Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q08AE8

- SPIR1_HUMAN

UniProt

Q08AE8 - SPIR1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein spire homolog 1

Gene

SPIRE1

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.2 Publications

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. cleavage furrow formation Source: UniProtKB
  3. establishment of meiotic spindle localization Source: UniProtKB
  4. formin-nucleated actin cable assembly Source: UniProtKB
  5. Golgi vesicle transport Source: Ensembl
  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:SPIRE1Imported
Synonyms:KIAA1135, SPIR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:30622. SPIRE1.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cytoplasmperinuclear region 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; 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.By similarity

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasmic vesicle membrane Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-KW
  4. Golgi apparatus Source: Ensembl
  5. plasma membrane Source: UniProtKB-KW
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 1PRO_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

BgeeiQ08AE8.
CleanExiHS_SPIRE1.
ExpressionAtlasiQ08AE8. baseline and differential.
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

1
756
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 414Combined sources
Helixi42 – 498Combined sources
Helixi55 – 7420Combined sources
Helixi85 – 873Combined sources
Beta strandi88 – 914Combined sources
Beta strandi96 – 983Combined sources
Beta strandi116 – 1205Combined sources
Helixi122 – 13716Combined sources
Turni138 – 1403Combined sources
Beta strandi145 – 1473Combined sources
Helixi151 – 16010Combined sources
Helixi196 – 2049Combined sources
Beta strandi207 – 2093Combined sources
Helixi210 – 2123Combined sources
Helixi213 – 23422Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili229 – 25729Sequence AnalysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the spire family.Curated
Contains 1 KIND domain.PROSITE-ProRule annotation
Contains 2 WH2 domains.Sequence Analysis

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG69783.
GeneTreeiENSGT00390000003058.
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

        10         20         30         40         50
MAQAAGPAGG GEPRTEAVGG EGPREPGAAG GAAGGSRDAL SLEEILRLYN
60 70 80 90 100
QPINEEQAWA VCYQCCGSLR AAARRRQPRH RVRSAAQIRV WRDGAVTLAP
110 120 130 140 150
AADDAGEPPP VAGKLGYSQC METEVIESLG IIIYKALDYG LKENEERELS
160 170 180 190 200
PPLEQLIDHM ANTVEADGSN DEGYEAAEEG LGDEDEKRKI SAIRSYRDVM
210 220 230 240 250
KLCAAHLPTE SDAPNHYQAV CRALFAETME LHTFLTKIKS AKENLKKIQE
260 270 280 290 300
MEKSDESSTD LEELKNADWA RFWVQVMRDL RNGVKLKKVQ ERQYNPLPIE
310 320 330 340 350
YQLTPYEMLM DDIRCKRYTL RKVMVNGDIP PRLKKSAHEI ILDFIRSRPP
360 370 380 390 400
LNPVSARKLK PTPPRPRSLH ERILEEIKAE RKLRPVSPEE IRRSRLAMRP
410 420 430 440 450
LSMSYSFDLS DVTTPESTKN LVESSMVNGG LTSQTKENGL STSQQVPAQR
460 470 480 490 500
KKLLRAPTLA ELDSSESEEE TLHKSTSSSS VSPSFPEEPV LEAVSTRKKP
510 520 530 540 550
PKFLPISSTP QPERRQPPQR RHSIEKETPT NVRQFLPPSR QSSRSLEEFC
560 570 580 590 600
YPVECLALTV EEVMHIRQVL VKAELEKYQQ YKDIYTALKK GKLCFCCRTR
610 620 630 640 650
RFSFFTWSYT CQFCKRPVCS QCCKKMRLPS KPYSTLPIFS LGPSALQRGE
660 670 680 690 700
SSMRSEKPST AHHRPLRSIA RFSSKSKSMD KSDEELQFPK ELMEDWSTME
710 720 730 740 750
VCVDCKKFIS EIISSSRRSL VLANKRARLK RKTQSFYMSS PGPSEYCPSE

RTISEI

Note: No experimental confirmation available.Curated

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. Curated
The sequence AAI25207.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI25208.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA86449.2 differs from that shown. Reason: Erroneous initiation. Curated

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. 2 PublicationsVSP_037925Add
BLAST
Alternative sequencei1 – 120120Missing in isoform 5. CuratedVSP_054464Add
BLAST
Alternative sequencei397 – 41014Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_052595Add
BLAST
Alternative sequencei616 – 756141RPVCS…TISEI → SDCLFNGTAHCQFYLG in isoform 4. 1 PublicationVSP_037926Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000409402; ENSP00000387266; ENSG00000134278. [Q08AE8-1]
ENST00000410092; ENSP00000387226; ENSG00000134278. [Q08AE8-2]
ENST00000440472; ENSP00000404752; ENSG00000134278. [Q08AE8-4]
ENST00000453447; ENSP00000407050; ENSG00000134278. [Q08AE8-5]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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 ENST00000409402 ; ENSP00000387266 ; ENSG00000134278 . [Q08AE8-1 ]
ENST00000410092 ; ENSP00000387226 ; ENSG00000134278 . [Q08AE8-2 ]
ENST00000440472 ; ENSP00000404752 ; ENSG00000134278 . [Q08AE8-4 ]
ENST00000453447 ; ENSP00000407050 ; ENSG00000134278 . [Q08AE8-5 ]
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.
GeneTreei ENSGT00390000003058.
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

Bgeei Q08AE8.
CleanExi HS_SPIRE1.
ExpressionAtlasi Q08AE8. baseline and differential.
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: BrainImported.
  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 cellImported.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 123-756 (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: BrainImported and TestisImported.
  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: November 26, 2014
This is version 77 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