Skip Header

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

Sperm-associated antigen 5

Gene

SPAG5

Organism
Homo sapiens (Human)
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 (PubMed:11724960, PubMed:12356910). Required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:17664331). 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 (PubMed:18361916, PubMed:21402792). Involved in centriole duplication. Required for CDK5RAP2, CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2 (PubMed:26297806). 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 (PubMed:23953116). May enhance GSK3B-mediated phosphorylation of other substrates, such as MAPT/TAU (PubMed:18055457).1 Publication7 Publications

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB
  • establishment of spindle orientation Source: GO_Central
  • mitotic sister chromatid segregation Source: UniProtKB
  • protein localization to centrosome Source: UniProtKB
  • regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  • spindle organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Sperm-associated antigen 5
Alternative name(s):
Astrin
Deepest
Mitotic spindle-associated protein p126
Short name:
MAP126
Gene namesi
Name:SPAG5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:13452. SPAG5.

Subcellular locationi

GO - Cellular componenti

  • centriolar satellite Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • kinetochore Source: UniProtKB
  • microtubule plus-end Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • mitotic spindle Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • spindle microtubule Source: GO_Central
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi111 – 1111T → A: Decreased phosphorylation by GSK3-beta. Partial loss of spindle association; when associated with A-937, A974 and A-978. 1 Publication
Mutagenesisi937 – 9371T → A: Decreased phosphorylation by GSK3-beta. Partial loss of spindle association; when associated with A-111, A974 and A-978. 1 Publication
Mutagenesisi974 – 9741S → A: Decreased phosphorylation by GSK3-beta; when associated with A-978. Partial loss of spindle association; when associated with A-111, A937 and A-978. 1 Publication
Mutagenesisi978 – 9781T → A: Decreased phosphorylation by GSK3-beta; when associated with A-97A. Partial loss of spindle association; when associated with A-111, A-937 and A-974. 1 Publication

Organism-specific databases

PharmGKBiPA134868542.

Polymorphism and mutation databases

BioMutaiSPAG5.
DMDMi47117278.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11931193Sperm-associated antigen 5PRO_0000072093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei66 – 661PhosphoserineCombined sources
Modified residuei111 – 1111Phosphothreonine; by GSK3-beta1 Publication
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei334 – 3341PhosphoserineCombined sources
Modified residuei336 – 3361PhosphothreonineCombined sources
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei362 – 3621PhosphoserineCombined sources
Modified residuei937 – 9371Phosphothreonine; by GSK3-beta1 Publication
Modified residuei974 – 9741Phosphoserine; by GSK3-beta1 Publication
Modified residuei978 – 9781Phosphothreonine; by GSK3-beta1 Publication

Post-translational modificationi

Phosphorylated by AURKA.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96R06.
MaxQBiQ96R06.
PaxDbiQ96R06.
PRIDEiQ96R06.

PTM databases

iPTMnetiQ96R06.
PhosphoSiteiQ96R06.

Expressioni

Tissue specificityi

Highly expressed in testis. Detected at low levels in placenta, liver, pancreas, thymus and colon.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.1 Publication

Gene expression databases

BgeeiQ96R06.
CleanExiHS_SPAG5.
ExpressionAtlasiQ96R06. baseline and differential.
GenevisibleiQ96R06. HS.

Organism-specific databases

HPAiHPA022008.
HPA022479.

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 (PubMed:24424245, PubMed:26297806).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMOTL2Q9Y2J4-43EBI-413317,EBI-10187270
BARD1A0AVN23EBI-413317,EBI-9977322
C1orf109Q9NX043EBI-413317,EBI-8643161
CCHCR1Q8TD31-33EBI-413317,EBI-10175300
CDC20BQ86Y333EBI-413317,EBI-10260504
CHCHD3Q9NX633EBI-413317,EBI-743375
CLASP1Q7Z4603EBI-413317,EBI-913476
DCXO436023EBI-413317,EBI-8646694
EIF4E2O605733EBI-413317,EBI-398610
FBXO28Q9NVF73EBI-413317,EBI-740282
GOLGA8DPQ0D2H93EBI-413317,EBI-10181276
GOLGA8GQ08AF83EBI-413317,EBI-10181260
HAUS1Q96CS23EBI-413317,EBI-2514791
KANSL1I3L4J33EBI-413317,EBI-10178305
LGALS14Q8TCE93EBI-413317,EBI-10274069
LINGO1Q96FE53EBI-413317,EBI-719955
ORC6Q9Y5N63EBI-413317,EBI-374840
POLR2LP628753EBI-413317,EBI-359527
RBM41Q96IZ53EBI-413317,EBI-740773
RPTORQ8N1229EBI-413317,EBI-1567928
SH2D4AQ9H7883EBI-413317,EBI-747035
SMARCE1Q969G33EBI-413317,EBI-455078
SNAP47Q5SQN13EBI-413317,EBI-10244848
TSHZ3A1L0U73EBI-413317,EBI-10171826
TTC23Q5W5X93EBI-413317,EBI-6447954
ZC2HC1CQ53FD03EBI-413317,EBI-740767
ZFC3H1G3V1X13EBI-413317,EBI-6448783
ZMAT2Q96NC03EBI-413317,EBI-2682299

Protein-protein interaction databases

BioGridi115861. 81 interactions.
DIPiDIP-30998N.
IntActiQ96R06. 62 interactions.
MINTiMINT-1350705.
STRINGi9606.ENSP00000323300.

Structurei

3D structure databases

ProteinModelPortaliQ96R06.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni482 – 850369Interaction with KNSTRNAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili545 – 60864Sequence analysisAdd
BLAST
Coiled coili759 – 868110Sequence analysisAdd
BLAST
Coiled coili979 – 1174196Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi617 – 789173Gln-richAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IIA9. Eukaryota.
ENOG410YG9P. LUCA.
GeneTreeiENSGT00400000022377.
HOGENOMiHOG000049113.
HOVERGENiHBG058119.
InParanoidiQ96R06.
OMAiWMSPLAW.
OrthoDBiEOG790G04.
PhylomeDBiQ96R06.
TreeFamiTF336280.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q96R06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRVKKLSLS LSPSPQTGKP SMRTPLRELT LQPGALTNSG KRSPACSSLT
60 70 80 90 100
PSLCKLGLQE GSNNSSPVDF VNNKRTDLSS EHFSHSSKWL ETCQHESDEQ
110 120 130 140 150
PLDPIPQISS TPKTSEEAVD PLGNYMVKTI VLVPSPLGQQ QDMIFEARLD
160 170 180 190 200
TMAETNSISL NGPLRTDDLV REEVAPCMGD RFSEVAAVSE KPIFQESPSH
210 220 230 240 250
LLEESPPNPC SEQLHCSKES LSSRTEAVRE DLVPSESNAF LPSSVLWLSP
260 270 280 290 300
STALAADFRV NHVDPEEEIV EHGAMEEREM RFPTHPKESE TEDQALVSSV
310 320 330 340 350
EDILSTCLTP NLVEMESQEA PGPAVEDVGR ILGSDTESWM SPLAWLEKGV
360 370 380 390 400
NTSVMLENLR QSLSLPSMLR DAAIGTTPFS TCSVGTWFTP SAPQEKSTNT
410 420 430 440 450
SQTGLVGTKH STSETEQLLC GRPPDLTALS RHDLEDNLLS SLVILEVLSR
460 470 480 490 500
QLRDWKSQLA VPHPETQDSS TQTDTSHSGI TNKLQHLKES HEMGQALQQA
510 520 530 540 550
RNVMQSWVLI SKELISLLHL SLLHLEEDKT TVSQESRRAE TLVCCCFDLL
560 570 580 590 600
KKLRAKLQSL KAEREEARHR EEMALRGKDA AEIVLEAFCA HASQRISQLE
610 620 630 640 650
QDLASMREFR GLLKDAQTQL VGLHAKQEEL VQQTVSLTST LQQDWRSMQL
660 670 680 690 700
DYTTWTALLS RSRQLTEKLT VKSQQALQER DVAIEEKQEV SRVLEQVSAQ
710 720 730 740 750
LEECKGQTEQ LELENSRLAT DLRAQLQILA NMDSQLKELQ SQHTHCAQDL
760 770 780 790 800
AMKDELLCQL TQSNEEQAAQ WQKEEMALKH MQAELQQQQA VLAKEVRDLK
810 820 830 840 850
ETLEFADQEN QVAHLELGQV ECQLKTTLEV LRERSLQCEN LKDTVENLTA
860 870 880 890 900
KLASTIADNQ EQDLEKTRQY SQKLGLLTEQ LQSLTLFLQT KLKEKTEQET
910 920 930 940 950
LLLSTACPPT QEHPLPNDRT FLGSILTAVA DEEPESTPVP LLGSDKSAFT
960 970 980 990 1000
RVASMVSLQP AETPGMEESL AEMSIMTTEL QSLCSLLQES KEEAIRTLQR
1010 1020 1030 1040 1050
KICELQARLQ AQEEQHQEVQ KAKEADIEKL NQALCLRYKN EKELQEVIQQ
1060 1070 1080 1090 1100
QNEKILEQID KSGELISLRE EVTHLTRSLR RAETETKVLQ EALAGQLDSN
1110 1120 1130 1140 1150
CQPMATNWIQ EKVWLSQEVD KLRVMFLEMK NEKEKLMIKF QSHRNILEEN
1160 1170 1180 1190
LRRSDKELEK LDDIVQHIYK TLLSIPEVVR GCKELQGLLE FLS
Length:1,193
Mass (Da):134,422
Last modified:May 10, 2004 - v2
Checksum:iA846DB3FE624519C
GO

Sequence cautioni

The sequence AAD02813.1 differs from that shown. Reason: Frameshift at position 1093. Curated
The sequence AAL06396.2 differs from that shown. Reason: Frameshift at position 1135. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381N → T in AAK91712 (PubMed:11724960).Curated
Sequence conflicti38 – 381N → T in AAL06396 (PubMed:11549262).Curated
Sequence conflicti38 – 381N → T in AAD02813 (Ref. 3) Curated
Sequence conflicti445 – 4473LEV → VEF in AAK91712 (PubMed:11724960).Curated
Sequence conflicti445 – 4473LEV → VEF in AAL06396 (PubMed:11549262).Curated
Sequence conflicti445 – 4473LEV → VEF in AAD02813 (Ref. 3) Curated
Sequence conflicti533 – 5331S → N in AAK91712 (PubMed:11724960).Curated
Sequence conflicti533 – 5331S → N in AAL06396 (PubMed:11549262).Curated
Sequence conflicti533 – 5331S → N in AAD02813 (Ref. 3) Curated
Sequence conflicti716 – 7161S → I in AAK91712 (PubMed:11724960).Curated
Sequence conflicti716 – 7161S → I in AAL06396 (PubMed:11549262).Curated
Sequence conflicti716 – 7161S → I in AAD02813 (Ref. 3) Curated
Sequence conflicti771 – 7722WQ → CV in AAK91712 (PubMed:11724960).Curated
Sequence conflicti771 – 7722WQ → CV in AAL06396 (PubMed:11549262).Curated
Sequence conflicti771 – 7722WQ → CV in AAD02813 (Ref. 3) Curated
Sequence conflicti1051 – 10511Missing in AAL06396 (PubMed:11549262).Curated
Sequence conflicti1051 – 10511Missing in AAD02813 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF399910 mRNA. Translation: AAK91712.1.
AF345347 mRNA. Translation: AAL06396.2. Frameshift.
AF063308 mRNA. Translation: AAD02813.1. Frameshift.
BC000322 mRNA. Translation: AAH00322.1.
AL122116 mRNA. Translation: CAB59275.1.
AL137585 mRNA. Translation: CAB70827.1.
CCDSiCCDS32594.1.
PIRiJC7765.
T34542.
T46296.
RefSeqiNP_006452.3. NM_006461.3.
UniGeneiHs.514033.

Genome annotation databases

EnsembliENST00000321765; ENSP00000323300; ENSG00000076382.
GeneIDi10615.
KEGGihsa:10615.
UCSCiuc002hbq.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF399910 mRNA. Translation: AAK91712.1.
AF345347 mRNA. Translation: AAL06396.2. Frameshift.
AF063308 mRNA. Translation: AAD02813.1. Frameshift.
BC000322 mRNA. Translation: AAH00322.1.
AL122116 mRNA. Translation: CAB59275.1.
AL137585 mRNA. Translation: CAB70827.1.
CCDSiCCDS32594.1.
PIRiJC7765.
T34542.
T46296.
RefSeqiNP_006452.3. NM_006461.3.
UniGeneiHs.514033.

3D structure databases

ProteinModelPortaliQ96R06.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115861. 81 interactions.
DIPiDIP-30998N.
IntActiQ96R06. 62 interactions.
MINTiMINT-1350705.
STRINGi9606.ENSP00000323300.

PTM databases

iPTMnetiQ96R06.
PhosphoSiteiQ96R06.

Polymorphism and mutation databases

BioMutaiSPAG5.
DMDMi47117278.

Proteomic databases

EPDiQ96R06.
MaxQBiQ96R06.
PaxDbiQ96R06.
PRIDEiQ96R06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321765; ENSP00000323300; ENSG00000076382.
GeneIDi10615.
KEGGihsa:10615.
UCSCiuc002hbq.4. human.

Organism-specific databases

CTDi10615.
GeneCardsiSPAG5.
HGNCiHGNC:13452. SPAG5.
HPAiHPA022008.
HPA022479.
MIMi615562. gene.
neXtProtiNX_Q96R06.
PharmGKBiPA134868542.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIA9. Eukaryota.
ENOG410YG9P. LUCA.
GeneTreeiENSGT00400000022377.
HOGENOMiHOG000049113.
HOVERGENiHBG058119.
InParanoidiQ96R06.
OMAiWMSPLAW.
OrthoDBiEOG790G04.
PhylomeDBiQ96R06.
TreeFamiTF336280.

Miscellaneous databases

ChiTaRSiSPAG5. human.
GeneWikiiSperm_associated_antigen_5.
GenomeRNAii10615.
NextBioi40330.
PROiQ96R06.
SOURCEiSearch...

Gene expression databases

BgeeiQ96R06.
CleanExiHS_SPAG5.
ExpressionAtlasiQ96R06. baseline and differential.
GenevisibleiQ96R06. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of mitotic microtubule-associated proteins using mass spectrometry identifies astrin, a spindle-associated protein."
    Mack G.J., Compton D.A.
    Proc. Natl. Acad. Sci. U.S.A. 98:14434-14439(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  2. "Cloning and characterization of hMAP126, a new member of mitotic spindle-associated proteins."
    Chang M.-S., Huang C.-J., Chen M.-L., Chen S.-T., Fan C.-C., Chu J.-M., Lin W.-C., Yang Y.-C.
    Biochem. Biophys. Res. Commun. 287:116-121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  3. Schnabel J., Weber K., Hatzfeld M.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cervix carcinoma.
  4. "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].
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-1193.
    Tissue: Testis.
  6. "The mitotic-spindle-associated protein astrin is essential for progression through mitosis."
    Gruber J., Harborth J., Schnabel J., Weber K., Hatzfeld M.
    J. Cell Sci. 115:4053-4059(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT STRUCTURE.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Astrin is required for the maintenance of sister chromatid cohesion and centrosome integrity."
    Thein K.H., Kleylein-Sohn J., Nigg E.A., Gruneberg U.
    J. Cell Biol. 178:345-354(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. Cited for: FUNCTION, INTERACTION WITH TUBULINS, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION BY AURKA.
  11. "Glycogen synthase kinase 3beta interacts with and phosphorylates the spindle-associated protein astrin."
    Cheng T.S., Hsiao Y.L., Lin C.C., Yu C.T., Hsu C.M., Chang M.S., Lee C.I., Huang C.Y., Howng S.L., Hong Y.R.
    J. Biol. Chem. 283:2454-2464(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-111; THR-937; SER-974 AND THR-978, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-111; THR-937; SER-974 AND THR-978.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-135 AND SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "SNM1B/Apollo interacts with astrin and is required for the prophase cell cycle checkpoint."
    Liu L., Akhter S., Bae J.B., Mukhopadhyay S.S., Richie C.T., Liu X., Legerski R.
    Cell Cycle 8:628-638(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCLRE1B.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-66; SER-135; SER-334; THR-336; SER-341 AND SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and facilitates chromosome alignment."
    Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.
    J. Cell Biol. 192:959-968(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH KNSTRN; PLK1; DYNLL1 AND SGOL2, INTERACTION WITH KNSTRN.
  19. Cited for: FUNCTION, INTERACTION WITH G3BP1 AND RPTOR, SUBCELLULAR LOCATION.
  20. "OSBP-related protein 8 (ORP8) interacts with Homo sapiens sperm associated antigen 5 (SPAG5) and mediates oxysterol interference of HepG2 cell cycle."
    Zhong W., Zhou Y., Li J., Mysore R., Luo W., Li S., Chang M.S., Olkkonen V.M., Yan D.
    Exp. Cell Res. 322:227-235(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OSBPL8.
  21. "Centriolar satellites assemble centrosomal microcephaly proteins to recruit CDK2 and promote centriole duplication."
    Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L., Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N., Walsh C.A., Reiter J.F.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK5RAP2 AND PCM1.

Entry informationi

Entry nameiSPAG5_HUMAN
AccessioniPrimary (citable) accession number: Q96R06
Secondary accession number(s): O95213
, Q9BWE8, Q9NT17, Q9UFE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: May 11, 2016
This is version 123 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) 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.