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Q08AE8

- SPIR1_HUMAN

UniProt

Q08AE8 - SPIR1_HUMAN

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Protein
Protein spire homolog 1
Gene
SPIRE1, KIAA1135, SPIR1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

GO - Biological processi

  1. Golgi vesicle transport Source: Ensembl
  2. actin cytoskeleton organization Source: UniProtKB
  3. cleavage furrow formation Source: UniProtKB
  4. establishment of meiotic spindle localization Source: UniProtKB
  5. formin-nucleated actin cable assembly Source: UniProtKB
  6. intracellular transport Source: UniProtKB
  7. polar body extrusion after meiotic divisions Source: UniProtKB
  8. protein transport Source: UniProtKB-KW
  9. vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein spire homolog 1
Short name:
Spir-1
Gene namesi
Name:SPIRE1
Synonyms:KIAA1135, SPIR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:30622. SPIRE1.

Subcellular locationi

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 Rab11.1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. cell cortex Source: UniProtKB
  3. cytoplasmic vesicle membrane Source: UniProtKB
  4. cytoskeleton Source: UniProtKB-SubCell
  5. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  6. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311I → K: Strongly reduces interaction with FMN2. 1 Publication
Mutagenesisi134 – 1341Y → K: Abolishes interaction with FMN2. 1 Publication
Mutagenesisi138 – 1381D → N: Abolishes interaction with FMN2. 2 Publications
Mutagenesisi146 – 1461E → A or K: Abolishes interaction with FMN2. 1 Publication

Organism-specific databases

PharmGKBiPA134895885.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 756755Protein spire homolog 1
PRO_0000309569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei464 – 4641Phosphoserine1 Publication
Modified residuei465 – 4651Phosphoserine1 Publication
Modified residuei467 – 4671Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ08AE8.
PaxDbiQ08AE8.
PRIDEiQ08AE8.

PTM databases

PhosphoSiteiQ08AE8.

Expressioni

Gene expression databases

ArrayExpressiQ08AE8.
BgeeiQ08AE8.
CleanExiHS_SPIRE1.
GenevestigatoriQ08AE8.

Organism-specific databases

HPAiHPA040737.
HPA040942.

Interactioni

Subunit structurei

Interacts with FMN2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
YWHAQP273481EBI-1055655,EBI-359854

Protein-protein interaction databases

BioGridi121237. 2 interactions.
DIPiDIP-42378N.
IntActiQ08AE8. 2 interactions.
MINTiMINT-3975323.
STRINGi9606.ENSP00000387266.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 414
Helixi42 – 498
Helixi55 – 7420
Helixi85 – 873
Beta strandi88 – 914
Beta strandi96 – 983
Beta strandi116 – 1205
Helixi122 – 13716
Turni138 – 1403
Beta strandi145 – 1473
Helixi151 – 16010
Helixi196 – 2049
Beta strandi207 – 2093
Helixi210 – 2123
Helixi213 – 23422

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YLEX-ray1.80A36-236[»]
2YLFX-ray2.05A36-236[»]
3R7GX-ray2.20A20-237[»]
3RBWX-ray3.20A/B/C/D20-237[»]
ProteinModelPortaliQ08AE8.
SMRiQ08AE8. Positions 34-236.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 231192KIND
Add
BLAST
Domaini305 – 32319WH2 1
Add
BLAST
Domaini369 – 38618WH2 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni131 – 1388Important for interaction with FMN2
Regioni556 – 57621Spir-box
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili229 – 25729 Reviewed prediction
Add
BLAST

Domaini

Binds to actin monomers via the WH2 domain By similarity.By similarity
The Spir-box targets binding to intracellular membrane structures.1 Publication

Sequence similaritiesi

Belongs to the spire family.
Contains 1 KIND domain.
Contains 2 WH2 domains.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG69783.
HOGENOMiHOG000013039.
HOVERGENiHBG058898.
InParanoidiQ08AE8.
KOiK02098.
OMAiTMELYTF.
OrthoDBiEOG77DJ5G.
PhylomeDBiQ08AE8.
TreeFamiTF326239.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR011019. KIND.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00750. KIND. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51377. KIND. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q08AE8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAQAAGPAGG GEPRTEAVGG EGPREPGAAG GAAGGSRDAL SLEEILRLYN    50
QPINEEQAWA VCYQCCGSLR AAARRRQPRH RVRSAAQIRV WRDGAVTLAP 100
AADDAGEPPP VAGKLGYSQC METEVIESLG IIIYKALDYG LKENEERELS 150
PPLEQLIDHM ANTVEADGSN DEGYEAAEEG LGDEDEKRKI SAIRSYRDVM 200
KLCAAHLPTE SDAPNHYQAV CRALFAETME LHTFLTKIKS AKENLKKIQE 250
MEKSDESSTD LEELKNADWA RFWVQVMRDL RNGVKLKKVQ ERQYNPLPIE 300
YQLTPYEMLM DDIRCKRYTL RKVMVNGDIP PRLKKSAHEI ILDFIRSRPP 350
LNPVSARKLK PTPPRPRSLH ERILEEIKAE RKLRPVSPEE IRRSRLAMRP 400
LSMSYSFDLS DVTTPESTKN LVESSMVNGG LTSQTKENGL STSQQVPAQR 450
KKLLRAPTLA ELDSSESEEE TLHKSTSSSS VSPSFPEEPV LEAVSTRKKP 500
PKFLPISSTP QPERRQPPQR RHSIEKETPT NVRQFLPPSR QSSRSLEEFC 550
YPVECLALTV EEVMHIRQVL VKAELEKYQQ YKDIYTALKK GKLCFCCRTR 600
RFSFFTWSYT CQFCKRPVCS QCCKKMRLPS KPYSTLPIFS LGPSALQRGE 650
SSMRSEKPST AHHRPLRSIA RFSSKSKSMD KSDEELQFPK ELMEDWSTME 700
VCVDCKKFIS EIISSSRRSL VLANKRARLK RKTQSFYMSS PGPSEYCPSE 750
RTISEI 756

Note: No experimental confirmation available.

Length:756
Mass (Da):85,544
Last modified:November 28, 2012 - v3
Checksum:i1379B39C8CA9DDB3
GO
Isoform 5 (identifier: Q08AE8-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: Missing.
     397-410: Missing.

Note: No experimental confirmation available. Derived from EST data.

Show »
Length:622
Mass (Da):71,568
Checksum:iD4DF3C072A295F96
GO
Isoform 22 Publications (identifier: Q08AE8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     397-410: Missing.

Show »
Length:742
Mass (Da):83,957
Checksum:iF76F168197958220
GO
Isoform 3 (identifier: Q08AE8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     397-410: Missing.

Show »
Length:583
Mass (Da):67,057
Checksum:i89163C062A16AB3D
GO
Isoform 4 (identifier: Q08AE8-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:458
Mass (Da):52,747
Checksum:iBCE16535DEA4326C
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti249 – 2491Q → P.
Corresponds to variant rs1785296 [ dbSNP | Ensembl ].
VAR_058695

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 159159Missing in isoform 3 and isoform 4.
VSP_037925Add
BLAST
Alternative sequencei1 – 120120Missing in isoform 5.
VSP_054464Add
BLAST
Alternative sequencei397 – 41014Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_052595Add
BLAST
Alternative sequencei616 – 756141RPVCS…TISEI → SDCLFNGTAHCQFYLG in isoform 4.
VSP_037926Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CH471113 Genomic DNA. Translation: EAX01546.1.
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.
CCDSiCCDS32790.2. [Q08AE8-2]
CCDS45829.1. [Q08AE8-1]
CCDS45830.1. [Q08AE8-5]
RefSeqiNP_001122098.1. NM_001128626.1. [Q08AE8-1]
NP_001122099.1. NM_001128627.1. [Q08AE8-5]
NP_064533.3. NM_020148.2. [Q08AE8-2]
UniGeneiHs.515283.

Genome annotation databases

EnsembliENST00000383356; ENSP00000372847; ENSG00000134278. [Q08AE8-4]
ENST00000409402; ENSP00000387266; ENSG00000134278. [Q08AE8-1]
ENST00000410092; ENSP00000387226; ENSG00000134278. [Q08AE8-2]
ENST00000440472; ENSP00000404752; ENSG00000134278. [Q08AE8-4]
ENST00000453447; ENSP00000407050; ENSG00000134278.
GeneIDi56907.
KEGGihsa:56907.
UCSCiuc002kre.3. human. [Q08AE8-1]
uc010wzw.2. human.
uc010wzy.2. human. [Q08AE8-2]

Polymorphism databases

DMDMi425906061.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CH471113 Genomic DNA. Translation: EAX01546.1 .
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 .
CCDSi CCDS32790.2. [Q08AE8-2 ]
CCDS45829.1. [Q08AE8-1 ]
CCDS45830.1. [Q08AE8-5 ]
RefSeqi NP_001122098.1. NM_001128626.1. [Q08AE8-1 ]
NP_001122099.1. NM_001128627.1. [Q08AE8-5 ]
NP_064533.3. NM_020148.2. [Q08AE8-2 ]
UniGenei Hs.515283.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YLE X-ray 1.80 A 36-236 [» ]
2YLF X-ray 2.05 A 36-236 [» ]
3R7G X-ray 2.20 A 20-237 [» ]
3RBW X-ray 3.20 A/B/C/D 20-237 [» ]
ProteinModelPortali Q08AE8.
SMRi Q08AE8. Positions 34-236.
ModBasei Search...

Protein-protein interaction databases

BioGridi 121237. 2 interactions.
DIPi DIP-42378N.
IntActi Q08AE8. 2 interactions.
MINTi MINT-3975323.
STRINGi 9606.ENSP00000387266.

PTM databases

PhosphoSitei Q08AE8.

Polymorphism databases

DMDMi 425906061.

Proteomic databases

MaxQBi Q08AE8.
PaxDbi Q08AE8.
PRIDEi Q08AE8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000383356 ; ENSP00000372847 ; ENSG00000134278 . [Q08AE8-4 ]
ENST00000409402 ; ENSP00000387266 ; ENSG00000134278 . [Q08AE8-1 ]
ENST00000410092 ; ENSP00000387226 ; ENSG00000134278 . [Q08AE8-2 ]
ENST00000440472 ; ENSP00000404752 ; ENSG00000134278 . [Q08AE8-4 ]
ENST00000453447 ; ENSP00000407050 ; ENSG00000134278 .
GeneIDi 56907.
KEGGi hsa:56907.
UCSCi uc002kre.3. human. [Q08AE8-1 ]
uc010wzw.2. human.
uc010wzy.2. human. [Q08AE8-2 ]

Organism-specific databases

CTDi 56907.
GeneCardsi GC18M012446.
HGNCi HGNC:30622. SPIRE1.
HPAi HPA040737.
HPA040942.
MIMi 609216. gene.
neXtProti NX_Q08AE8.
PharmGKBi PA134895885.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69783.
HOGENOMi HOG000013039.
HOVERGENi HBG058898.
InParanoidi Q08AE8.
KOi K02098.
OMAi TMELYTF.
OrthoDBi EOG77DJ5G.
PhylomeDBi Q08AE8.
TreeFami TF326239.

Miscellaneous databases

ChiTaRSi SPIRE1. human.
GenomeRNAii 56907.
NextBioi 35535270.
PROi Q08AE8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q08AE8.
Bgeei Q08AE8.
CleanExi HS_SPIRE1.
Genevestigatori Q08AE8.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
InterProi IPR011019. KIND.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
SMARTi SM00750. KIND. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS51377. KIND. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 123-756 (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Brain and Testis.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-465 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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.
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "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.
  13. "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.

Entry informationi

Entry nameiSPIR1_HUMAN
AccessioniPrimary (citable) accession number: Q08AE8
Secondary accession number(s): A8K2B5
, J3KQ50, J3KQR5, Q1RMD4, Q8NDP1, Q9NQ71, Q9ULT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 28, 2012
Last modified: September 3, 2014
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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