[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; TISSUE=Brain; DOI=10.1016/0092-8674(94)90216-X; PubMed=7999144 [NCBI, ExPASy, EBI, Israel, Japan] Habets G.G.M., Scholtes E.H.M., Zuydgeest D., van der Kammen R.A., Stam J.C., Berns A., Collard J.G.; "Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins."; Cell 77:537-549(1994).
[2]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1074/mcp.T500041-MCP200; PubMed=16452087 [NCBI, ExPASy, EBI, Israel, Japan] Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."; Mol. Cell. Proteomics 5:914-922(2006).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1323, AND MASS SPECTROMETRY. TISSUE=Mast cell; PubMed=17947660 [NCBI, ExPASy, EBI, Israel, Japan] Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.; "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."; J. Immunol. 179:5864-5876(2007).
[4]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1033-1406 IN COMPLEX WITH RAC1. DOI=10.1038/35047014; PubMed=11130063 [NCBI, ExPASy, EBI, Israel, Japan] Worthylake D.K., Rossman K.L., Sondek J.; "Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1."; Nature 408:682-688(2000).

Comments

FUNCTION: 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 (By similarity). Affects invasiveness of T-lymphoma cells.
SUBUNIT: Interacts with BAIAP2 (By similarity).
TISSUE SPECIFICITY: 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.
SIMILARITY: Belongs to the TIAM family.
SIMILARITY: Contains 1 DH (DBL-homology) domain.
SIMILARITY: Contains 1 PDZ (DHR) domain.
SIMILARITY: Contains 2 PH domains.
SIMILARITY: Contains 1 RBD (Ras-binding) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U05245; AAA18830.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00119006; -.

A54146; A54146.

3D structure databases

PDB

1FOE; X-ray; 2.80 A; A/C/E/G=1033-1406.

[ExPASy / RCSB / EBI]

1FOE; -.

Q60610; 835-935.

PTM databases

Q60610; -.

2D gel databases

SWISS-2DPAGE

Q60610; -.

Organism-specific databases

MGI

MGI:103306; Tiam1.

Gene expression databases

Q60610; -.

Q60610; -.

MM_TIAM1; -.

ENSMUSG00000002489; Mus musculus.

Ontologies

GO:0005622;	Cellular component: intracellular (inferred from electronic annotation from InterPro).
GO:0005886;	Cellular component: plasma membrane (inferred from direct assay from MGI).
GO:0046875;	Molecular function: ephrin receptor binding (inferred from physical interaction from MGI).
GO:0005543;	Molecular function: phospholipid binding (inferred from direct assay from MGI).
GO:0005057;	Molecular function: receptor signaling protein activity (inferred from electronic annotation from InterPro).
GO:0005089;	Molecular function: Rho guanyl-nucleotide exchange factor activity (inferred from electronic annotation from InterPro).
GO:0048013;	Biological process: ephrin receptor signaling pathway (inferred from direct assay from MGI).
GO:0050772;	Biological process: positive regulation of axonogenesis (inferred from mutant phenotype from MGI).
GO:0035023;	Biological process: regulation of Rho protein signal transduction (inferred from electronic annotation from InterPro).
GO:0007264;	Biological process: small GTPase mediated signal transduction (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR000219; DH-domain.
IPR001331; GDS_CDC24_CS.
IPR001478; PDZ/DHR/GLGF.
IPR011993; PH_type.
IPR001849; Pleckstrin_homology.
IPR003116; Raf-like_ras_bd.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 2.
G3DSA:1.20.900.10; RhoGEF; 1.

Pfam

PF00595; PDZ; 1.
PF00169; PH; 2.
PF02196; RBD; 1.
PF00621; RhoGEF; 1.
Pfam graphical view of domain structure.

SMART

SM00228; PDZ; 1.
SM00233; PH; 2.
SM00455; RBD; 1.
SM00325; RhoGEF; 1.
SMART graphical view of domain structure.

PROSITE

PS00741; DH_1; 1.
PS50010; DH_2; 1.
PS50106; PDZ; 1.
PS50003; PH_DOMAIN; 1.
PS50898; RBD; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q60610; -.

Genome annotation databases

Ensembl

ENSMUSG00000002489; Mus musculus. [Contig view]

KEGG

mmu:21844; -.

Phylogenomic databases

HOGENOM

Q60610; -.

HOVERGEN

Q60610; -.

Other

301314; -.

Q60610; -.

Tiam1; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Guanine-nucleotide releasing factor; Lipoprotein; Myristate; Phosphoprotein; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (Potential).`
`CHAIN`	`2 1591`	`1590`	`T-lymphoma invasion and metastasis-inducing protein 1.`	`PRO_0000080977`
`DOMAIN`	`434 549`	`116`	`PH 1.`
`DOMAIN`	`765 832`	`68`	`RBD.`
`DOMAIN`	`845 908`	`64`	`PDZ.`
`DOMAIN`	`1040 1234`	`195`	`DH.`
`DOMAIN`	`1261 1397`	`137`	`PH 2.`
`COMPBIAS`	`595 598`	`4`	`Poly-Lys.`
`COMPBIAS`	`1445 1449`	`5`	`Poly-Arg.`
`MOD_RES`	`231 231`		`Phosphoserine.`
`MOD_RES`	`1323 1323`		`Phosphotyrosine.`
`LIPID`	`2 2`		`N-myristoyl glycine (Potential).`
`HELIX`	`1037 1065`	`29`
`HELIX`	`1067 1071`	`5`
`STRAND`	`1073 1076`	`4`
`HELIX`	`1078 1085`	`8`
`HELIX`	`1088 1106`	`19`
`HELIX`	`1112 1114`	`3`
`HELIX`	`1118 1121`	`4`
`HELIX`	`1122 1135`	`14`
`HELIX`	`1138 1141`	`4`
`HELIX`	`1142 1148`	`7`
`TURN`	`1149 1151`	`3`
`HELIX`	`1152 1156`	`5`
`TURN`	`1157 1161`	`5`
`HELIX`	`1163 1172`	`10`
`HELIX`	`1178 1180`	`3`
`HELIX`	`1182 1185`	`4`
`HELIX`	`1188 1193`	`6`
`HELIX`	`1196 1205`	`10`
`HELIX`	`1212 1249`	`38`
`HELIX`	`1264 1266`	`3`
`STRAND`	`1267 1277`	`11`
`HELIX`	`1280 1283`	`4`
`STRAND`	`1290 1296`	`7`
`STRAND`	`1299 1304`	`6`
`TURN`	`1318 1321`	`4`
`STRAND`	`1332 1336`	`5`
`HELIX`	`1337 1339`	`3`
`STRAND`	`1340 1343`	`4`
`TURN`	`1348 1351`	`4`
`STRAND`	`1355 1360`	`6`
`HELIX`	`1365 1367`	`3`
`STRAND`	`1371 1379`	`9`
`HELIX`	`1380 1400`	`21`

Sequence information

Length: 1591 AA [This is the length of the unprocessed precursor]

Molecular weight: 177533 Da [This is the MW of the unprocessed precursor]

CRC64: ECC2BAB189A6F019 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGNAESQNVD HEFYGEKHAS LGRKHTSRSL RLSHKTRRTR HASSGKAIHR NSEVSTRSSS 

        70         80         90        100        110        120 
TPSIPQSLAE NGLEPFSQEG ALDDFGDPIW VDRVDMGLRP VSYTDSSVTP SVDGSIVLTA 

       130        140        150        160        170        180 
ASVQSMPDSE ESRLYGDDAT YLAEGGRRQC PYTSNGPTFM ETASFKKKRS KSADIWREDS 

       190        200        210        220        230        240 
LEFSLSDLSQ EHLTSNEEIL GSAEEKDCEE ARGMETEASP RQLSTCQRAN SLGDLYAQKN 

       250        260        270        280        290        300 
SGVKANGGPR NRFSSYCRNL VSDIPDLAKH KMPPAAAEET PPYSNYNTLP CRKSHCLSEG 

       310        320        330        340        350        360 
ATNPQISLSK SMQGRRAKTT QDVNTGEGSE FADSGIEGAT TDTDLLSRRS NATNSSYSPP 

       370        380        390        400        410        420 
TGRAFVGSDS GSSSTGDRAR QGVYENFRRE LEMSTTNSES LEEAGSAHSD EQSSGTLSSP 

       430        440        450        460        470        480 
GQSDILLTAA QGTVRKAGAL AVKNFLVHKK NKKVESATRR KWKHYWVSLK GCTLFFYETD 

       490        500        510        520        530        540 
GRSGIDHNSV PKHAVWVENS IVQAVPEHPK KDFVFCLSNS LGDAFLFQTT SQTELENWIT 

       550        560        570        580        590        600 
AIHSACAAAV ARHHHKEDTL RLLKSEIKKL EQKIDMDEKM KKMGEMQLSS VTDSKKKKTI 

       610        620        630        640        650        660 
LDQIFVWEQN LEQFQMDLFR FRCYLASLQG GELPNPKRLL AFASRPTKVA MGRLGIFSVS 

       670        680        690        700        710        720 
SFHALVAART GEIGVRRRTQ AMSRSASKRR SRFSSLWGLD TTSKKKQGRP TINQVFGEGT 

       730        740        750        760        770        780 
DAVKRSLEGI FDDTVPDGKR EKEVVLPSVH QHNPDCDIWV HEYFTPSWFC LPNNQPALTV 

       790        800        810        820        830        840 
VRPGDTARDT LELICKTHQL DHSAHYLRLK FLMENRVQFY IPQPEEDIYE LLYKEIEICP 

       850        860        870        880        890        900 
KVTQNIHIEK SDAAADNYGF LLSSVDEDGI RRLYVNSVKE TGLASKKGLK AGDEILEINN 

       910        920        930        940        950        960 
RAAGTLNSSM LKDFLSQPSL GLLVRTYPEP EGGVELLENP PHRVDGPVDL GESPLAFLTS 

       970        980        990       1000       1010       1020 
NPGHSLSSEQ GSSAETAPEE GEGPDLESSD ETDHSSKSTE QVAAFCRSLH EMSPSDSSPS 

      1030       1040       1050       1060       1070       1080 
PQDATSPQLA TTRQLSDADK LRKVICELLE TERTYVKDLN CLMERYLKPL QKETFLTQDE 

      1090       1100       1110       1120       1130       1140 
LDVLFGNLTE MVEFQVEFLK TLEDGVRLVP DLEKLEKVDQ FKKVLFSLGG SFLYYADRFK 

      1150       1160       1170       1180       1190       1200 
LYSAFCASHT KVPKVLVKAK TDTAFKAFLD AQNPRQQHSS TLESYLIKPI QRVLKYPLLL 

      1210       1220       1230       1240       1250       1260 
RELFALTDAE SEEHYHLDVA IKTMNKVASH INEMQKIHEE FGAVFDQLIA EQTGEKKEVA 

      1270       1280       1290       1300       1310       1320 
DLSMGDLLLH TSVIWLNPPA SLGKWKKEPE LAAFVFKTAV VLVYKDGSKQ KKKLVGSHRL 

      1330       1340       1350       1360       1370       1380 
SIYEEWDPFR FRHMIPTEAL QVRALPSADA EANAVCEIVH VKSESEGRPE RVFHLCCSSP 

      1390       1400       1410       1420       1430       1440 
ESRKDFLKSV HSILRDKHRR QLLKTESLPS AQQYVPFGGK RLCALKGARP AMSRAVSAPS 

      1450       1460       1470       1480       1490       1500 
KSLGRRRRRL ARNRFTIDSD AISASSPEKE PQQPAGGGDT DRWVEEQFDL AQYEEQDDIK 

      1510       1520       1530       1540       1550       1560 
ETDILSDDDE FCESLKGASV DRDLQEQLQA ASISQRARGR RTLDSHASRM TQLKKQAALS 

      1570       1580       1590 
GINGGLESAS EEVIWVRRED FAPSRKLNTE I

Q60610 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools