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Protein

T-lymphoma invasion and metastasis-inducing protein 1

Gene

Tiam1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates RAC1, CDC42, and to a lesser extent RHOA. Required for normal cell adhesion and cell migration (By similarity). Affects invasiveness of T-lymphoma cells.By similarity

GO - Molecular functioni

  • ephrin receptor binding Source: MGI
  • guanyl-nucleotide exchange factor activity Source: MGI
  • kinase binding Source: MGI
  • phospholipid binding Source: MGI
  • Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • signal transducer activity, downstream of receptor Source: InterPro

GO - Biological processi

  • activation of GTPase activity Source: ParkinsonsUK-UCL
  • brain-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  • cell-matrix adhesion Source: UniProtKB
  • cell migration Source: UniProtKB
  • ephrin receptor signaling pathway Source: MGI
  • positive regulation of axonogenesis Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of neuron projection development Source: UniProtKB
  • positive regulation of protein binding Source: MGI
  • Rac protein signal transduction Source: UniProtKB
  • regulation of dopaminergic neuron differentiation Source: ParkinsonsUK-UCL
  • regulation of GTPase activity Source: UniProtKB
  • regulation of non-canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • regulation of Rho protein signal transduction Source: InterPro
  • small GTPase mediated signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
T-lymphoma invasion and metastasis-inducing protein 1
Short name:
TIAM-1
Gene namesi
Name:Tiam1
Synonyms:Tiam-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103306. Tiam1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell contact zone Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cytosol Source: MGI
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • kinocilium Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi459 – 460RR → AA: Reduces phosphatidylinositol phosphate binding. 1 Publication2
Mutagenesisi622R → A: Reduces PARD3 binding; when associated with A-645. 1
Mutagenesisi645R → A: Reduces PARD3 binding; when associated with A-622. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedSequence analysis
ChainiPRO_00000809772 – 1591T-lymphoma invasion and metastasis-inducing protein 1Add BLAST1590

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineSequence analysis1
Modified residuei231PhosphoserineCombined sources1
Modified residuei356PhosphoserineCombined sources1
Modified residuei358PhosphoserineCombined sources1
Modified residuei695PhosphoserineCombined sources1
Modified residuei829Phosphotyrosine; by NTRK21 Publication1
Modified residuei1323PhosphotyrosineCombined sources1
Modified residuei1519PhosphoserineCombined sources1

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ60610.
MaxQBiQ60610.
PaxDbiQ60610.
PRIDEiQ60610.

2D gel databases

SWISS-2DPAGEQ60610.

PTM databases

iPTMnetiQ60610.
PhosphoSitePlusiQ60610.

Miscellaneous databases

PMAP-CutDBQ60610.

Expressioni

Tissue specificityi

Highly expressed in brain and testis and at low or moderate levels in almost all other normal tissues. Found in virtually all analyzed tumor cell lines including B- and T-lymphomas, neuroblastomas, melanomas and carcinomas.

Gene expression databases

CleanExiMM_TIAM1.

Interactioni

Subunit structurei

Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1 (By similarity). Interacts with BAIAP2. Interacts (via PDZ domain) with CNTNAP4, SDC1 and SDC3 (via C-terminus) (By similarity). Interacts with CD44, PARD3 and MAPK8IP2. Interacts with EPHA8; regulates clathrin-mediated endocytosis of EPHA8. Interacts with NTRK2; mediates the activation of RAC1 by BDNF.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cd44P153798EBI-1030321,EBI-7565891

GO - Molecular functioni

  • ephrin receptor binding Source: MGI
  • kinase binding Source: MGI
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-37821N.
IntActiQ60610. 6 interactors.
STRINGi10090.ENSMUSP00000002588.

Structurei

Secondary structure

11591
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1037 – 1065Combined sources29
Helixi1067 – 1071Combined sources5
Beta strandi1073 – 1076Combined sources4
Helixi1078 – 1085Combined sources8
Helixi1088 – 1106Combined sources19
Helixi1112 – 1114Combined sources3
Helixi1118 – 1121Combined sources4
Helixi1122 – 1135Combined sources14
Helixi1138 – 1141Combined sources4
Helixi1142 – 1148Combined sources7
Turni1149 – 1151Combined sources3
Helixi1152 – 1156Combined sources5
Turni1157 – 1161Combined sources5
Helixi1163 – 1172Combined sources10
Helixi1178 – 1180Combined sources3
Helixi1182 – 1185Combined sources4
Helixi1188 – 1193Combined sources6
Helixi1196 – 1205Combined sources10
Helixi1212 – 1249Combined sources38
Helixi1264 – 1266Combined sources3
Beta strandi1267 – 1277Combined sources11
Helixi1280 – 1283Combined sources4
Beta strandi1290 – 1296Combined sources7
Beta strandi1299 – 1304Combined sources6
Turni1318 – 1321Combined sources4
Beta strandi1332 – 1336Combined sources5
Helixi1337 – 1339Combined sources3
Beta strandi1340 – 1343Combined sources4
Turni1348 – 1351Combined sources4
Beta strandi1355 – 1360Combined sources6
Helixi1365 – 1367Combined sources3
Beta strandi1371 – 1379Combined sources9
Helixi1380 – 1400Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FOEX-ray2.80A/C/E/G1033-1406[»]
3A8NX-ray4.50A429-702[»]
ProteinModelPortaliQ60610.
SMRiQ60610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60610.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini434 – 549PH 1PROSITE-ProRule annotationAdd BLAST116
Domaini765 – 832RBDPROSITE-ProRule annotationAdd BLAST68
Domaini845 – 908PDZPROSITE-ProRule annotationAdd BLAST64
Domaini1040 – 1234DHPROSITE-ProRule annotationAdd BLAST195
Domaini1261 – 1397PH 2PROSITE-ProRule annotationAdd BLAST137

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi595 – 598Poly-Lys4
Compositional biasi1445 – 1449Poly-Arg5

Domaini

The first PH domain mediates interaction with membranes enriched in phosphoinositides.1 Publication

Sequence similaritiesi

Belongs to the TIAM family.Curated
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation
Contains 1 RBD (Ras-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410ITS1. Eukaryota.
ENOG410XPCM. LUCA.
HOGENOMiHOG000154573.
HOVERGENiHBG059279.
InParanoidiQ60610.
PhylomeDBiQ60610.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
2.30.42.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR003116. RBD_dom.
IPR033360. TIAM1.
[Graphical view]
PANTHERiPTHR22826:SF88. PTHR22826:SF88. 2 hits.
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 2 hits.
PF02196. RBD. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
SM00455. RBD. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 2 hits.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50898. RBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNAESQNVD HEFYGEKHAS LGRKHTSRSL RLSHKTRRTR HASSGKAIHR
60 70 80 90 100
NSEVSTRSSS TPSIPQSLAE NGLEPFSQEG ALDDFGDPIW VDRVDMGLRP
110 120 130 140 150
VSYTDSSVTP SVDGSIVLTA ASVQSMPDSE ESRLYGDDAT YLAEGGRRQC
160 170 180 190 200
PYTSNGPTFM ETASFKKKRS KSADIWREDS LEFSLSDLSQ EHLTSNEEIL
210 220 230 240 250
GSAEEKDCEE ARGMETEASP RQLSTCQRAN SLGDLYAQKN SGVKANGGPR
260 270 280 290 300
NRFSSYCRNL VSDIPDLAKH KMPPAAAEET PPYSNYNTLP CRKSHCLSEG
310 320 330 340 350
ATNPQISLSK SMQGRRAKTT QDVNTGEGSE FADSGIEGAT TDTDLLSRRS
360 370 380 390 400
NATNSSYSPP TGRAFVGSDS GSSSTGDRAR QGVYENFRRE LEMSTTNSES
410 420 430 440 450
LEEAGSAHSD EQSSGTLSSP GQSDILLTAA QGTVRKAGAL AVKNFLVHKK
460 470 480 490 500
NKKVESATRR KWKHYWVSLK GCTLFFYETD GRSGIDHNSV PKHAVWVENS
510 520 530 540 550
IVQAVPEHPK KDFVFCLSNS LGDAFLFQTT SQTELENWIT AIHSACAAAV
560 570 580 590 600
ARHHHKEDTL RLLKSEIKKL EQKIDMDEKM KKMGEMQLSS VTDSKKKKTI
610 620 630 640 650
LDQIFVWEQN LEQFQMDLFR FRCYLASLQG GELPNPKRLL AFASRPTKVA
660 670 680 690 700
MGRLGIFSVS SFHALVAART GEIGVRRRTQ AMSRSASKRR SRFSSLWGLD
710 720 730 740 750
TTSKKKQGRP TINQVFGEGT DAVKRSLEGI FDDTVPDGKR EKEVVLPSVH
760 770 780 790 800
QHNPDCDIWV HEYFTPSWFC LPNNQPALTV VRPGDTARDT LELICKTHQL
810 820 830 840 850
DHSAHYLRLK FLMENRVQFY IPQPEEDIYE LLYKEIEICP KVTQNIHIEK
860 870 880 890 900
SDAAADNYGF LLSSVDEDGI RRLYVNSVKE TGLASKKGLK AGDEILEINN
910 920 930 940 950
RAAGTLNSSM LKDFLSQPSL GLLVRTYPEP EGGVELLENP PHRVDGPVDL
960 970 980 990 1000
GESPLAFLTS NPGHSLSSEQ GSSAETAPEE GEGPDLESSD ETDHSSKSTE
1010 1020 1030 1040 1050
QVAAFCRSLH EMSPSDSSPS PQDATSPQLA TTRQLSDADK LRKVICELLE
1060 1070 1080 1090 1100
TERTYVKDLN CLMERYLKPL QKETFLTQDE LDVLFGNLTE MVEFQVEFLK
1110 1120 1130 1140 1150
TLEDGVRLVP DLEKLEKVDQ FKKVLFSLGG SFLYYADRFK LYSAFCASHT
1160 1170 1180 1190 1200
KVPKVLVKAK TDTAFKAFLD AQNPRQQHSS TLESYLIKPI QRVLKYPLLL
1210 1220 1230 1240 1250
RELFALTDAE SEEHYHLDVA IKTMNKVASH INEMQKIHEE FGAVFDQLIA
1260 1270 1280 1290 1300
EQTGEKKEVA DLSMGDLLLH TSVIWLNPPA SLGKWKKEPE LAAFVFKTAV
1310 1320 1330 1340 1350
VLVYKDGSKQ KKKLVGSHRL SIYEEWDPFR FRHMIPTEAL QVRALPSADA
1360 1370 1380 1390 1400
EANAVCEIVH VKSESEGRPE RVFHLCCSSP ESRKDFLKSV HSILRDKHRR
1410 1420 1430 1440 1450
QLLKTESLPS AQQYVPFGGK RLCALKGARP AMSRAVSAPS KSLGRRRRRL
1460 1470 1480 1490 1500
ARNRFTIDSD AISASSPEKE PQQPAGGGDT DRWVEEQFDL AQYEEQDDIK
1510 1520 1530 1540 1550
ETDILSDDDE FCESLKGASV DRDLQEQLQA ASISQRARGR RTLDSHASRM
1560 1570 1580 1590
TQLKKQAALS GINGGLESAS EEVIWVRRED FAPSRKLNTE I
Length:1,591
Mass (Da):177,533
Last modified:November 1, 1996 - v1
Checksum:iECC2BAB189A6F019
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05245 mRNA. Translation: AAA18830.1.
CCDSiCCDS28314.1.
PIRiA54146.
UniGeneiMm.310902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05245 mRNA. Translation: AAA18830.1.
CCDSiCCDS28314.1.
PIRiA54146.
UniGeneiMm.310902.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FOEX-ray2.80A/C/E/G1033-1406[»]
3A8NX-ray4.50A429-702[»]
ProteinModelPortaliQ60610.
SMRiQ60610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37821N.
IntActiQ60610. 6 interactors.
STRINGi10090.ENSMUSP00000002588.

PTM databases

iPTMnetiQ60610.
PhosphoSitePlusiQ60610.

2D gel databases

SWISS-2DPAGEQ60610.

Proteomic databases

EPDiQ60610.
MaxQBiQ60610.
PaxDbiQ60610.
PRIDEiQ60610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:103306. Tiam1.

Phylogenomic databases

eggNOGiENOG410ITS1. Eukaryota.
ENOG410XPCM. LUCA.
HOGENOMiHOG000154573.
HOVERGENiHBG059279.
InParanoidiQ60610.
PhylomeDBiQ60610.

Miscellaneous databases

ChiTaRSiTiam1. mouse.
EvolutionaryTraceiQ60610.
PMAP-CutDBQ60610.
PROiQ60610.
SOURCEiSearch...

Gene expression databases

CleanExiMM_TIAM1.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
2.30.42.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR003116. RBD_dom.
IPR033360. TIAM1.
[Graphical view]
PANTHERiPTHR22826:SF88. PTHR22826:SF88. 2 hits.
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 2 hits.
PF02196. RBD. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
SM00455. RBD. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF50729. SSF50729. 2 hits.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50898. RBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTIAM1_MOUSE
AccessioniPrimary (citable) accession number: Q60610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.