Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q765P7 (MTSSL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MTSS1-like protein
Alternative name(s):
Actin-bundling with BAIAP2 homology protein 1
Short name=ABBA-1
Gene names
Name:MTSS1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function in actin bundling. Ref.1

Sequence similarities

Belongs to the MTSS1 family.

Contains 1 IMD (IRSp53/MIM homology) domain.

Contains 1 WH2 domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfilopodium assembly

Inferred from electronic annotation. Source: InterPro

signal transduction

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q765P7-1)

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.
Isoform 2 (identifier: Q765P7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     153-155: Missing.
     264-294: SPSSSSSRKSSMCSAPSSSSSAKGGGAPWPG → VPSEPFVSFLSVRFWKNSPLLPAPSTPSSPI
     295-747: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 747747MTSS1-like protein
PRO_0000319610

Regions

Domain1 – 252252IMD
Domain719 – 73618WH2
Coiled coil135 – 15925 Potential
Compositional bias252 – 383132Ser-rich

Amino acid modifications

Modified residue4411Phosphoserine Ref.5 Ref.8
Modified residue5791Phosphoserine Ref.5
Modified residue6011Phosphoserine Ref.4
Modified residue6121Phosphoserine Ref.5
Modified residue6241Phosphoserine Ref.5
Modified residue6341Phosphoserine Ref.5
Modified residue6391Phosphoserine Ref.4 Ref.5
Modified residue6431Phosphothreonine Ref.4

Natural variations

Alternative sequence153 – 1553Missing in isoform 2.
VSP_031513
Alternative sequence264 – 29431SPSSS…APWPG → VPSEPFVSFLSVRFWKNSPL LPAPSTPSSPI in isoform 2.
VSP_031514
Alternative sequence295 – 747453Missing in isoform 2.
VSP_031515

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9D0EEF31702E9736

FASTA74779,929
        10         20         30         40         50         60 
METAEKECGA LGGLFQAIVN DMKSSYPIWE DFNSKATKLH SQLRTTVLAA VAFLDAFQKV 

        70         80         90        100        110        120 
ADMATNTRGA TRDIGSALTR MCMRHRSIET KLRQFTNALL ESLINPLQER IEDWKKAANQ 

       130        140        150        160        170        180 
LDKDHAKEYK RARHEIKKKS SDTLKLQKKA RKELLGKGDL QPQLDSALQD VNDMYLLLEE 

       190        200        210        220        230        240 
TEKQAVRRAL IEERGRFCTF ITFLQPVVNG ELTMLGEITH LQGIIDDLVV LTAEPHKLPP 

       250        260        270        280        290        300 
ASEQVIKDLK GSDYSWSYQT PPSSPSSSSS RKSSMCSAPS SSSSAKGGGA PWPGGAQTYS 

       310        320        330        340        350        360 
PSSTCRYRSL AQPATTTARL SSVSSHDSGF VSQDATYSKP PSPMPSDITS QKSSSSASSE 

       370        380        390        400        410        420 
ASETCQSVSE CSSPTSDWSK VGSHEQPSGA TLQRRKDRVE LLRDTEPGPA SGGTLGPSGE 

       430        440        450        460        470        480 
EAPRPRMSPA TIAAKHGEEV SPAASDLAMV LTRGLSLEHQ KSSRDSLQYS SGYSTQTTTP 

       490        500        510        520        530        540 
SCSEDTIPSQ GSDYDCYSVN GDADSEGPPE FDKSSTIPRN SNIAQNYRRL IQTKRPASTA 

       550        560        570        580        590        600 
GLPTAGLPTA TGLPSGAPPG VATIRRTPST KPTVRRALSS AGPIPIRPPI VPVKTPTVPD 

       610        620        630        640        650        660 
SPGYMGPTRA GSEECVFYTD ETASPLAPDL AKASPKRLSL PNTAWGSPSP EAAGYPGAGA 

       670        680        690        700        710        720 
EDEQQQLAAN RHSLVEKLGE LVAGAHALGE GQFPFPTALS ATPTEETPTP PPAATSDPPA 

       730        740 
EDMLVAIRRG VRLRRTVTND RSAPRIL 

« Hide

Isoform 2 [UniParc].

Checksum: CF46678FF8C4A83D
Show »

FASTA29132,799

References

« Hide 'large scale' references
[1]"A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein."
Yamagishi A., Masuda M., Ohki T., Onishi H., Mochizuki N.
J. Biol. Chem. 279:14929-14936(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN.
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] OF 80-747 (ISOFORM 2).
Tissue: Skin.
[4]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-639 AND THR-643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-579; SER-612; SER-624; SER-634 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB115770 mRNA. Translation: BAC98378.1.
AC020763 Genomic DNA. No translation available.
BC002770 mRNA. Translation: AAH02770.1.
CCDSCCDS32476.1. [Q765P7-1]
RefSeqNP_612392.1. NM_138383.2. [Q765P7-1]
UniGeneHs.432387.

3D structure databases

ProteinModelPortalQ765P7.
SMRQ765P7. Positions 5-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ765P7. 1 interaction.
STRING9606.ENSP00000341171.

PTM databases

PhosphoSiteQ765P7.

Polymorphism databases

DMDM74727332.

Proteomic databases

MaxQBQ765P7.
PaxDbQ765P7.
PRIDEQ765P7.

Protocols and materials databases

DNASU92154.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338779; ENSP00000341171; ENSG00000132613. [Q765P7-1]
GeneID92154.
KEGGhsa:92154.
UCSCuc002ezj.3. human. [Q765P7-1]

Organism-specific databases

CTD92154.
GeneCardsGC16M070695.
HGNCHGNC:25094. MTSS1L.
HPAHPA048531.
neXtProtNX_Q765P7.
PharmGKBPA164723215.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72831.
HOGENOMHOG000113691.
HOVERGENHBG052530.
InParanoidQ765P7.
OMAAEKECGA.
OrthoDBEOG7T7GSJ.
PhylomeDBQ765P7.
TreeFamTF320619.

Gene expression databases

BgeeQ765P7.
GenevestigatorQ765P7.

Family and domain databases

InterProIPR013606. IRSp53/MIM_homology_IMD.
[Graphical view]
PfamPF08397. IMD. 1 hit.
[Graphical view]
PROSITEPS51338. IMD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMTSS1L. human.
GenomeRNAi92154.
NextBio77613.
PROQ765P7.

Entry information

Entry nameMTSSL_HUMAN
AccessionPrimary (citable) accession number: Q765P7
Secondary accession number(s): A6NJI7, Q9BUA8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM