

Gene expression databases

ArrayExpress

Q16181.

Bgee

Q16181.

CleanEx

HS_SEPT7.

Genevestigator

Q16181.

GermOnline

ENSG00000122545. Homo sapiens.

Family and domain databases

InterPro

IPR000038. Cell_div_GTP-bd.
IPR016491. Septin.
IPR008115. Septin7.
[Graphical view]

PANTHER

PTHR18884. Cell_Div_GTP_bd. 1 hit.

Pfam

PF00735. Septin. 1 hit.
[Graphical view]

PIRSF

PIRSF006698. Septin. 1 hit.

PRINTS

PR01742. SEPTIN7.

ProtoNet

Search...

Other

NextBio

4150.

SOURCE

Search...

Entry information

Entry name

SEPT7_HUMAN

Accession

Primary (citable) accession number: Q16181
Secondary accession number(s): Q52M76, Q6NX50

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 10, 2005
Last modified:	January 25, 2012
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.