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Protein

MTSS1-like protein

Gene

MTSS1L

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

Functioni

Involved in plasma membrane dynamics. Potentiated PDGF-mediated formation of membrane ruffles and lamellipodia in fibroblasts, acting via RAC1 activation (PubMed:14752106). May function in actin bundling (PubMed:14752106).1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
MTSS1-like protein
Alternative name(s):
Actin-bundling with BAIAP2 homology protein 1
Short name:
ABBA-1
Gene namesi
Name:MTSS1L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25094. MTSS1L.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi115K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi116K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi123K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi127K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-130, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi130K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi137K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-138, D-139, D-145, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi138K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-139, D-145, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi139K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-145, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi145K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-148, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi148K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-149, D-152 and D-157. 1 Publication1
Mutagenesisi149K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-152 and D-157. 1 Publication1
Mutagenesisi152K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149 and D-157. 1 Publication1
Mutagenesisi157K → D: Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149 and D-152. 1 Publication1

Organism-specific databases

DisGeNETi92154.
OpenTargetsiENSG00000132613.
PharmGKBiPA164723215.

Polymorphism and mutation databases

BioMutaiMTSS1L.
DMDMi74727332.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003196101 – 747MTSS1-like proteinAdd BLAST747

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei260PhosphothreonineBy similarity1
Modified residuei264PhosphoserineBy similarity1
Modified residuei441PhosphoserineCombined sources1
Modified residuei579PhosphoserineCombined sources1
Modified residuei601PhosphoserineCombined sources1
Modified residuei612PhosphoserineCombined sources1
Modified residuei624PhosphoserineCombined sources1
Modified residuei634PhosphoserineCombined sources1
Modified residuei639PhosphoserineCombined sources1
Modified residuei643PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ765P7.
MaxQBiQ765P7.
PaxDbiQ765P7.
PeptideAtlasiQ765P7.
PRIDEiQ765P7.

PTM databases

iPTMnetiQ765P7.
PhosphoSitePlusiQ765P7.

Expressioni

Gene expression databases

BgeeiENSG00000132613.
ExpressionAtlasiQ765P7. baseline and differential.
GenevisibleiQ765P7. HS.

Organism-specific databases

HPAiHPA048531.

Interactioni

Subunit structurei

Interacts (via IMD domain) with RAC1; this interaction may be important to potentiate PDGF-induced RAC1 activation.1 Publication

Protein-protein interaction databases

BioGridi124914. 2 interactors.
IntActiQ765P7. 2 interactors.
STRINGi9606.ENSP00000341171.

Structurei

3D structure databases

ProteinModelPortaliQ765P7.
SMRiQ765P7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 252IMDPROSITE-ProRule annotationAdd BLAST252
Domaini719 – 736WH2Add BLAST18

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili135 – 159Sequence analysisAdd BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi252 – 383Ser-richAdd BLAST132

Sequence similaritiesi

Belongs to the MTSS1 family.Curated
Contains 1 IMD (IRSp53/MIM homology) domain.PROSITE-ProRule annotation
Contains 1 WH2 domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGVU. Eukaryota.
ENOG410XRT4. LUCA.
GeneTreeiENSGT00390000002637.
HOGENOMiHOG000113691.
HOVERGENiHBG052530.
InParanoidiQ765P7.
KOiK20128.
OMAiAEKECGA.
OrthoDBiEOG091G083M.
PhylomeDBiQ765P7.
TreeFamiTF320619.

Family and domain databases

InterProiIPR013606. I-BAR_dom.
IPR030127. MIM/ABBA.
[Graphical view]
PANTHERiPTHR15708. PTHR15708. 2 hits.
PfamiPF08397. IMD. 1 hit.
[Graphical view]
PROSITEiPS51338. IMD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q765P7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
METAEKECGA LGGLFQAIVN DMKSSYPIWE DFNSKATKLH SQLRTTVLAA
60 70 80 90 100
VAFLDAFQKV ADMATNTRGA TRDIGSALTR MCMRHRSIET KLRQFTNALL
110 120 130 140 150
ESLINPLQER IEDWKKAANQ LDKDHAKEYK RARHEIKKKS SDTLKLQKKA
160 170 180 190 200
RKELLGKGDL QPQLDSALQD VNDMYLLLEE TEKQAVRRAL IEERGRFCTF
210 220 230 240 250
ITFLQPVVNG ELTMLGEITH LQGIIDDLVV LTAEPHKLPP ASEQVIKDLK
260 270 280 290 300
GSDYSWSYQT PPSSPSSSSS RKSSMCSAPS SSSSAKGGGA PWPGGAQTYS
310 320 330 340 350
PSSTCRYRSL AQPATTTARL SSVSSHDSGF VSQDATYSKP PSPMPSDITS
360 370 380 390 400
QKSSSSASSE ASETCQSVSE CSSPTSDWSK VGSHEQPSGA TLQRRKDRVE
410 420 430 440 450
LLRDTEPGPA SGGTLGPSGE EAPRPRMSPA TIAAKHGEEV SPAASDLAMV
460 470 480 490 500
LTRGLSLEHQ KSSRDSLQYS SGYSTQTTTP SCSEDTIPSQ GSDYDCYSVN
510 520 530 540 550
GDADSEGPPE FDKSSTIPRN SNIAQNYRRL IQTKRPASTA GLPTAGLPTA
560 570 580 590 600
TGLPSGAPPG VATIRRTPST KPTVRRALSS AGPIPIRPPI VPVKTPTVPD
610 620 630 640 650
SPGYMGPTRA GSEECVFYTD ETASPLAPDL AKASPKRLSL PNTAWGSPSP
660 670 680 690 700
EAAGYPGAGA EDEQQQLAAN RHSLVEKLGE LVAGAHALGE GQFPFPTALS
710 720 730 740
ATPTEETPTP PPAATSDPPA EDMLVAIRRG VRLRRTVTND RSAPRIL
Length:747
Mass (Da):79,929
Last modified:July 5, 2004 - v1
Checksum:i9D0EEF31702E9736
GO
Isoform 2 (identifier: Q765P7-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:291
Mass (Da):32,799
Checksum:iCF46678FF8C4A83D
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_031513153 – 155Missing in isoform 2. 1 Publication3
Alternative sequenceiVSP_031514264 – 294SPSSS…APWPG → VPSEPFVSFLSVRFWKNSPL LPAPSTPSSPI in isoform 2. 1 PublicationAdd BLAST31
Alternative sequenceiVSP_031515295 – 747Missing in isoform 2. 1 PublicationAdd BLAST453

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB115770 mRNA. Translation: BAC98378.1.
AC020763 Genomic DNA. No translation available.
BC002770 mRNA. Translation: AAH02770.1.
CCDSiCCDS32476.1. [Q765P7-1]
RefSeqiNP_612392.1. NM_138383.2. [Q765P7-1]
UniGeneiHs.432387.

Genome annotation databases

EnsembliENST00000338779; ENSP00000341171; ENSG00000132613. [Q765P7-1]
GeneIDi92154.
KEGGihsa:92154.
UCSCiuc002ezj.4. human. [Q765P7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB115770 mRNA. Translation: BAC98378.1.
AC020763 Genomic DNA. No translation available.
BC002770 mRNA. Translation: AAH02770.1.
CCDSiCCDS32476.1. [Q765P7-1]
RefSeqiNP_612392.1. NM_138383.2. [Q765P7-1]
UniGeneiHs.432387.

3D structure databases

ProteinModelPortaliQ765P7.
SMRiQ765P7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124914. 2 interactors.
IntActiQ765P7. 2 interactors.
STRINGi9606.ENSP00000341171.

PTM databases

iPTMnetiQ765P7.
PhosphoSitePlusiQ765P7.

Polymorphism and mutation databases

BioMutaiMTSS1L.
DMDMi74727332.

Proteomic databases

EPDiQ765P7.
MaxQBiQ765P7.
PaxDbiQ765P7.
PeptideAtlasiQ765P7.
PRIDEiQ765P7.

Protocols and materials databases

DNASUi92154.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338779; ENSP00000341171; ENSG00000132613. [Q765P7-1]
GeneIDi92154.
KEGGihsa:92154.
UCSCiuc002ezj.4. human. [Q765P7-1]

Organism-specific databases

CTDi92154.
DisGeNETi92154.
GeneCardsiMTSS1L.
HGNCiHGNC:25094. MTSS1L.
HPAiHPA048531.
MIMi616951. gene.
neXtProtiNX_Q765P7.
OpenTargetsiENSG00000132613.
PharmGKBiPA164723215.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGVU. Eukaryota.
ENOG410XRT4. LUCA.
GeneTreeiENSGT00390000002637.
HOGENOMiHOG000113691.
HOVERGENiHBG052530.
InParanoidiQ765P7.
KOiK20128.
OMAiAEKECGA.
OrthoDBiEOG091G083M.
PhylomeDBiQ765P7.
TreeFamiTF320619.

Miscellaneous databases

ChiTaRSiMTSS1L. human.
GenomeRNAii92154.
PROiQ765P7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132613.
ExpressionAtlasiQ765P7. baseline and differential.
GenevisibleiQ765P7. HS.

Family and domain databases

InterProiIPR013606. I-BAR_dom.
IPR030127. MIM/ABBA.
[Graphical view]
PANTHERiPTHR15708. PTHR15708. 2 hits.
PfamiPF08397. IMD. 1 hit.
[Graphical view]
PROSITEiPS51338. IMD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTSSL_HUMAN
AccessioniPrimary (citable) accession number: Q765P7
Secondary accession number(s): A6NJI7, Q9BUA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 97 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.