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Protein

Spindlin-1

Gene

Spin1

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

Functioni

Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway dowstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (By similarity). Overexpression induces metaphase arrest and chromosomal instability (PubMed:18543248). Localizes to active rDNA loci and promotes the expression of rRNA genes. May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption (PubMed:23894536).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei173 – 1731Histone H3K4me3 and H3R8me2aBy similarity
Binding sitei180 – 1801Histone H3K4me3 and H3R8me2aBy similarity
Binding sitei184 – 1841Histone H3K4me3 and H3R8me2aBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein

Keywords - Biological processi

Cell cycle, Meiosis, Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Spindlin-1
Alternative name(s):
30000 Mr metaphase complex
SSEC P
Spindlin1
Gene namesi
Name:Spin1
Synonyms:Spin
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:109242. Spin1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasmcytoskeletonspindle 1 Publication
  • Nucleusnucleolus By similarity

  • Note: Associates with the meiotic spindle.1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • nucleolus Source: UniProtKB
  • nucleus Source: MGI
  • spindle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Early postnatal lethality. Ovarian folliculogenesis and oocyte growth appear normal but fully grown oocytes show defects in resuming meiosis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Spindlin-1PRO_0000181368Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-acetyllysineCombined sources
Modified residuei109 – 1091Phosphoserine; by AURKABy similarity
Modified residuei124 – 1241Phosphoserine; by AURKABy similarity
Modified residuei199 – 1991PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated during oocyte meiotic maturation.1 Publication
Post-translationally modified during the first mitotic cell cycle.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ61142.
MaxQBiQ61142.
PaxDbiQ61142.
PeptideAtlasiQ61142.
PRIDEiQ61142.

2D gel databases

REPRODUCTION-2DPAGEQ61142.

PTM databases

iPTMnetiQ61142.
PhosphoSiteiQ61142.

Expressioni

Tissue specificityi

Oocyte, egg, and very early embryo; not in the 8-, and 16-cell stage of the embryo. Isoform 1: Present in testis. Isoform 1 is more highly expressed in adult testes compared with newborn testes (at protein level).1 Publication

Developmental stagei

Gametogenesis. Synthesized from maternal transcripts but not from the zygote genome.1 Publication

Gene expression databases

BgeeiQ61142.
CleanExiMM_SPIN1.
GenevisibleiQ61142. MM.

Interactioni

Subunit structurei

Homodimer; may form higher-order oligomers. Interacts with TCF7L2/TCF4; the interaction is direct (By similarity). Interacts with HABP4 and SERBP1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ61142. 1 interaction.
STRINGi10090.ENSMUSP00000093473.

Structurei

3D structure databases

ProteinModelPortaliQ61142.
SMRiQ61142. Positions 50-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 11664Tudor-like domain 1By similarityAdd
BLAST
Regioni93 – 986Histone H3K4me3 and H3R8me2a bindingBy similarity
Regioni132 – 19362Tudor-like domain 2By similarityAdd
BLAST
Regioni142 – 1421Histone H3K4me3 and H3R8me2a bindingBy similarity
Regioni213 – 26250Tudor-like domain 3By similarityAdd
BLAST
Regioni250 – 2523Histone H3K4me3 and H3R8me2a bindingBy similarity

Domaini

The 3 tudor-like domains (also named Spin/Ssty repeats) specifically recognize and bind methylated histones. H3K4me3 and H3R8me2a are recognized by tudor-like domains 2 and 1, respectively.By similarity

Sequence similaritiesi

Belongs to the SPIN/STSY family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IGUH. Eukaryota.
ENOG410XQI2. LUCA.
GeneTreeiENSGT00760000119261.
HOGENOMiHOG000293367.
HOVERGENiHBG000686.
InParanoidiQ61142.
OMAiKHRSNVG.
OrthoDBiEOG7CK37K.
PhylomeDBiQ61142.
TreeFamiTF332665.

Family and domain databases

InterProiIPR003671. SPIN/Ssty.
IPR029579. Spindlin-1/z.
[Graphical view]
PANTHERiPTHR10405. PTHR10405. 1 hit.
PTHR10405:SF15. PTHR10405:SF15. 1 hit.
PfamiPF02513. Spin-Ssty. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q61142-1) [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
MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRTSV GPSKPVSQPR
60 70 80 90 100
RNIVGCRIQH GWREGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL
110 120 130 140 150
ELNKDERVSA LEVLPDRVAT SRISDAHLAD TMIGKAVEHM FETEDGSKDE
160 170 180 190 200
WRGMVLARAP VMNTWFYITY EKDPVLYMYQ LLDDYKEGDL RIMPDSNDSP
210 220 230 240 250
PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP SVYFIKFDDD
260
FHIYVYDLVK TS
Length:262
Mass (Da):29,643
Last modified:April 18, 2006 - v2
Checksum:i33005229982E110E
GO
Isoform 2 (identifier: Q61142-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHK → MASASSPASCPR

Show »
Length:240
Mass (Da):27,137
Checksum:iD48F03847E8CF876
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434MKTPF…RTSHK → MASASSPASCPR in isoform 2. 2 PublicationsVSP_017942Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48972 mRNA. Translation: AAA91233.1.
AK088127 mRNA. Translation: BAC40162.1.
AK134259 mRNA. Translation: BAE22069.1.
AK136251 mRNA. Translation: BAE22897.1.
AK139899 mRNA. Translation: BAE24175.1.
AK162171 mRNA. Translation: BAE36769.1.
AK162195 mRNA. Translation: BAE36784.1.
AK162258 mRNA. Translation: BAE36820.1.
AK163263 mRNA. Translation: BAE37266.1.
AK163293 mRNA. Translation: BAE37280.1.
AK163382 mRNA. Translation: BAE37327.1.
AK166528 mRNA. Translation: BAE38832.1.
AK166580 mRNA. Translation: BAE38869.1.
AK166677 mRNA. Translation: BAE38937.1.
AK168544 mRNA. Translation: BAE40420.1.
BC016517 mRNA. Translation: AAH16517.1.
CCDSiCCDS26510.1. [Q61142-1]
RefSeqiNP_001269957.1. NM_001283028.1. [Q61142-1]
NP_001269958.1. NM_001283029.1. [Q61142-1]
NP_001269959.1. NM_001283030.1.
NP_035592.1. NM_011462.3. [Q61142-2]
NP_666155.1. NM_146043.4. [Q61142-1]
XP_006516956.1. XM_006516893.2. [Q61142-1]
XP_006516957.1. XM_006516894.2. [Q61142-1]
UniGeneiMm.188432.

Genome annotation databases

EnsembliENSMUST00000095797; ENSMUSP00000093473; ENSMUSG00000021395. [Q61142-1]
GeneIDi20729.
KEGGimmu:20729.
UCSCiuc007qly.2. mouse. [Q61142-1]
uc007qmb.3. mouse. [Q61142-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48972 mRNA. Translation: AAA91233.1.
AK088127 mRNA. Translation: BAC40162.1.
AK134259 mRNA. Translation: BAE22069.1.
AK136251 mRNA. Translation: BAE22897.1.
AK139899 mRNA. Translation: BAE24175.1.
AK162171 mRNA. Translation: BAE36769.1.
AK162195 mRNA. Translation: BAE36784.1.
AK162258 mRNA. Translation: BAE36820.1.
AK163263 mRNA. Translation: BAE37266.1.
AK163293 mRNA. Translation: BAE37280.1.
AK163382 mRNA. Translation: BAE37327.1.
AK166528 mRNA. Translation: BAE38832.1.
AK166580 mRNA. Translation: BAE38869.1.
AK166677 mRNA. Translation: BAE38937.1.
AK168544 mRNA. Translation: BAE40420.1.
BC016517 mRNA. Translation: AAH16517.1.
CCDSiCCDS26510.1. [Q61142-1]
RefSeqiNP_001269957.1. NM_001283028.1. [Q61142-1]
NP_001269958.1. NM_001283029.1. [Q61142-1]
NP_001269959.1. NM_001283030.1.
NP_035592.1. NM_011462.3. [Q61142-2]
NP_666155.1. NM_146043.4. [Q61142-1]
XP_006516956.1. XM_006516893.2. [Q61142-1]
XP_006516957.1. XM_006516894.2. [Q61142-1]
UniGeneiMm.188432.

3D structure databases

ProteinModelPortaliQ61142.
SMRiQ61142. Positions 50-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61142. 1 interaction.
STRINGi10090.ENSMUSP00000093473.

PTM databases

iPTMnetiQ61142.
PhosphoSiteiQ61142.

2D gel databases

REPRODUCTION-2DPAGEQ61142.

Proteomic databases

EPDiQ61142.
MaxQBiQ61142.
PaxDbiQ61142.
PeptideAtlasiQ61142.
PRIDEiQ61142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000095797; ENSMUSP00000093473; ENSMUSG00000021395. [Q61142-1]
GeneIDi20729.
KEGGimmu:20729.
UCSCiuc007qly.2. mouse. [Q61142-1]
uc007qmb.3. mouse. [Q61142-2]

Organism-specific databases

CTDi10927.
MGIiMGI:109242. Spin1.

Phylogenomic databases

eggNOGiENOG410IGUH. Eukaryota.
ENOG410XQI2. LUCA.
GeneTreeiENSGT00760000119261.
HOGENOMiHOG000293367.
HOVERGENiHBG000686.
InParanoidiQ61142.
OMAiKHRSNVG.
OrthoDBiEOG7CK37K.
PhylomeDBiQ61142.
TreeFamiTF332665.

Miscellaneous databases

ChiTaRSiSpin1. mouse.
PROiQ61142.
SOURCEiSearch...

Gene expression databases

BgeeiQ61142.
CleanExiMM_SPIN1.
GenevisibleiQ61142. MM.

Family and domain databases

InterProiIPR003671. SPIN/Ssty.
IPR029579. Spindlin-1/z.
[Graphical view]
PANTHERiPTHR10405. PTHR10405. 1 hit.
PTHR10405:SF15. PTHR10405:SF15. 1 hit.
PfamiPF02513. Spin-Ssty. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Spindlin, a major maternal transcript expressed in the mouse during the transition from oocyte to embryo."
    Oh B., Hwang S.Y., Solter D., Knowles B.B.
    Development 124:493-503(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Strain: C57BL/6 X DBA/2.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Embryonic heart, Embryonic limb and Thymus.
  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] (ISOFORM 1).
    Strain: NMRI.
    Tissue: Mammary tumor.
  4. "Characterization of Spindlin1 isoform2 in mouse testis."
    Zhang K.M., Wang Y.F., Huo R., Bi Y., Lin M., Sha J.H., Zhou Z.M.
    Asian J. Androl. 10:741-748(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY (ISOFORM 1).
  5. "Overexpression of spindlin1 induces metaphase arrest and chromosomal instability."
    Zhang P., Cong B., Yuan H., Chen L., Lv Y., Bai C., Nan X., Shi S., Yue W., Pei X.
    J. Cell. Physiol. 217:400-408(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. "A tudor domain protein SPINDLIN1 interacts with the mRNA-binding protein SERBP1 and is involved in mouse oocyte meiotic resumption."
    Chew T.G., Peaston A., Lim A.K., Lorthongpanich C., Knowles B.B., Solter D.
    PLoS ONE 8:E69764-E69764(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH HABP4 AND SERBP1.

Entry informationi

Entry nameiSPIN1_MOUSE
AccessioniPrimary (citable) accession number: Q61142
Secondary accession number(s): Q3TLC3, Q3UT05, Q91VG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 18, 2006
Last modified: July 6, 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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.