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

Spindlin-1

Gene

SPIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (PubMed:24589551). Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes (PubMed:21960006). 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.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei173Histone H3K4me3 and H3R8me2a1
Binding sitei180Histone H3K4me3 and H3R8me2a1
Binding sitei184Histone H3K4me3 and H3R8me2a1

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, Developmental protein
Biological processCell cycle, Meiosis, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Spindlin-1
Alternative name(s):
Ovarian cancer-related protein
Spindlin1
Gene namesi
Name:SPIN1
Synonyms:OCR, SPIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000106723.16
HGNCiHGNC:11243 SPIN1
MIMi609936 gene
neXtProtiNX_Q9Y657

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi72W → A or R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication1
Mutagenesisi98Y → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication1
Mutagenesisi109S → A: Impaired phosphorylation. 1 Publication1
Mutagenesisi124S → A: Impaired phosphorylation. 1 Publication1
Mutagenesisi141F → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. 2 Publications1
Mutagenesisi142E → A: Impaired binding to histone H3K4me3 and H3R8me2a. 1 Publication1
Mutagenesisi170Y → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. 2 Publications1
Mutagenesisi177Y → A: Impaired binding to histone H3K4me3 and H3R8me2a. 1 Publication1
Mutagenesisi184D → A or R: Impaired binding to histone H3K4me3 and H3R8me2a. 2 Publications1
Mutagenesisi189D → A or R: Impaired binding to histone H3K4me3. 1 Publication1
Mutagenesisi251F → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication1

Organism-specific databases

DisGeNETi10927
OpenTargetsiENSG00000106723
PharmGKBiPA162404504

Polymorphism and mutation databases

BioMutaiSPIN1
DMDMi93141317

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001813671 – 262Spindlin-1Add BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei44N6-acetyllysine; alternateBy similarity1
Cross-linki44Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei109Phosphoserine; by AURKA1 Publication1
Modified residuei124Phosphoserine; by AURKACombined sources1 Publication1
Modified residuei199PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated during oocyte meiotic maturation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y657
MaxQBiQ9Y657
PaxDbiQ9Y657
PeptideAtlasiQ9Y657
PRIDEiQ9Y657
ProteomicsDBi86603

PTM databases

iPTMnetiQ9Y657
PhosphoSitePlusiQ9Y657

Expressioni

Tissue specificityi

Highly expressed in ovarian cancer tissues.1 Publication

Gene expression databases

BgeeiENSG00000106723 Expressed in 229 organ(s), highest expression level in female gonad
CleanExiHS_SPIN1
ExpressionAtlasiQ9Y657 baseline and differential
GenevisibleiQ9Y657 HS

Organism-specific databases

HPAiHPA000162
HPA068784

Interactioni

Subunit structurei

Homodimer; may form higher-order oligomers (PubMed:17082182). Interacts with TCF7L2/TCF4; the interaction is direct (PubMed:22258766, PubMed:24589551, PubMed:29061846). Interacts with HABP4 and SERBP1 (By similarity). Interacts with C11orf84/SPINDOC (PubMed:29061846).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPB1P047922EBI-727129,EBI-352682

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116130, 41 interactors
DIPiDIP-40062N
IntActiQ9Y657, 11 interactors
MINTiQ9Y657
STRINGi9606.ENSP00000365019

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9Y657
SMRiQ9Y657
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y657

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 116Tudor-like domain 1Add BLAST64
Regioni93 – 98Histone H3K4me3 and H3R8me2a binding6
Regioni132 – 193Tudor-like domain 2Add BLAST62
Regioni142Histone H3K4me3 and H3R8me2a binding1
Regioni213 – 262Tudor-like domain 3Add BLAST50
Regioni250 – 252Histone H3K4me3 and H3R8me2a binding3

Domaini

The 3 tudor-like domains (also named Spin/Ssty repeats) specifically recognize and bind methylated histones (PubMed:23077255, PubMed:24589551). H3K4me3 and H3R8me2a are recognized by tudor-like domains 2 and 1, respectively (PubMed:24589551).3 Publications

Sequence similaritiesi

Belongs to the SPIN/STSY family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IGUH Eukaryota
ENOG410XQI2 LUCA
GeneTreeiENSGT00760000119261
HOGENOMiHOG000293367
HOVERGENiHBG000686
InParanoidiQ9Y657
OMAiKHRSNVG
OrthoDBiEOG091G0EE3
PhylomeDBiQ9Y657
TreeFamiTF332665

Family and domain databases

InterProiView protein in InterPro
IPR003671 SPIN/Ssty
IPR029565 Spindlin-1
PANTHERiPTHR10405 PTHR10405, 1 hit
PTHR10405:SF15 PTHR10405:SF15, 1 hit
PfamiView protein in Pfam
PF02513 Spin-Ssty, 3 hits

Sequencei

Sequence statusi: Complete.

Q9Y657-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRSSV GPSKPVSQPR
60 70 80 90 100
RNIVGCRIQH GWKEGNGPVT 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):29,601
Last modified:April 18, 2006 - v3
Checksum:i49F86CBCC7A0AA01
GO

Sequence cautioni

The sequence AAD43035 differs from that shown. Reason: Frameshift at position 21.Curated
The sequence AAG38112 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAG48367 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB66653 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.Curated
The sequence CAG38515 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49P → S in BAG52466 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_053690221A → P. Corresponds to variant dbSNP:rs34794905Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106682 mRNA Translation: AAD43035.1 Frameshift.
AF087864 mRNA Translation: AAG48367.1 Different initiation.
AF317228 mRNA Translation: AAG38112.1 Different initiation.
AL136719 mRNA Translation: CAB66653.1 Sequence problems.
BT007314 mRNA Translation: AAP35978.1
AK092017 mRNA Translation: BAG52466.1
AK289691 mRNA Translation: BAF82380.1
AK290009 mRNA Translation: BAF82698.1
AK315854 mRNA Translation: BAF98745.1
AL353748 Genomic DNA No translation available.
CH471089 Genomic DNA Translation: EAW62753.1
BC013571 mRNA No translation available.
BC114515 mRNA Translation: AAI14516.1
BC114565 mRNA Translation: AAI14566.1
CR533484 mRNA Translation: CAG38515.1 Sequence problems.
CCDSiCCDS43843.1
RefSeqiNP_006708.2, NM_006717.2
UniGeneiHs.146804

Genome annotation databases

EnsembliENST00000375859; ENSP00000365019; ENSG00000106723
GeneIDi10927
KEGGihsa:10927
UCSCiuc004apy.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106682 mRNA Translation: AAD43035.1 Frameshift.
AF087864 mRNA Translation: AAG48367.1 Different initiation.
AF317228 mRNA Translation: AAG38112.1 Different initiation.
AL136719 mRNA Translation: CAB66653.1 Sequence problems.
BT007314 mRNA Translation: AAP35978.1
AK092017 mRNA Translation: BAG52466.1
AK289691 mRNA Translation: BAF82380.1
AK290009 mRNA Translation: BAF82698.1
AK315854 mRNA Translation: BAF98745.1
AL353748 Genomic DNA No translation available.
CH471089 Genomic DNA Translation: EAW62753.1
BC013571 mRNA No translation available.
BC114515 mRNA Translation: AAI14516.1
BC114565 mRNA Translation: AAI14566.1
CR533484 mRNA Translation: CAG38515.1 Sequence problems.
CCDSiCCDS43843.1
RefSeqiNP_006708.2, NM_006717.2
UniGeneiHs.146804

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NS2X-ray2.20A/B26-262[»]
4H75X-ray2.10A27-262[»]
4MZFX-ray2.10B50-262[»]
4MZGX-ray1.70B/D50-262[»]
4MZHX-ray2.20A50-262[»]
5JSGX-ray2.50A/B50-262[»]
5JSJX-ray2.35A/B50-262[»]
5Y5WX-ray3.30A/B/C/D51-262[»]
ProteinModelPortaliQ9Y657
SMRiQ9Y657
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116130, 41 interactors
DIPiDIP-40062N
IntActiQ9Y657, 11 interactors
MINTiQ9Y657
STRINGi9606.ENSP00000365019

PTM databases

iPTMnetiQ9Y657
PhosphoSitePlusiQ9Y657

Polymorphism and mutation databases

BioMutaiSPIN1
DMDMi93141317

Proteomic databases

EPDiQ9Y657
MaxQBiQ9Y657
PaxDbiQ9Y657
PeptideAtlasiQ9Y657
PRIDEiQ9Y657
ProteomicsDBi86603

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375859; ENSP00000365019; ENSG00000106723
GeneIDi10927
KEGGihsa:10927
UCSCiuc004apy.4 human

Organism-specific databases

CTDi10927
DisGeNETi10927
EuPathDBiHostDB:ENSG00000106723.16
GeneCardsiSPIN1
HGNCiHGNC:11243 SPIN1
HPAiHPA000162
HPA068784
MIMi609936 gene
neXtProtiNX_Q9Y657
OpenTargetsiENSG00000106723
PharmGKBiPA162404504
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGUH Eukaryota
ENOG410XQI2 LUCA
GeneTreeiENSGT00760000119261
HOGENOMiHOG000293367
HOVERGENiHBG000686
InParanoidiQ9Y657
OMAiKHRSNVG
OrthoDBiEOG091G0EE3
PhylomeDBiQ9Y657
TreeFamiTF332665

Miscellaneous databases

ChiTaRSiSPIN1 human
EvolutionaryTraceiQ9Y657
GeneWikiiSPIN1
GenomeRNAii10927
PROiPR:Q9Y657
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106723 Expressed in 229 organ(s), highest expression level in female gonad
CleanExiHS_SPIN1
ExpressionAtlasiQ9Y657 baseline and differential
GenevisibleiQ9Y657 HS

Family and domain databases

InterProiView protein in InterPro
IPR003671 SPIN/Ssty
IPR029565 Spindlin-1
PANTHERiPTHR10405 PTHR10405, 1 hit
PTHR10405:SF15 PTHR10405:SF15, 1 hit
PfamiView protein in Pfam
PF02513 Spin-Ssty, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiSPIN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y657
Secondary accession number(s): A8K0X6
, B3KRQ4, Q7KZJ8, Q9GZT2, Q9H0N7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: April 18, 2006
Last modified: September 12, 2018
This is version 143 of the entry and version 3 of the sequence. See 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 9
    Human chromosome 9: 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. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again