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Protein

T-lymphoma invasion and metastasis-inducing protein 2

Gene

Tiam2

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 specifically RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane.5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiR-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-416482. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
T-lymphoma invasion and metastasis-inducing protein 2
Short name:
TIAM-2
Alternative name(s):
SIF and TIAM1-like exchange factor
Gene namesi
Name:Tiam2
Synonyms:Kiaa2016, Stef
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1344338. Tiam2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • filopodium Source: UniProtKB-SubCell
  • growth cone Source: UniProtKB-SubCell
  • lamellipodium Source: UniProtKB-SubCell
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1655 – 16551S → A: No change of phosphorylation by Rho-kinase. 1 Publication
Mutagenesisi1656 – 16561T → A: No change of phosphorylation by Rho-kinase. 1 Publication
Mutagenesisi1662 – 16621T → A: Strongly decrease phosphorylation by Rho-kinase. No change in promoting neurite growth; when associated with A-1668 and A-1672. 1 Publication
Mutagenesisi1668 – 16681T → A: Slight decrease phosphorylation by Rho-kinase. No change in promoting neurite growth; when associated with A-1662 and A-1672. 1 Publication
Mutagenesisi1672 – 16721S → A: Slight decrease phosphorylation by Rho-kinase. No change in promoting neurite growth; when associated with A-1662 and A-1668. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 17151714T-lymphoma invasion and metastasis-inducing protein 2PRO_0000317468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence analysis
Modified residuei1604 – 16041PhosphoserineCombined sources
Modified residuei1662 – 16621Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated on serine and threonine residues. Phosphorylated on Thr-1662 by Rho-kinase. Its phosphorylation by Rho-kinase inhibits its guanine nucleotide exchange activity, its interaction with MAP1A, MAP1B, PARP1 and YWHAE and reduces its ability to promote neurite growth.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ6ZPF3.
PaxDbiQ6ZPF3.
PRIDEiQ6ZPF3.

PTM databases

iPTMnetiQ6ZPF3.
PhosphoSiteiQ6ZPF3.

Expressioni

Tissue specificityi

Expressed in fetal brain (at protein level). Expressed in the olfactory bulb, cortical plate of the cerebral cortex, caudate putamen, hippocampus, ependymal cells of the lateral surface of the lateral ventricles of the brain. Weakly expressed in heart, lung, liver, skeletal muscle, kidney and testis.6 Publications

Developmental stagei

Expressed in cerebral cortex, predominantly in the cortical plate and intermediate zone and weakly in the ventricular zone, in neurites and the growth cone of neurites of the hippocampus at 15 dpc (at protein level). Expressed in embryo at 7, 11, 15 and 17 dpc. Expressed in the preplate which consists of the Cajal-Retzius cells and the precursors of subplate neurons, in neurons of the telecephalon, in primordia of cerebral cortex and hippocampus at 12 dpc. Expressed in the cortical plate, striatum and fourth ventricle of the brain, in the cartilaginous tissues including Meckel, costal, vertebral and tracheal cartilage at 14.5 dpc. Expressed in cerebral cortex, hippocampus, olfactory bulbs, rostral migratory pathway and the striatum at 17 dpc.5 Publications

Gene expression databases

BgeeiQ6ZPF3.
CleanExiMM_TIAM2.
GenevisibleiQ6ZPF3. MM.

Interactioni

Subunit structurei

Interacts with MAP1A, MAP1B, PARP1 and YWHAE. Interacts with CD44, PARD3 and MAPK8IP2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cd44P153798EBI-7565978,EBI-7565891
PARD3Q8TEW02EBI-7565978,EBI-81968From a different organism.
PARD3Q8TEW0-26EBI-7565978,EBI-9118204From a different organism.

Protein-protein interaction databases

IntActiQ6ZPF3. 5 interactions.
MINTiMINT-4131203.
STRINGi10090.ENSMUSP00000072020.

Structurei

Secondary structure

1
1715
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi505 – 52016Combined sources
Helixi521 – 5233Combined sources
Beta strandi524 – 5274Combined sources
Beta strandi534 – 5418Combined sources
Beta strandi544 – 5507Combined sources
Beta strandi563 – 5675Combined sources
Beta strandi572 – 5754Combined sources
Beta strandi583 – 5897Combined sources
Beta strandi595 – 5995Combined sources
Helixi603 – 62422Combined sources
Helixi630 – 65930Combined sources
Helixi665 – 70036Combined sources
Helixi707 – 7115Combined sources
Helixi716 – 72510Combined sources
Helixi730 – 73910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A8PX-ray2.10A/B/C/D500-757[»]
3A8QX-ray3.20A/B/C/D500-757[»]
ProteinModelPortaliQ6ZPF3.
SMRiQ6ZPF3. Positions 504-741, 1115-1482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6ZPF3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini504 – 618115PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini831 – 90272RBDPROSITE-ProRule annotationAdd
BLAST
Domaini911 – 99787PDZPROSITE-ProRule annotationAdd
BLAST
Domaini1120 – 1314195DHPROSITE-ProRule annotationAdd
BLAST
Domaini1347 – 1478132PH 2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili665 – 69228Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi215 – 335121Ser-richAdd
BLAST
Compositional biasi1512 – 156453Ser-richAdd
BLAST

Domaini

The PH 1 domain and amino acids 619-780 (a region called TSS; otherwise known as CC-Ex) are necessary for membrane localization. PH 1 and TSS domains are necessary for Rac1 activity. The PH 2 domain is engaged in the enhancement of the catalytic activity of the adjacent DH domain. The PH 1, TSS and DH domains are necessary to induce neurite-like structure.

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

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410KDSQ. Eukaryota.
ENOG410XPCM. LUCA.
GeneTreeiENSGT00760000118925.
HOVERGENiHBG059279.
InParanoidiQ6ZPF3.
KOiK16847.
OMAiFNTLETP.
OrthoDBiEOG7F24RZ.
PhylomeDBiQ6ZPF3.
TreeFamiTF319686.

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.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZPF3-1) [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
MGNSESQYTF QGSKNHSNTV TGAKQKPCSL KIRSVHAKDE KSLHGWTHGS
60 70 80 90 100
SGAGYKSRSL ARSCLSHFKN HQPYATRLSG PTCKVSKGTT YSKHRANTPG
110 120 130 140 150
NDFQGNSGAF LPENGFHYVD RESEESHITS NGHLLTCYGR KESLASTPPG
160 170 180 190 200
EDHRSPRVLI KTLGKLDGCL RVEFHNGGNP HKGTSEDPSG PVRLLRYSPT
210 220 230 240 250
LASETCPVRE TRRHSAAGSP SSQRPSPTDS RLRSSKGSSL SSESSWYDSP
260 270 280 290 300
WGNAGEVSEV EGSFLAPSTP DPSLPSSFPP SDTKKPFNQS SSLSSLRELY
310 320 330 340 350
KDPNLGCRSP SGTCLSSNEY ISSQVSLNNR VSFASDMDVP SRVDHRDPLH
360 370 380 390 400
YSSFTLPCRK SKALTEDAAK KDTLKARMRR FSDWTGSLSR KKRKLQEPRS
410 420 430 440 450
MEGSEYFDSH SDGLNAEGQV PAQTSSLLWS GGSAQTLPHR SESTHAISVD
460 470 480 490 500
PLRQNIYENF MRELEMSRSN TEHVETSTET MESSSESVSS LEQLDLLFEK
510 520 530 540 550
EQGVVRKAGW LFFKPLVTLQ KERKLELVAR RKWKQYWVTL KGCTLLFYET
560 570 580 590 600
YGKNSTEQNS APRCALFAED SIVQSVPEHP KKEHVFCLSN SCGDVYLFQA
610 620 630 640 650
TSQTDLENWV TAIHSACASL FAKKHGKEDT VRLLKSQTRS LLQKIDMDSK
660 670 680 690 700
MKKMAELQLS VVSDPKNRKA IENQIRQWEQ NLEKFHMDLF RMRCYLASLQ
710 720 730 740 750
GGELPNPKSL LAATSRPSKL ALGRLGVLSV SSFHALVCSR DDSTLRKRTL
760 770 780 790 800
SLTQRGKSKK GIFSSLKGLD TLARKGREKR ASITQMFDSS HSHGFLGTQL
810 820 830 840 850
PQKSTNSNKA HDLHLYGSAV DSALRDSMWE VQTYVHFQDN EGVTVTIKPE
860 870 880 890 900
HRVEDVLALV CKMRQLEPTH YGLQLRKVVD KSVEWCVPAL YEYMQEQVYD
910 920 930 940 950
EIEVFPLSVY DVQLTKTGDM TDFGFAVTVQ VDEHQHLNRI FISDVLPDSL
960 970 980 990 1000
AYGGGLRKGN EITSLNGEPV SDLDIQQMEA LFSEKSVGLT LVARPVTTRR
1010 1020 1030 1040 1050
TLCASWSDSD LFSRDQKSLP PSPNQSQLLE EFLDNFRKTA TSDFSNVPEI
1060 1070 1080 1090 1100
TTGLKRSQTE GTLDQVPHRE KMEQTFLSAD QIAELCRDLN NTHTNSMEAP
1110 1120 1130 1140 1150
TESHDPPPRP LARHLSDADR LRKVIQELVD TEKSYVKDLS CLFELYLEPL
1160 1170 1180 1190 1200
QNETFLTQDE MESLFGSLPE MLEFQKVFLE TLEDAISASS DFSVLETPSQ
1210 1220 1230 1240 1250
FRKLLFSLGG SFLYYADHFK LYSGFCANHI KVQRVLERAK TDKAFKAFLD
1260 1270 1280 1290 1300
ARNPTKQHSS TLESYLIKPV QRVLKYPLLL KELVSLTDHE SEEHYHLTEA
1310 1320 1330 1340 1350
LKAMEKVASH INEMQKIYED YGMVFDQLVA EQSGTEKEVT ELSMGELLMH
1360 1370 1380 1390 1400
STVSWLNPFL SLGKARKDIE LTVFVFKRAV ILVYKENCKL KKKLPSNSRP
1410 1420 1430 1440 1450
AHNSADLDPF KFRWLIPISA LQVRLGNTAG TENNSTWELI HTKSEIEGRP
1460 1470 1480 1490 1500
ETIFQLCCSD SENKTSIVKV IRSILRENFR RHIKCELPLE KTCKDRLVPL
1510 1520 1530 1540 1550
KNRVPVSAKL ASSRSLKGLR TSSSSEWPSE PSKGNSLDSD ECSLSSGTQS
1560 1570 1580 1590 1600
SGCPVAESRR DSKSTELEKD AQEGLAEFPD GLIKESDILS DEDEDFHHPL
1610 1620 1630 1640 1650
KQGSPTKDIE IQFQRLKISE ESDVHPVGQQ PLTESGEQPK LVRGHFCPIK
1660 1670 1680 1690 1700
RKANSTKRGR GTLLKAQTRH QSLDSHPETA SIDLNLVLER EFSVQSLTSV
1710
VNEEGFYETQ SHGKS
Length:1,715
Mass (Da):192,567
Last modified:February 5, 2008 - v2
Checksum:i96C1E063BC6F36C0
GO
Isoform 2 (identifier: Q6ZPF3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     616-616: Missing.

Show »
Length:1,714
Mass (Da):192,496
Checksum:i2FFD3D8FE4D53D8B
GO
Isoform 3 (identifier: Q6ZPF3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1096: Missing.

Show »
Length:619
Mass (Da):70,146
Checksum:i61EBCE09292C61A2
GO
Isoform 4 (identifier: Q6ZPF3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     786-788: MFD → VSS
     789-1715: Missing.

Note: No experimental confirmation available.
Show »
Length:788
Mass (Da):87,583
Checksum:i6234115FF79D5B03
GO

Sequence cautioni

The sequence BAC98284.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451G → D in BAE34377 (PubMed:16141072).Curated
Sequence conflicti98 – 981T → A in BAC98284 (PubMed:14621295).Curated
Sequence conflicti261 – 2611E → D in BAC98284 (PubMed:14621295).Curated
Sequence conflicti803 – 8031K → Q in BAA81823 (PubMed:10364228).Curated
Sequence conflicti856 – 8561V → I in BAA81823 (PubMed:10364228).Curated
Sequence conflicti860 – 8601V → A in BAA81823 (PubMed:10364228).Curated
Sequence conflicti860 – 8601V → A in BAC98284 (PubMed:14621295).Curated
Sequence conflicti1077 – 10771L → P in BAA81823 (PubMed:10364228).Curated
Sequence conflicti1234 – 12341R → K in AAF28865 (PubMed:10512681).Curated
Sequence conflicti1248 – 12481F → C in AAF28865 (PubMed:10512681).Curated
Sequence conflicti1397 – 13971N → D in AAF28865 (PubMed:10512681).Curated
Sequence conflicti1446 – 14461I → V in AAF28865 (PubMed:10512681).Curated
Sequence conflicti1611 – 16111I → L in BAC98284 (PubMed:14621295).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 10961096Missing in isoform 3. 1 PublicationVSP_030976Add
BLAST
Alternative sequencei616 – 6161Missing in isoform 2. 1 PublicationVSP_030977
Alternative sequencei786 – 7883MFD → VSS in isoform 4. 1 PublicationVSP_030978
Alternative sequencei789 – 1715927Missing in isoform 4. 1 PublicationVSP_030979Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022915 mRNA. Translation: BAA81823.1.
AK129474 mRNA. Translation: BAC98284.1. Different initiation.
AK158137 mRNA. Translation: BAE34377.1.
AK161947 mRNA. Translation: BAE36649.1.
BC067048 mRNA. Translation: AAH67048.1.
BC079600 mRNA. Translation: AAH79600.1.
AF121102 mRNA. Translation: AAF28865.1.
CCDSiCCDS37421.1. [Q6ZPF3-1]
RefSeqiNP_001116470.1. NM_001122998.1. [Q6ZPF3-1]
NP_001273686.1. NM_001286757.1. [Q6ZPF3-3]
NP_001273687.1. NM_001286758.1.
NP_036008.2. NM_011878.2. [Q6ZPF3-1]
XP_006523288.1. XM_006523225.2. [Q6ZPF3-1]
XP_006523289.1. XM_006523226.1. [Q6ZPF3-1]
XP_006523296.1. XM_006523233.1. [Q6ZPF3-3]
UniGeneiMm.137134.

Genome annotation databases

EnsembliENSMUST00000072156; ENSMUSP00000072020; ENSMUSG00000023800. [Q6ZPF3-1]
ENSMUST00000169838; ENSMUSP00000125842; ENSMUSG00000023800. [Q6ZPF3-1]
GeneIDi24001.
KEGGimmu:24001.
UCSCiuc008aeo.1. mouse. [Q6ZPF3-1]
uc008aep.1. mouse. [Q6ZPF3-4]
uc008aer.1. mouse. [Q6ZPF3-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022915 mRNA. Translation: BAA81823.1.
AK129474 mRNA. Translation: BAC98284.1. Different initiation.
AK158137 mRNA. Translation: BAE34377.1.
AK161947 mRNA. Translation: BAE36649.1.
BC067048 mRNA. Translation: AAH67048.1.
BC079600 mRNA. Translation: AAH79600.1.
AF121102 mRNA. Translation: AAF28865.1.
CCDSiCCDS37421.1. [Q6ZPF3-1]
RefSeqiNP_001116470.1. NM_001122998.1. [Q6ZPF3-1]
NP_001273686.1. NM_001286757.1. [Q6ZPF3-3]
NP_001273687.1. NM_001286758.1.
NP_036008.2. NM_011878.2. [Q6ZPF3-1]
XP_006523288.1. XM_006523225.2. [Q6ZPF3-1]
XP_006523289.1. XM_006523226.1. [Q6ZPF3-1]
XP_006523296.1. XM_006523233.1. [Q6ZPF3-3]
UniGeneiMm.137134.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A8PX-ray2.10A/B/C/D500-757[»]
3A8QX-ray3.20A/B/C/D500-757[»]
ProteinModelPortaliQ6ZPF3.
SMRiQ6ZPF3. Positions 504-741, 1115-1482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6ZPF3. 5 interactions.
MINTiMINT-4131203.
STRINGi10090.ENSMUSP00000072020.

PTM databases

iPTMnetiQ6ZPF3.
PhosphoSiteiQ6ZPF3.

Proteomic databases

MaxQBiQ6ZPF3.
PaxDbiQ6ZPF3.
PRIDEiQ6ZPF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072156; ENSMUSP00000072020; ENSMUSG00000023800. [Q6ZPF3-1]
ENSMUST00000169838; ENSMUSP00000125842; ENSMUSG00000023800. [Q6ZPF3-1]
GeneIDi24001.
KEGGimmu:24001.
UCSCiuc008aeo.1. mouse. [Q6ZPF3-1]
uc008aep.1. mouse. [Q6ZPF3-4]
uc008aer.1. mouse. [Q6ZPF3-3]

Organism-specific databases

CTDi26230.
MGIiMGI:1344338. Tiam2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410KDSQ. Eukaryota.
ENOG410XPCM. LUCA.
GeneTreeiENSGT00760000118925.
HOVERGENiHBG059279.
InParanoidiQ6ZPF3.
KOiK16847.
OMAiFNTLETP.
OrthoDBiEOG7F24RZ.
PhylomeDBiQ6ZPF3.
TreeFamiTF319686.

Enzyme and pathway databases

ReactomeiR-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-416482. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSiTiam2. mouse.
EvolutionaryTraceiQ6ZPF3.
NextBioi303925.
PROiQ6ZPF3.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZPF3.
CleanExiMM_TIAM2.
GenevisibleiQ6ZPF3. MM.

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.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the stef gene that encodes a novel guanine nucleotide exchange factor specific for Rac1."
    Hoshino M., Sone M., Fukata M., Kuroda S., Kaibuchi K., Nabeshima Y., Hama C.
    J. Biol. Chem. 274:17837-17844(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Brain.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Inner ear and Olfactory bulb.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Cloning and characterization of T-cell lymphoma invasion and metastasis 2 (TIAM2), a novel guanine nucleotide exchange factor related to TIAM1."
    Chiu C.-Y., Leng S., Martin K.A., Kim E., Gorman S., Duhl D.M.
    Genomics 61:66-73(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1232-1498, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  6. "Characterization of STEF, a guanine nucleotide exchange factor for Rac1, required for neurite growth."
    Matsuo N., Hoshino M., Yoshizawa M., Nabeshima Y.
    J. Biol. Chem. 277:2860-2868(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Expression of stef, an activator of Rac1, correlates with the stages of neuronal morphological development in the mouse brain."
    Yoshizawa M., Hoshino M., Sone M., Nabeshima Y.
    Mech. Dev. 113:65-68(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "The in vivo roles of STEF/Tiam1, Rac1 and JNK in cortical neuronal migration."
    Kawauchi T., Chihama K., Nabeshima Y., Hoshino M.
    EMBO J. 22:4190-4201(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  9. "Roles of STEF/Tiam1, guanine nucleotide exchange factors for Rac1, in regulation of growth cone morphology."
    Matsuo N., Terao M., Nabeshima Y., Hoshino M.
    Mol. Cell. Neurosci. 24:69-81(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. Cited for: FUNCTION, INTERACTION WITH MAP1A; MAP1B; PARP1 AND YWHAE, PHOSPHORYLATION AT THR-1662, MUTAGENESIS OF SER-1655; THR-1656; THR-1662; THR-1668 AND SER-1672.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  12. "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module."
    Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T., Kaibuchi K., Hakoshima T.
    EMBO J. 29:236-250(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 500-757, INTERACTION WITH CD44; PARD3 AND MAPK8IP2.

Entry informationi

Entry nameiTIAM2_MOUSE
AccessioniPrimary (citable) accession number: Q6ZPF3
Secondary accession number(s): Q3TSM6
, Q3TZ33, Q6AXF2, Q6NXJ2, Q9JLY2, Q9WVS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: May 11, 2016
This is version 103 of the entry and version 2 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.