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Q08AE8 (SPIR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Protein spire homolog 1

Short name=Spir-1
Gene names
Name:SPIRE1
Synonyms:KIAA1135, SPIR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. Ref.7 Ref.9 UniProtKB Q9U1K1

Subunit structure

Interacts with FMN2. Ref.11 Ref.12

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion By similarity. Punctate spots in perinuclear region and cytoplasm, colocalized with Rab11. Ref.7

Domain

Binds to actin monomers via the WH2 domain By similarity. UniProtKB Q9U1K1

The Spir-box targets binding to intracellular membrane structures. Ref.7

Sequence similarities

Belongs to the spire family.

Contains 1 KIND domain.

Contains 2 WH2 domains.

Sequence caution

The sequence AAI15006.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI25207.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI25208.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA86449.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi vesicle transport

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton organization

Inferred from mutant phenotype Ref.9. Source: UniProtKB

cleavage furrow formation

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of meiotic spindle localization

Inferred from mutant phenotype Ref.9. Source: UniProtKB

formin-nucleated actin cable assembly

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular transport

Inferred from sequence or structural similarity. Source: UniProtKB

polar body extrusion after meiotic divisions

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YWHAQP273481EBI-1055655,EBI-359854

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.6 (identifier: Q08AE8-1)

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.
Note: No experimental confirmation available.
Isoform 2 Ref.6 Ref.7 (identifier: Q08AE8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     397-410: Missing.
Isoform 3 (identifier: Q08AE8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     397-410: Missing.
Isoform 4 (identifier: Q08AE8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     397-410: Missing.
     616-756: RPVCSQCCKK...CPSERTISEI → SDCLFNGTAHCQFYLG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 756755Protein spire homolog 1
PRO_0000309569

Regions

Domain40 – 231192KIND
Domain305 – 32319WH2 1
Domain369 – 38618WH2 2
Region131 – 1388Important for interaction with FMN2
Region556 – 57621Spir-box
Coiled coil229 – 25729 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue4641Phosphoserine Ref.8
Modified residue4651Phosphoserine Ref.8
Modified residue4671Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 159159Missing in isoform 3 and isoform 4.
VSP_037925
Alternative sequence397 – 41014Missing in isoform 2, isoform 3 and isoform 4.
VSP_052595
Alternative sequence616 – 756141RPVCS…TISEI → SDCLFNGTAHCQFYLG in isoform 4.
VSP_037926
Natural variant2491Q → P.
Corresponds to variant rs1785296 [ dbSNP | Ensembl ].
VAR_058695

Experimental info

Mutagenesis1311I → K: Strongly reduces interaction with FMN2. Ref.12
Mutagenesis1341Y → K: Abolishes interaction with FMN2. Ref.11
Mutagenesis1381D → N: Abolishes interaction with FMN2. Ref.11 Ref.12
Mutagenesis1461E → A or K: Abolishes interaction with FMN2. Ref.12

Secondary structure

.......................... 756
Helix Strand Turn

Details...

Sequences

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

Last modified November 28, 2012. Version 3.
Checksum: 1379B39C8CA9DDB3

FASTA75685,544
        10         20         30         40         50         60 
MAQAAGPAGG GEPRTEAVGG EGPREPGAAG GAAGGSRDAL SLEEILRLYN QPINEEQAWA 

        70         80         90        100        110        120 
VCYQCCGSLR AAARRRQPRH RVRSAAQIRV WRDGAVTLAP AADDAGEPPP VAGKLGYSQC 

       130        140        150        160        170        180 
METEVIESLG IIIYKALDYG LKENEERELS PPLEQLIDHM ANTVEADGSN DEGYEAAEEG 

       190        200        210        220        230        240 
LGDEDEKRKI SAIRSYRDVM KLCAAHLPTE SDAPNHYQAV CRALFAETME LHTFLTKIKS 

       250        260        270        280        290        300 
AKENLKKIQE MEKSDESSTD LEELKNADWA RFWVQVMRDL RNGVKLKKVQ ERQYNPLPIE 

       310        320        330        340        350        360 
YQLTPYEMLM DDIRCKRYTL RKVMVNGDIP PRLKKSAHEI ILDFIRSRPP LNPVSARKLK 

       370        380        390        400        410        420 
PTPPRPRSLH ERILEEIKAE RKLRPVSPEE IRRSRLAMRP LSMSYSFDLS DVTTPESTKN 

       430        440        450        460        470        480 
LVESSMVNGG LTSQTKENGL STSQQVPAQR KKLLRAPTLA ELDSSESEEE TLHKSTSSSS 

       490        500        510        520        530        540 
VSPSFPEEPV LEAVSTRKKP PKFLPISSTP QPERRQPPQR RHSIEKETPT NVRQFLPPSR 

       550        560        570        580        590        600 
QSSRSLEEFC YPVECLALTV EEVMHIRQVL VKAELEKYQQ YKDIYTALKK GKLCFCCRTR 

       610        620        630        640        650        660 
RFSFFTWSYT CQFCKRPVCS QCCKKMRLPS KPYSTLPIFS LGPSALQRGE SSMRSEKPST 

       670        680        690        700        710        720 
AHHRPLRSIA RFSSKSKSMD KSDEELQFPK ELMEDWSTME VCVDCKKFIS EIISSSRRSL 

       730        740        750 
VLANKRARLK RKTQSFYMSS PGPSEYCPSE RTISEI 

« Hide

Isoform 2 [UniParc].

Checksum: F76F168197958220
Show »

FASTA74283,957
Isoform 3 [UniParc].

Checksum: 89163C062A16AB3D
Show »

FASTA58367,057
Isoform 4 [UniParc].

Checksum: BCE16535DEA4326C
Show »

FASTA45852,747

References

« Hide 'large scale' references
[1]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"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 3).
Tissue: Thalamus.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Testis.
[5]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
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] OF 44-756 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-756 (ISOFORMS 1 AND 2).
Tissue: Embryonic stem cell.
[7]"The Spir actin organizers are involved in vesicle transport processes."
Kerkhoff E., Simpson J.C., Leberfinger C.B., Otto I.M., Doerks T., Bork P., Rapp U.R., Raabe T., Pepperkok R.
Curr. Biol. 11:1963-1968(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 123-756 (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Brain and Testis.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-465 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division."
Pfender S., Kuznetsov V., Pleiser S., Kerkhoff E., Schuh M.
Curr. Biol. 21:955-960(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2 formin SPIR interaction motif (FSI) complex."
Zeth K., Pechlivanis M., Samol A., Pleiser S., Vonrhein C., Kerkhoff E.
J. Biol. Chem. 286:30732-30739(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-236 IN COMPLEX WITH FMN2, INTERACTION WITH FMN2, MUTAGENESIS OF TYR-134 AND ASP-138.
[12]"Structure and function of the interacting domains of Spire and Fmn-family formins."
Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W., Quinlan M.E., Eck M.J.
Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-237 IN COMPLEX WITH FMN2, INTERACTION WITH FMN2, MUTAGENESIS OF ILE-131; ASP-138 AND GLU-146.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB032961 mRNA. Translation: BAA86449.2. Different initiation.
AK290180 mRNA. Translation: BAF82869.1.
AL833817 mRNA. Translation: CAD38680.1.
AP001028 Genomic DNA. No translation available.
AP001029 Genomic DNA. No translation available.
AP005482 Genomic DNA. No translation available.
BC115005 mRNA. Translation: AAI15006.1. Different initiation.
BC125206 mRNA. Translation: AAI25207.1. Different initiation.
BC125207 mRNA. Translation: AAI25208.1. Different initiation.
AJ277587 mRNA. Translation: CAB96370.1.
RefSeqNP_001122098.1. NM_001128626.1.
NP_001122099.1. NM_001128627.1.
NP_064533.3. NM_020148.2.
UniGeneHs.515283.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YLEX-ray1.80A31-236[»]
2YLFX-ray2.05A31-236[»]
3R7GX-ray2.20A20-237[»]
3RBWX-ray3.20A/B/C/D20-237[»]
ProteinModelPortalQ08AE8.
SMRQ08AE8. Positions 34-236, 557-628.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121237. 2 interactions.
IntActQ08AE8. 2 interactions.
MINTMINT-3975323.
STRING9606.ENSP00000387266.

PTM databases

PhosphoSiteQ08AE8.

Polymorphism databases

DMDM425906061.

Proteomic databases

PaxDbQ08AE8.
PRIDEQ08AE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000383356; ENSP00000372847; ENSG00000134278. [Q08AE8-4]
ENST00000409402; ENSP00000387266; ENSG00000134278. [Q08AE8-1]
ENST00000410092; ENSP00000387226; ENSG00000134278. [Q08AE8-2]
ENST00000440472; ENSP00000404752; ENSG00000134278. [Q08AE8-4]
GeneID56907.
KEGGhsa:56907.
UCSCuc002kre.3. human. [Q08AE8-1]
uc010wzy.2. human. [Q08AE8-2]

Organism-specific databases

CTD56907.
GeneCardsGC18M012446.
HGNCHGNC:30622. SPIRE1.
HPAHPA040737.
HPA040942.
MIM609216. gene.
neXtProtNX_Q08AE8.
PharmGKBPA134895885.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69783.
HOGENOMHOG000013039.
HOVERGENHBG058898.
InParanoidQ08AE8.
KOK02098.
OMASTGHHRP.
OrthoDBEOG77DJ5G.
TreeFamTF326239.

Gene expression databases

ArrayExpressQ08AE8.
BgeeQ08AE8.
CleanExHS_SPIRE1.
GenevestigatorQ08AE8.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
InterProIPR011019. KIND.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTSM00750. KIND. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS51377. KIND. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPIRE1. human.
GenomeRNAi56907.
NextBio35535270.
PROQ08AE8.
SOURCESearch...

Entry information

Entry nameSPIR1_HUMAN
AccessionPrimary (citable) accession number: Q08AE8
Secondary accession number(s): A8K2B5 expand/collapse secondary AC list , J3KQ50, Q1RMD4, Q8NDP1, Q9NQ71, Q9ULT4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 28, 2012
Last modified: April 16, 2014
This is version 70 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 18

Human chromosome 18: entries, gene names and cross-references to MIM