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Protein

Sperm-associated antigen 5

Gene

Spag5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase. Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture. In complex with SKAP, promotes stable microtubule-kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle, but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes. Involved in centriole duplication. Required for CDK5RAP22, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2. In non-mitotic cells, upon stress induction, inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs), thereby preventing mTORC1 hyperactivation-induced apoptosis. May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Sperm-associated antigen 5
Alternative name(s):
Mastrin
Mitotic spindle-associated protein p126
Short name:
MAP126
Gene namesi
Name:Spag5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1927470. Spag5.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Cytoplasmcytoskeletonspindle pole By similarity
  • Chromosomecentromerekinetochore By similarity
  • Midbody By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite By similarity

  • Note: Colocalizes with PCM1 at centriolar satellites throughout the cell cycle (By similarity). In a punctate pattern in interphase cells. During mitosis, detected at spindle poles during prophase, throughout the spindle in metaphase and anaphase, and at midzone microtubules in anaphase and telophase. Efficient targeting to the mitotic spindle may depend upon phosphorylation by GSK3B. Detected on kinetochores of chromosomes that have congressed. The astrin (SPAG5)-kinastrin (SKAP) complex localizes to the microtubule plus ends (By similarity). In non-mitotic non-stressed cells, shows a microtubuli pattern. During oxidative stress, accumulates in stress granules (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11651165Sperm-associated antigen 5PRO_0000072094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei66 – 661PhosphoserineBy similarity
Modified residuei321 – 3211PhosphoserineBy similarity
Modified residuei342 – 3421PhosphoserineBy similarity
Modified residuei946 – 9461Phosphoserine; by GSK3-betaBy similarity

Post-translational modificationi

Phosphorylated by AURKA.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7TME2.
MaxQBiQ7TME2.
PaxDbiQ7TME2.
PRIDEiQ7TME2.

PTM databases

iPTMnetiQ7TME2.
PhosphoSiteiQ7TME2.

Expressioni

Tissue specificityi

Detected in testis, but not in the other tissues tested.1 Publication

Inductioni

Expression is cell cycle-regulated, with an increase from prophase to cytokinesis and return to basal levels at the next G1 phase.By similarity

Gene expression databases

BgeeiQ7TME2.
CleanExiMM_SPAG5.
GenevisibleiQ7TME2. MM.

Interactioni

Subunit structurei

Homodimer, with a globular head domain and a long stalk. Homooligomer; the globular head domains associate, resulting in aster-like structures. Binds to microtubules in the mitotic spindle. Interacts with DCLRE1B/Apollo. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2. Interacts with KNSTRN. Interacts with RPTOR; this interaction competes with RPTOR binding to MTOR, resulting in decreased mTORC1 formation. Interacts with G3BP1. The complex formed with G3BP1 AND RPTOR is increased by oxidative stress. Interacts with OSBPL8, PCM1 and CDK5RAP2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207577. 10 interactions.
IntActiQ7TME2. 11 interactions.
STRINGi10090.ENSMUSP00000045286.

Structurei

3D structure databases

ProteinModelPortaliQ7TME2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni453 – 821369Interaction with KNSTRNBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili509 – 856348Sequence analysisAdd
BLAST
Coiled coili937 – 1146210Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IIA9. Eukaryota.
ENOG410YG9P. LUCA.
GeneTreeiENSGT00400000022377.
HOGENOMiHOG000049113.
HOVERGENiHBG058119.
InParanoidiQ7TME2.
OMAiWMSPLAW.
OrthoDBiEOG790G04.
PhylomeDBiQ7TME2.
TreeFamiTF336280.

Family and domain databases

InterProiIPR028728. Astrin.
[Graphical view]
PANTHERiPTHR15347:SF1. PTHR15347:SF1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7TME2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRVKTLNLG LSPSPQKGKP AMSTPLRELK LQPEALADSG KGPSMISALT
60 70 80 90 100
PYLCRLELKE RCNNSSPVDF INTENNFLSE QFSHPSTHIE ACQRESDPTP
110 120 130 140 150
ESNSLFHTLE EAIETVDDFV VDPRDDSIVE SMVLLPFSLG QQQDLMLQAH
160 170 180 190 200
LDTTAERTKS SLNESLGLED LVGKEVAPCV EDSLTEIVAI RPEQPTFQDP
210 220 230 240 250
PLGPSDTEDA PVDLVPSENV LNFSLARLSP SAVLAQDFSV DHVDPGEETV
260 270 280 290 300
ENRVLQEMET SFPTFPEEAE LGDQAPAANA EAVSPLYLTS SLVEMGPREA
310 320 330 340 350
PGPTVEDASR IPGLESETWM SPLAWLEKGV NTSVMLQNLR QSLSFSSVLQ
360 370 380 390 400
DAAVGNTPLA TCSVGTSFTP PAPLEVGTKD STSETERLLL GCRPPDLATL
410 420 430 440 450
SRHDLEENLL NSLVLLEVLS HQLQAWKSQL TVPHREARDS STQTDSSPCG
460 470 480 490 500
VTKTPKHLQD SKEIRQALLQ ARNVMQSWGL VSGDLLSLLH LSLTHVQEGR
510 520 530 540 550
VTVSQESQRS KTLVSSCSRV LKKLKAKLQS LKTECEEARH SKEMALKGKA
560 570 580 590 600
AAEAVLEAFR AHASQRISQL EQGLTSMQEF RGLLQEAQTQ LIGLHTEQKE
610 620 630 640 650
LAQQTVSLSS ALQQDWTSVQ LNYGIWAALL SWSRELTKKL TAKSRQALQE
660 670 680 690 700
RDAAIEEKKQ VVKEVEQVSA HLEDCKGQIE QLKLENSRLT ADLSAQLQIL
710 720 730 740 750
TSTESQLKEV RSQHSRCVQD LAVKDELLCQ LTQSNKEQAT QWQKEEMELK
760 770 780 790 800
HIQAELLQQQ AVLAKEVQDL RETVEFIDEE SQVAHRELGQ IESQLKVTLE
810 820 830 840 850
LLRERSLQCE TLRDTVDSLR AELASTEAKH EKQALEKTHQ HSQELRLLAE
860 870 880 890 900
QLQSLTLFLQ AKLKENKAES EIILPSTGSA PAQEHPLSND SSISEQTPTA
910 920 930 940 950
AVDEVPEPAP VPLLGSVKSA FTRVASMASF QPTETPDLEK SLAEMSTVLQ
960 970 980 990 1000
ELKSLCSLLQ ESKEEATGVL QREICELHSR LQAQEEEHQE ALKAKEADME
1010 1020 1030 1040 1050
KLNQALCLLR KNEKELLEVI QKQNEKILGQ IDKSGQLINL REEVTQLTQS
1060 1070 1080 1090 1100
LRRAETETKV LQEALEGQLD PSCQLMATNW IQEKVFLSQE VSKLRVMFLE
1110 1120 1130 1140 1150
MKTEKEQLMD KYLSHRHILE ENLRRSDTEL KKLDDTIQHV YETLLSIPET
1160
MKSCKELQGL LEFLS
Length:1,165
Mass (Da):129,993
Last modified:October 1, 2003 - v1
Checksum:i0885C71A3AB7A96A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481A → S in AAO15441 (PubMed:12893248).Curated
Sequence conflicti98 – 981P → S in AAO15441 (PubMed:12893248).Curated
Sequence conflicti225 – 2251L → P in AAO15441 (PubMed:12893248).Curated
Sequence conflicti244 – 2441D → N in AAO15441 (PubMed:12893248).Curated
Sequence conflicti347 – 3471S → P in AAO15441 (PubMed:12893248).Curated
Sequence conflicti441 – 4411S → G in AAO15441 (PubMed:12893248).Curated
Sequence conflicti663 – 6653KEV → TGM in AAO15441 (PubMed:12893248).Curated
Sequence conflicti776 – 7761F → S in AAO15441 (PubMed:12893248).Curated
Sequence conflicti888 – 8892SN → PS in AAO15441 (PubMed:12893248).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF420307 mRNA. Translation: AAO15441.1.
AY226907 Genomic DNA. Translation: AAP46103.1.
AL591070 Genomic DNA. Translation: CAI24319.1.
BC052672 mRNA. Translation: AAH52672.1.
CCDSiCCDS25098.1.
RefSeqiNP_059103.1. NM_017407.2.
UniGeneiMm.24250.

Genome annotation databases

EnsembliENSMUST00000045026; ENSMUSP00000045286; ENSMUSG00000002055.
GeneIDi54141.
KEGGimmu:54141.
UCSCiuc007kiv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF420307 mRNA. Translation: AAO15441.1.
AY226907 Genomic DNA. Translation: AAP46103.1.
AL591070 Genomic DNA. Translation: CAI24319.1.
BC052672 mRNA. Translation: AAH52672.1.
CCDSiCCDS25098.1.
RefSeqiNP_059103.1. NM_017407.2.
UniGeneiMm.24250.

3D structure databases

ProteinModelPortaliQ7TME2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207577. 10 interactions.
IntActiQ7TME2. 11 interactions.
STRINGi10090.ENSMUSP00000045286.

PTM databases

iPTMnetiQ7TME2.
PhosphoSiteiQ7TME2.

Proteomic databases

EPDiQ7TME2.
MaxQBiQ7TME2.
PaxDbiQ7TME2.
PRIDEiQ7TME2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045026; ENSMUSP00000045286; ENSMUSG00000002055.
GeneIDi54141.
KEGGimmu:54141.
UCSCiuc007kiv.2. mouse.

Organism-specific databases

CTDi10615.
MGIiMGI:1927470. Spag5.

Phylogenomic databases

eggNOGiENOG410IIA9. Eukaryota.
ENOG410YG9P. LUCA.
GeneTreeiENSGT00400000022377.
HOGENOMiHOG000049113.
HOVERGENiHBG058119.
InParanoidiQ7TME2.
OMAiWMSPLAW.
OrthoDBiEOG790G04.
PhylomeDBiQ7TME2.
TreeFamiTF336280.

Miscellaneous databases

ChiTaRSiSpag5. mouse.
NextBioi310965.
PROiQ7TME2.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TME2.
CleanExiMM_SPAG5.
GenevisibleiQ7TME2. MM.

Family and domain databases

InterProiIPR028728. Astrin.
[Graphical view]
PANTHERiPTHR15347:SF1. PTHR15347:SF1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ and NIH Swiss.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: C3H/He.
    Tissue: Osteoblast.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiSPAG5_MOUSE
AccessioniPrimary (citable) accession number: Q7TME2
Secondary accession number(s): B1AQC8, Q8CH61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: April 13, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.