Q08AE8 (SPIR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein spire homolog 1
Short name=Spir-1

Gene names

Name:	SPIRE1
Synonyms:	KIAA1135, SPIR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	756 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10 Ref.11
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › perinuclear 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, co-localised 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 process	Protein transport Transport
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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_component	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
YWHAQ	P27348	1	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 756

756

Protein spire homolog 1

PRO_0000309569

Regions

Domain

40 – 231

192

KIND

Domain

305 – 323

19

WH2 1

Domain

369 – 386

18

WH2 2

Region

131 – 138

8

Important for interaction with FMN2

Region

556 – 576

21

Spir-box

Coiled coil

229 – 257

29

Potential

Amino acid modifications

Modified residue

464

1

Phosphoserine Ref.8

Modified residue

465

1

Phosphoserine Ref.8

Modified residue

467

1

Phosphoserine Ref.8

Natural variations

Alternative sequence

1 – 159

159

Missing in isoform 3 and isoform 4.

VSP_037925

Alternative sequence

397 – 410

14

Missing in isoform 2, isoform 3 and isoform 4.

VSP_052595

Alternative sequence

616 – 756

141

RPVCS…TISEI → SDCLFNGTAHCQFYLG in isoform 4.

VSP_037926

Natural variant

249

1

Q → P.
Corresponds to variant rs1785296 [ dbSNP | Ensembl ].

VAR_058695

Experimental info

Mutagenesis

131

1

I → K: Strongly reduces interaction with FMN2. Ref.11

Mutagenesis

134

1

Y → K: Abolishes interaction with FMN2. Ref.10

Mutagenesis

138

1

D → N: Abolishes interaction with FMN2. Ref.10 Ref.11

Mutagenesis

146

1

E → A or K: Abolishes interaction with FMN2. Ref.11

Secondary structure

1

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756

Helix Strand Turn

Details...

Beta strand

38 – 41

4

Helix

42 – 49

8

Helix

55 – 74

20

Helix

85 – 87

3

Beta strand

88 – 91

4

Beta strand

96 – 98

3

Beta strand

116 – 120

5

Helix

122 – 137

16

Turn

138 – 140

3

Beta strand

145 – 147

3

Helix

151 – 160

10

Helix

196 – 204

9

Beta strand

207 – 209

3

Helix

210 – 212

3

Helix

213 – 234

22

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2012. Version 3. Checksum: 1379B39C8CA9DDB3	FASTA	756	85,544
	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
	Isoform 2 [UniParc]. Checksum: F76F168197958220	FASTA	742	83,957
	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 IRRSRLDVTT PESTKNLVES SMVNGGLTSQ 430 440 450 460 470 480 TKENGLSTSQ QVPAQRKKLL RAPTLAELDS SESEEETLHK STSSSSVSPS FPEEPVLEAV 490 500 510 520 530 540 STRKKPPKFL PISSTPQPER RQPPQRRHSI EKETPTNVRQ FLPPSRQSSR SLEEFCYPVE 550 560 570 580 590 600 CLALTVEEVM HIRQVLVKAE LEKYQQYKDI YTALKKGKLC FCCRTRRFSF FTWSYTCQFC 610 620 630 640 650 660 KRPVCSQCCK KMRLPSKPYS TLPIFSLGPS ALQRGESSMR SEKPSTAHHR PLRSIARFSS 670 680 690 700 710 720 KSKSMDKSDE ELQFPKELME DWSTMEVCVD CKKFISEIIS SSRRSLVLAN KRARLKRKTQ 730 740 SFYMSSPGPS EYCPSERTIS EI
	Isoform 3 [UniParc]. Checksum: 89163C062A16AB3D	FASTA	583	67,057
	10 20 30 40 50 60 MANTVEADGS NDEGYEAAEE GLGDEDEKRK ISAIRSYRDV MKLCAAHLPT ESDAPNHYQA 70 80 90 100 110 120 VCRALFAETM ELHTFLTKIK SAKENLKKIQ EMEKSDESST DLEELKNADW ARFWVQVMRD 130 140 150 160 170 180 LRNGVKLKKV QERQYNPLPI EYQLTPYEML MDDIRCKRYT LRKVMVNGDI PPRLKKSAHE 190 200 210 220 230 240 IILDFIRSRP PLNPVSARKL KPTPPRPRSL HERILEEIKA ERKLRPVSPE EIRRSRLDVT 250 260 270 280 290 300 TPESTKNLVE SSMVNGGLTS QTKENGLSTS QQVPAQRKKL LRAPTLAELD SSESEEETLH 310 320 330 340 350 360 KSTSSSSVSP SFPEEPVLEA VSTRKKPPKF LPISSTPQPE RRQPPQRRHS IEKETPTNVR 370 380 390 400 410 420 QFLPPSRQSS RSLEEFCYPV ECLALTVEEV MHIRQVLVKA ELEKYQQYKD IYTALKKGKL 430 440 450 460 470 480 CFCCRTRRFS FFTWSYTCQF CKRPVCSQCC KKMRLPSKPY STLPIFSLGP SALQRGESSM 490 500 510 520 530 540 RSEKPSTAHH RPLRSIARFS SKSKSMDKSD EELQFPKELM EDWSTMEVCV DCKKFISEII 550 560 570 580 SSSRRSLVLA NKRARLKRKT QSFYMSSPGP SEYCPSERTI SEI
	Isoform 4 [UniParc]. Checksum: BCE16535DEA4326C	FASTA	458	52,747
	10 20 30 40 50 60 MANTVEADGS NDEGYEAAEE GLGDEDEKRK ISAIRSYRDV MKLCAAHLPT ESDAPNHYQA 70 80 90 100 110 120 VCRALFAETM ELHTFLTKIK SAKENLKKIQ EMEKSDESST DLEELKNADW ARFWVQVMRD 130 140 150 160 170 180 LRNGVKLKKV QERQYNPLPI EYQLTPYEML MDDIRCKRYT LRKVMVNGDI PPRLKKSAHE 190 200 210 220 230 240 IILDFIRSRP PLNPVSARKL KPTPPRPRSL HERILEEIKA ERKLRPVSPE EIRRSRLDVT 250 260 270 280 290 300 TPESTKNLVE SSMVNGGLTS QTKENGLSTS QQVPAQRKKL LRAPTLAELD SSESEEETLH 310 320 330 340 350 360 KSTSSSSVSP SFPEEPVLEA VSTRKKPPKF LPISSTPQPE RRQPPQRRHS IEKETPTNVR 370 380 390 400 410 420 QFLPPSRQSS RSLEEFCYPV ECLALTVEEV MHIRQVLVKA ELEKYQQYKD IYTALKKGKL 430 440 450 CFCCRTRRFS FFTWSYTCQF CKSDCLFNGT AHCQFYLG

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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]	"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.
[11]	"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.

IPI

IPI00171145.
IPI00645268.
IPI00896365.
IPI00917940.

RefSeq

NP_001122098.1. NM_001128626.1.
NP_001122099.1. NM_001128627.1.
NP_064533.3. NM_020148.2.

UniGene

Hs.515283.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YLE	X-ray	1.80	A	31-236	[»]
2YLF	X-ray	2.05	A	31-236	[»]
3R7G	X-ray	2.20	A	20-237	[»]
3RBW	X-ray	3.20	A/B/C/D	20-237	[»]

ProteinModelPortal

Q08AE8.

SMR

Q08AE8. Positions 34-236.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q08AE8. 1 interaction.

MINT

MINT-3975323.

STRING

9606.ENSP00000387266.

PTM databases

PhosphoSite

Q08AE8.

Polymorphism databases

DMDM

215273889.

Proteomic databases

PaxDb

Q08AE8.

PRIDE

Q08AE8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000383356; ENSP00000372847; ENSG00000134278.
ENST00000409402; ENSP00000387266; ENSG00000134278.
ENST00000410092; ENSP00000387226; ENSG00000134278.
ENST00000440472; ENSP00000404752; ENSG00000134278.

GeneID

56907.

KEGG

hsa:56907.

UCSC

uc002kre.3. human.
uc010wzw.2. human.
uc010wzx.2. human.

Organism-specific databases

CTD

56907.

GeneCards

GC18M012446.

HGNC

HGNC:30622. SPIRE1.

HPA

HPA040737.
HPA040942.

MIM

609216. gene.

neXtProt

NX_Q08AE8.

PharmGKB

PA134895885.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG69783.

HOGENOM

HOG000013039.

HOVERGEN

HBG058898.

InParanoid

Q08AE8.

KO

K02098.

OMA

STGHHRP.

OrthoDB

EOG44J2HS.

Gene expression databases

ArrayExpress

Q08AE8.

Bgee

Q08AE8.

CleanEx

HS_SPIRE1.

Genevestigator

Q08AE8.

Family and domain databases

Gene3D

3.30.40.10. 2 hits.

InterPro

IPR011019. KIND.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

SMART

SM00750. KIND. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS51377. KIND. 1 hit.
PS51082. WH2. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SPIRE1. human.

GenomeRNAi

56907.

NextBio

35535270.

SOURCE

Search...

Entry information

Entry name

SPIR1_HUMAN

Accession

Primary (citable) accession number: Q08AE8
Secondary accession number(s): A8K2B5 , J3KQ50, Q1RMD4, Q8NDP1, Q9NQ71, Q9ULT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 28, 2012
Last modified:	May 1, 2013
This is version 62 of the entry and version 3 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.