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Q8IYM1 (SEP12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Septin-12
Gene names
Name:SEPT12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Filament-forming cytoskeletal GTPase By similarity. May play a role in cytokinesis Potential.

Subunit structure

Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation By similarity. Interacts with SEPT6 and SEPT11. Forms homodimers. Ref.2 Ref.8

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonspindle. Cell projectionciliumflagellum. Note: At interphase, forms a filamentous structure in the cytoplasm. During anaphase, translocates to the central spindle region and to the midbody during cytokinesis. Found in the sperm annulus. Ref.2 Ref.9

Tissue specificity

Widely expressed. Ref.7

Involvement in disease

Spermatogenic failure 10 (SPGF10) [MIM:614822]: An infertility disorder caused by spermatogenesis defects. It results in decreased sperm motility, concentration, and multiple sperm structural defects. The most prominent feature is a defective sperm annulus, a ring structure that demarcates the midpiece and the principal piece of the sperm tail.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the septin family.

Sequence caution

The sequence AAH24017.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SEPT6Q141413EBI-2585067,EBI-745901

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IYM1-1)

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: Q8IYM1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     125-170: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Septin-12
PRO_0000312860

Regions

Nucleotide binding56 – 638GTP By similarity
Nucleotide binding195 – 2039GTP By similarity

Sites

Binding site891GTP By similarity
Binding site1151GTP; via amide nitrogen By similarity
Binding site2511GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2661GTP By similarity

Natural variations

Alternative sequence125 – 17046Missing in isoform 2.
VSP_029918
Natural variant891T → M in SPGF10; results in significantly reduced GTP hydrolysis. Ref.9
Corresponds to variant rs199696526 [ dbSNP | Ensembl ].
VAR_068097
Natural variant1971D → N in SPGF10; results in significantly reduced GTP hydrolysis due to impaired GTP binding. Ref.9
VAR_068098
Natural variant2131Q → R.
Corresponds to variant rs6500633 [ dbSNP | Ensembl ].
VAR_057176

Experimental info

Mutagenesis561G → N: Abolishes binding to GTP and to SEPT11, and also abolishes the ability of SEPT12 to form filamentous structures. Ref.8
Sequence conflict221P → T in AAH24017. Ref.6
Sequence conflict2581V → M in BAB71681. Ref.4
Sequence conflict2801H → L in AAH24017. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 31968F366DEFB4FD

FASTA35840,748
        10         20         30         40         50         60 
MDPLRRSPSP CLSSQPSSPS TPPCEMLGPV GIEAVLDQLK IKAMKMGFEF NIMVVGQSGL 

        70         80         90        100        110        120 
GKSTMVNTLF KSKVWKSNPP GLGVPTPQTL QLHSLTHVIE EKGVKLKLTV TDTPGFGDQI 

       130        140        150        160        170        180 
NNDNCWDPIL GYINEQYEQY LQEEILITRQ RHIPDTRVHC CVYFVPPTGH CLRPLDIEFL 

       190        200        210        220        230        240 
QRLCRTVNVV PVIARADSLT MEEREAFRRR IQQNLRTHCI DVYPQMCFDE DINDKILNSK 

       250        260        270        280        290        300 
LRDRIPFAVV GADQEHLVNG RCVLGRKTKW GIIEVENMAH CEFPLLRDLL IRSHLQDLKD 

       310        320        330        340        350 
ITHNIHYENY RVIRLNESHL LPRGPGWVNL APASPGQLTT PRTFKVCRGA HDDSDDEF 

« Hide

Isoform 2 [UniParc].

Checksum: A9C83873ABB4CBE4
Show »

FASTA31235,191

References

« Hide 'large scale' references
[1]"Sept12 is a component of the mammalian sperm tail annulus."
Steels J.D., Estey M.P., Froese C.D., Reynaud D., Pace-Asciak C., Trimble W.S.
Cell Motil. Cytoskeleton 64:794-807(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 1).
[2]"SEPT12 interacts with SEPT6 and this interaction alters the filament structure of SEPT6 in Hela cells."
Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.
J. Biochem. Mol. Biol. 40:973-978(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SEPT6 AND SEPT11, SUBCELLULAR LOCATION.
Tissue: Testis.
[3]"Molecular cloning of septin 12 transcript variant 2 from human testis."
Wang J.R., Xing X.W., Jiang X.Z., Tang Y.X., Yang J.F., Dai Y.B., Tan J.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Testis.
[7]"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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"GTP binding is required for SEPT12 to form filaments and to interact with SEPT11."
Ding X., Yu W., Liu M., Shen S., Chen F., Cao L., Wan B., Yu L.
Mol. Cells 25:385-389(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, INTERACTION WITH SEPT11, GTP-BINDING, MUTAGENESIS OF GLY-56.
[9]"SEPT12 mutations cause male infertility with defective sperm annulus."
Kuo Y.C., Lin Y.H., Chen H.I., Wang Y.Y., Chiou Y.W., Lin H.H., Pan H.A., Wu C.M., Su S.M., Hsu C.C., Kuo P.L.
Hum. Mutat. 33:710-719(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, VARIANTS SPGF10 MET-89 AND ASN-197, CHARACTERIZATION OF VARIANTS SPGF10 MET-89 AND ASN-197.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ456996 mRNA. Translation: ABE68946.1.
DQ517531 mRNA. Translation: ABF61438.1.
EF620906 mRNA. Translation: ABR10901.1.
AK058139 mRNA. Translation: BAB71681.1.
CH471112 Genomic DNA. Translation: EAW85265.1.
BC024017 mRNA. Translation: AAH24017.1. Different initiation.
BC035619 mRNA. Translation: AAH35619.1.
RefSeqNP_001147930.1. NM_001154458.2.
NP_653206.2. NM_144605.4.
UniGeneHs.126780.

3D structure databases

ProteinModelPortalQ8IYM1.
SMRQ8IYM1. Positions 48-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125863. 1 interaction.
IntActQ8IYM1. 1 interaction.
STRING9606.ENSP00000268231.

PTM databases

PhosphoSiteQ8IYM1.

Polymorphism databases

DMDM74750767.

Proteomic databases

PaxDbQ8IYM1.
PRIDEQ8IYM1.

Protocols and materials databases

DNASU124404.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268231; ENSP00000268231; ENSG00000140623. [Q8IYM1-1]
ENST00000396693; ENSP00000379922; ENSG00000140623. [Q8IYM1-2]
GeneID124404.
KEGGhsa:124404.
UCSCuc002cxq.3. human. [Q8IYM1-1]
uc002cxr.3. human. [Q8IYM1-2]

Organism-specific databases

CTD124404.
GeneCardsGC16M004829.
HGNCHGNC:26348. SEPT12.
HPAHPA041128.
MIM611562. gene.
614822. phenotype.
neXtProtNX_Q8IYM1.
PharmGKBPA162402916.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5019.
HOGENOMHOG000233586.
HOVERGENHBG065093.
InParanoidQ8IYM1.
KOK16938.
OMAIRLNESH.
PhylomeDBQ8IYM1.
TreeFamTF101078.

Gene expression databases

ArrayExpressQ8IYM1.
BgeeQ8IYM1.
CleanExHS_SEPT12.
GenevestigatorQ8IYM1.

Family and domain databases

InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi124404.
NextBio81269.
PROQ8IYM1.
SOURCESearch...

Entry information

Entry nameSEP12_HUMAN
AccessionPrimary (citable) accession number: Q8IYM1
Secondary accession number(s): Q0P6B0, Q1PBH0, Q96LL0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: March 1, 2003
Last modified: March 19, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM