Q9BTV5 (FSD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibronectin type III and SPRY domain-containing protein 1

Alternative name(s):
MID1-related protein 1
Microtubule-associated protein GLFND

Gene names

Name:	FSD1
Synonyms:	GLFND, MIR1
ORF Names:	VLP27

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in microtubule organization and stabilization. Ref.2 Ref.5
Subunit structure	Oligomerization is required for binding to microtubules.
Subcellular location	Cytoplasm › cytoskeleton › centrosome. 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. Ref.2 Ref.5
Tissue specificity	Highly expressed in brain tissues, including cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe, temporal lobe and putamen. Lower expression in spinal chord. Ref.1 Ref.5
Domain	B30.2 box contains a microtubule-binding site.
Sequence similarities	Contains 1 B30.2/SPRY domain. Contains 1 COS domain. Contains 1 fibronectin type-III domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 496	496	Fibronectin type III and SPRY domain-containing protein 1		PRO_0000316537
Regions
	Domain	105 – 162	58	COS
	Domain	165 – 267	103	Fibronectin type-III
	Domain	268 – 477	210	B30.2/SPRY
	Coiled coil	4 – 99	96	Potential
Amino acid modifications
	Modified residue	313	1	Phosphoserine Ref.6
	Modified residue	317	1	Phosphoserine Ref.6
	Modified residue	324	1	Phosphoserine Ref.6
	Modified residue	491	1	Phosphoserine By similarity
Natural variations
	Natural variant	232	1	L → V. Ref.1 Corresponds to variant rs35139245 [ dbSNP | Ensembl ].		VAR_038385
Experimental info
	Mutagenesis	313	1	S → A in mitosis, remained associated with microtubules; when associated with A-317; A-322 and A-324. Ref.5
	Mutagenesis	313	1	S → D: Reduced ability to associate with microtubules; when associated with D-317; E-322 and D-324. Ref.5
	Mutagenesis	317	1	S → A in mitosis, remained associated with microtubules; when associated with A-313; A-322 and A-324. Ref.5
	Mutagenesis	317	1	S → D: Reduced ability to associate with microtubules; when associated with D-313; E-322 and D-324. Ref.5
	Mutagenesis	322	1	T → A in mitosis, remained associated with microtubules; when associated with A-313; A-317 and A-324. Ref.5
	Mutagenesis	322	1	T → E: Reduced ability to associate with microtubules; when associated with D-313; D-317 and D-324. Ref.5
	Mutagenesis	324	1	S → A in mitosis, remained associated with microtubules; when associated with A-313; A-317 and A-322. Ref.5
	Mutagenesis	324	1	S → D: Reduced ability to associate with microtubules; when associated with D-313; D-317 and E-322. Ref.5
	Sequence conflict	295	1	G → R in BAB13885. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9BTV5 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 0FE7B18F14C80D46	FASTA	496	55,820
	10 20 30 40 50 60 MEEQREALRK IIKTLAVKNE EIQSFIYSLK QMLLNVEANS AKVQEDLEAE FQSLFSLLEE 70 80 90 100 110 120 LKEGMLMKIK QDRASRTYEL QNQLAACTRA LESSEELLET ANQTLQAMDS EDFPQAAKQI 130 140 150 160 170 180 KDGVTMAPAF RLSLKAKVSD NMSHLMVDFA QERQMLQALK FLPVPSAPVI DLAESLVADN 190 200 210 220 230 240 CVTLVWRMPD EDSKIDHYVL EYRRTNFEGP PRLKEDQPWM VIEGIRQTEY TLTGLKFDMK 250 260 270 280 290 300 YMNFRVKACN KAVAGEFSEP VTLETPAFMF RLDASTSHQN LRVDDLSVEW DAMGGKVQDI 310 320 330 340 350 360 KAREKDGKGR TASPINSPAR GTPSPKRMPS GRGGRDRFTA ESYTVLGDTL IDGGEHYWEV 370 380 390 400 410 420 RYEPDSKAFG VGVAYRSLGR FEQLGKTAAS WCLHVNNWLQ VSFTAKHANK VKVLDAPVPD 430 440 450 460 470 480 CLGVHCDFHQ GLLSFYNART KQVLHTFKTR FTQPLLPAFT VWCGSFQVTT GLQVPSAVRC 490 LQKRGSATSS SNTSLT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of human FSD1, a novel brain specific gene on chromosome 19 with paralogy to 9q31." Carim-Todd L., Escarceller M., Estivill X., Sumoy L. Biochim. Biophys. Acta 1518:200-203(2001) [PubMed: 11267680] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT VAL-232.
[2]	"Identification of a novel microtubule-associated protein that regulates microtubule organization and cytokinesis by using a GFP-screening strategy." Manabe R., Whitmore L., Weiss J.M., Horwitz A.R. Curr. Biol. 12:1946-1951(2002) [PubMed: 12445389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION. Tissue: Fibrosarcoma.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo and Testis.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"A novel centrosome-associated protein with affinity for microtubules." Stein P.A., Toret C.P., Salic A.N., Rolls M.M., Rapoport T.A. J. Cell Sci. 115:3389-3402(2002) [PubMed: 12154070] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-313; SER-317; THR-322 AND SER-324.
[6]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-317 AND SER-324, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00305827.
RefSeq	NP_077309.1. NM_024333.2.
UniGene	Hs.28144.
3D structure databases
HSSP	HSSP built from PDB template 1X5F based on UniProtKB Q92859.
ProteinModelPortal	Q9BTV5.
SMR	Q9BTV5. Positions 164-260.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BTV5. 2 interactions.
MINT	MINT-1368061.
STRING	Q9BTV5.
PTM databases
PhosphoSite	Q9BTV5.
Polymorphism databases
DMDM	74733152.
Proteomic databases
PRIDE	Q9BTV5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000221856; ENSP00000221856; ENSG00000105255.
GeneID	79187.
KEGG	hsa:79187.
UCSC	uc002lzy.1. human.
Organism-specific databases
CTD	79187.
GeneCards	GC19P004304.
H-InvDB	HIX0014661.
HGNC	HGNC:13745. FSD1.
HPA	HPA043141.
MIM	609828. gene.
neXtProt	NX_Q9BTV5.
PharmGKB	PA134882882.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14077.
GeneTree	ENSGT00560000076722.
HOGENOM	HBG446524.
HOVERGEN	HBG107931.
InParanoid	Q9BTV5.
OMA	AKHANKA.
OrthoDB	EOG4B5P50.
PhylomeDB	Q9BTV5.
Gene expression databases
ArrayExpress	Q9BTV5.
Bgee	Q9BTV5.
CleanEx	HS_FSD1.
Genevestigator	Q9BTV5.
Family and domain databases
InterPro	IPR001870. B30.2/SPRY. IPR003649. Bbox_C. IPR008985. ConA-like_lec_gl. IPR017903. COS_domain. IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR003877. SPRY_rcpt. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF00041. fn3. 1 hit. PF00622. SPRY. 1 hit. [Graphical view]
SMART	SM00502. BBC. 1 hit. SM00060. FN3. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit. SSF49265. FN_III-like. 1 hit.
PROSITE	PS50188. B302_SPRY. 1 hit. PS51262. COS. 1 hit. PS50853. FN3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	68182.
SOURCE	Search...

Entry information

Entry name

FSD1_HUMAN

Accession

Primary (citable) accession number: Q9BTV5
Secondary accession number(s): B2RDT0, Q9BXN0, Q9HAG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.