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Protein

Fibronectin type III and SPRY domain-containing protein 1

Gene

FSD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in microtubule organization and stabilization.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105255-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin type III and SPRY domain-containing protein 1
Alternative name(s):
MID1-related protein 1
Microtubule-associated protein GLFND
Gene namesi
Name:FSD1
Synonyms:GLFND, MIR1
ORF Names:VLP27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:13745. FSD1.

Subcellular locationi

  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
  • Nucleus
  • Cytoplasm
  • Cleavage furrow

  • Note: Cell-cycle-dependent association with the centrosome. Colocalizes with a subpopulation of microtubules. Does not associates with microtubules during mitosis but reassociates with microtubules during cytokinesis. Localizes to the central portions of a small subset of microtubules in interphase cells and a subpopulation of microtubules in the cleavage furrow, not present in the mitotic spindle.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi313S → A in mitosis, remained associated with microtubules; when associated with A-317; A-322 and A-324. 1 Publication1
Mutagenesisi313S → D: Reduced ability to associate with microtubules; when associated with D-317; E-322 and D-324. 1 Publication1
Mutagenesisi317S → A in mitosis, remained associated with microtubules; when associated with A-313; A-322 and A-324. 1 Publication1
Mutagenesisi317S → D: Reduced ability to associate with microtubules; when associated with D-313; E-322 and D-324. 1 Publication1
Mutagenesisi322T → A in mitosis, remained associated with microtubules; when associated with A-313; A-317 and A-324. 1 Publication1
Mutagenesisi322T → E: Reduced ability to associate with microtubules; when associated with D-313; D-317 and D-324. 1 Publication1
Mutagenesisi324S → A in mitosis, remained associated with microtubules; when associated with A-313; A-317 and A-322. 1 Publication1
Mutagenesisi324S → D: Reduced ability to associate with microtubules; when associated with D-313; D-317 and E-322. 1 Publication1

Organism-specific databases

DisGeNETi79187.
OpenTargetsiENSG00000105255.
PharmGKBiPA134882882.

Polymorphism and mutation databases

BioMutaiFSD1.
DMDMi74733152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003165371 – 496Fibronectin type III and SPRY domain-containing protein 1Add BLAST496

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei310Omega-N-methylarginineBy similarity1
Modified residuei320Omega-N-methylarginineCombined sources1

Keywords - PTMi

Methylation

Proteomic databases

EPDiQ9BTV5.
MaxQBiQ9BTV5.
PaxDbiQ9BTV5.
PeptideAtlasiQ9BTV5.
PRIDEiQ9BTV5.

PTM databases

iPTMnetiQ9BTV5.
PhosphoSitePlusiQ9BTV5.

Expressioni

Tissue specificityi

Highly expressed in brain tissues, including cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe, temporal lobe and putamen. Lower expression in spinal chord.2 Publications

Gene expression databases

BgeeiENSG00000105255.
CleanExiHS_FSD1.
ExpressionAtlasiQ9BTV5. baseline and differential.
GenevisibleiQ9BTV5. HS.

Organism-specific databases

HPAiHPA043141.

Interactioni

Subunit structurei

Oligomerization is required for binding to microtubules.

Protein-protein interaction databases

BioGridi122600. 52 interactors.
IntActiQ9BTV5. 4 interactors.
MINTiMINT-1368061.
STRINGi9606.ENSP00000221856.

Structurei

3D structure databases

ProteinModelPortaliQ9BTV5.
SMRiQ9BTV5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini105 – 162COSPROSITE-ProRule annotationAdd BLAST58
Domaini164 – 268Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST105
Domaini268 – 477B30.2/SPRYPROSITE-ProRule annotationAdd BLAST210

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili4 – 99Sequence analysisAdd BLAST96

Domaini

B30.2 box contains a microtubule-binding site.

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 COS domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410ITFY. Eukaryota.
ENOG410ZECU. LUCA.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000231656.
HOVERGENiHBG107931.
InParanoidiQ9BTV5.
OMAiAFMVWNG.
OrthoDBiEOG091G072W.
PhylomeDBiQ9BTV5.
TreeFamiTF333654.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003649. Bbox_C.
IPR013320. ConA-like_dom.
IPR017903. COS_domain.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00060. FN3. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS51262. COS. 1 hit.
PS50853. FN3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BTV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEQREALRK IIKTLAVKNE EIQSFIYSLK QMLLNVEANS AKVQEDLEAE
60 70 80 90 100
FQSLFSLLEE LKEGMLMKIK QDRASRTYEL QNQLAACTRA LESSEELLET
110 120 130 140 150
ANQTLQAMDS EDFPQAAKQI KDGVTMAPAF RLSLKAKVSD NMSHLMVDFA
160 170 180 190 200
QERQMLQALK FLPVPSAPVI DLAESLVADN CVTLVWRMPD EDSKIDHYVL
210 220 230 240 250
EYRRTNFEGP PRLKEDQPWM VIEGIRQTEY TLTGLKFDMK YMNFRVKACN
260 270 280 290 300
KAVAGEFSEP VTLETPAFMF RLDASTSHQN LRVDDLSVEW DAMGGKVQDI
310 320 330 340 350
KAREKDGKGR TASPINSPAR GTPSPKRMPS GRGGRDRFTA ESYTVLGDTL
360 370 380 390 400
IDGGEHYWEV RYEPDSKAFG VGVAYRSLGR FEQLGKTAAS WCLHVNNWLQ
410 420 430 440 450
VSFTAKHANK VKVLDAPVPD CLGVHCDFHQ GLLSFYNART KQVLHTFKTR
460 470 480 490
FTQPLLPAFT VWCGSFQVTT GLQVPSAVRC LQKRGSATSS SNTSLT
Length:496
Mass (Da):55,820
Last modified:June 1, 2001 - v1
Checksum:i0FE7B18F14C80D46
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti295G → R in BAB13885 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038385232L → V.1 PublicationCorresponds to variant rs35139245dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF316829 mRNA. Translation: AAK26747.1.
AY032617 mRNA. Translation: AAK51145.1.
AK021750 mRNA. Translation: BAB13885.1.
AK315661 mRNA. Translation: BAG38027.1.
BC003124 mRNA. Translation: AAH03124.1.
CCDSiCCDS12127.1.
RefSeqiNP_077309.1. NM_024333.2.
UniGeneiHs.28144.

Genome annotation databases

EnsembliENST00000221856; ENSP00000221856; ENSG00000105255.
GeneIDi79187.
KEGGihsa:79187.
UCSCiuc002lzy.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF316829 mRNA. Translation: AAK26747.1.
AY032617 mRNA. Translation: AAK51145.1.
AK021750 mRNA. Translation: BAB13885.1.
AK315661 mRNA. Translation: BAG38027.1.
BC003124 mRNA. Translation: AAH03124.1.
CCDSiCCDS12127.1.
RefSeqiNP_077309.1. NM_024333.2.
UniGeneiHs.28144.

3D structure databases

ProteinModelPortaliQ9BTV5.
SMRiQ9BTV5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122600. 52 interactors.
IntActiQ9BTV5. 4 interactors.
MINTiMINT-1368061.
STRINGi9606.ENSP00000221856.

PTM databases

iPTMnetiQ9BTV5.
PhosphoSitePlusiQ9BTV5.

Polymorphism and mutation databases

BioMutaiFSD1.
DMDMi74733152.

Proteomic databases

EPDiQ9BTV5.
MaxQBiQ9BTV5.
PaxDbiQ9BTV5.
PeptideAtlasiQ9BTV5.
PRIDEiQ9BTV5.

Protocols and materials databases

DNASUi79187.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221856; ENSP00000221856; ENSG00000105255.
GeneIDi79187.
KEGGihsa:79187.
UCSCiuc002lzy.3. human.

Organism-specific databases

CTDi79187.
DisGeNETi79187.
GeneCardsiFSD1.
HGNCiHGNC:13745. FSD1.
HPAiHPA043141.
MIMi609828. gene.
neXtProtiNX_Q9BTV5.
OpenTargetsiENSG00000105255.
PharmGKBiPA134882882.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITFY. Eukaryota.
ENOG410ZECU. LUCA.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000231656.
HOVERGENiHBG107931.
InParanoidiQ9BTV5.
OMAiAFMVWNG.
OrthoDBiEOG091G072W.
PhylomeDBiQ9BTV5.
TreeFamiTF333654.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105255-MONOMER.

Miscellaneous databases

GenomeRNAii79187.
PROiQ9BTV5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105255.
CleanExiHS_FSD1.
ExpressionAtlasiQ9BTV5. baseline and differential.
GenevisibleiQ9BTV5. HS.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003649. Bbox_C.
IPR013320. ConA-like_dom.
IPR017903. COS_domain.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00060. FN3. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS51262. COS. 1 hit.
PS50853. FN3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFSD1_HUMAN
AccessioniPrimary (citable) accession number: Q9BTV5
Secondary accession number(s): B2RDT0, Q9BXN0, Q9HAG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 136 of the entry and version 1 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 19
    Human chromosome 19: 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. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.