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Entry version 148 (10 Apr 2019)
Sequence version 3 (18 Apr 2006)
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Protein

Spindlin-1

Gene

SPIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei173Histone H3K4me3 and H3R8me2a1
Binding sitei180Histone H3K4me3 and H3R8me2a1
Binding sitei184Histone H3K4me3 and H3R8me2a1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Spindlin-1
Alternative name(s):
Ovarian cancer-related protein
Spindlin1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SPIN1
Synonyms:OCR, SPIN
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000106723.16

Human Gene Nomenclature Database

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HGNCi
HGNC:11243 SPIN1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
609936 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9Y657

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
10927

Open Targets

More...
OpenTargetsi
ENSG00000106723

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162404504

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SPIN1

Domain mapping of disease mutations (DMDM)

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DMDMi
93141317

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001813671 – 262Spindlin-1Add BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated during oocyte meiotic maturation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9Y657

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9Y657

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9Y657

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9Y657

PeptideAtlas

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PeptideAtlasi
Q9Y657

PRoteomics IDEntifications database

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PRIDEi
Q9Y657

ProteomicsDB human proteome resource

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ProteomicsDBi
86603

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9Y657

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9Y657

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in ovarian cancer tissues.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000106723 Expressed in 229 organ(s), highest expression level in female gonad

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9Y657 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9Y657 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA000162
HPA068784

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
116130, 43 interactors

Database of interacting proteins

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DIPi
DIP-40062N

Protein interaction database and analysis system

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IntActi
Q9Y657, 10 interactors

Molecular INTeraction database

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MINTi
Q9Y657

STRING: functional protein association networks

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STRINGi
9606.ENSP00000365019

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
6I8BX-ray1.76B/E48-262[»]
6I8LX-ray1.58B48-262[»]
6I8YX-ray1.52A48-262[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9Y657

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9Y657

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9Y657

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SPIN/STSY family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IGUH Eukaryota
ENOG410XQI2 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182925

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000293367

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000686

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9Y657

Identification of Orthologs from Complete Genome Data

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OMAi
KHRSNVG

Database of Orthologous Groups

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OrthoDBi
1027563at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9Y657

TreeFam database of animal gene trees

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TreeFami
TF332665

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003671 SPIN/Ssty
IPR029565 Spindlin-1

The PANTHER Classification System

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PANTHERi
PTHR10405 PTHR10405, 1 hit
PTHR10405:SF15 PTHR10405:SF15, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02513 Spin-Ssty, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i49F86CBCC7A0AA01
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti49P → S in BAG52466 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_053690221A → P. Corresponds to variant dbSNP:rs34794905Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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.

The Consensus CDS (CCDS) project

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CCDSi
CCDS43843.1

NCBI Reference Sequences

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RefSeqi
NP_006708.2, NM_006717.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.146804

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000375859; ENSP00000365019; ENSG00000106723

Database of genes from NCBI RefSeq genomes

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GeneIDi
10927

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:10927

UCSC genome browser

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UCSCi
uc004apy.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
6I8BX-ray1.76B/E48-262[»]
6I8LX-ray1.58B48-262[»]
6I8YX-ray1.52A48-262[»]
ProteinModelPortaliQ9Y657
SMRiQ9Y657
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116130, 43 interactors
DIPiDIP-40062N
IntActiQ9Y657, 10 interactors
MINTiQ9Y657
STRINGi9606.ENSP00000365019

PTM databases

iPTMnetiQ9Y657
PhosphoSitePlusiQ9Y657

Polymorphism and mutation databases

BioMutaiSPIN1
DMDMi93141317

Proteomic databases

EPDiQ9Y657
jPOSTiQ9Y657
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

Comparative Toxicogenomics Database

More...
CTDi
10927
DisGeNETi10927
EuPathDBiHostDB:ENSG00000106723.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SPIN1
HGNCiHGNC:11243 SPIN1
HPAiHPA000162
HPA068784
MIMi609936 gene
neXtProtiNX_Q9Y657
OpenTargetsiENSG00000106723
PharmGKBiPA162404504

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IGUH Eukaryota
ENOG410XQI2 LUCA
GeneTreeiENSGT00950000182925
HOGENOMiHOG000293367
HOVERGENiHBG000686
InParanoidiQ9Y657
OMAiKHRSNVG
OrthoDBi1027563at2759
PhylomeDBiQ9Y657
TreeFamiTF332665

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SPIN1 human
EvolutionaryTraceiQ9Y657

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
SPIN1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
10927

Protein Ontology

More...
PROi
PR:Q9Y657

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000106723 Expressed in 229 organ(s), highest expression level in female gonad
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSPIN1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y657
Secondary accession number(s): A8K0X6
, B3KRQ4, Q7KZJ8, Q9GZT2, Q9H0N7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: April 18, 2006
Last modified: April 10, 2019
This is version 148 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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