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Q13009 (TIAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-lymphoma invasion and metastasis-inducing protein 1

Short name=TIAM-1
Gene names
Name:TIAM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1591 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Required for normal cell adhesion and cell migration. Ref.14

Subunit structure

Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Interacts with NTRK2; mediates the activation of RAC1 by BDNF. Interacts with MAPK8IP2 and CD44 By similarity. Interacts with BAIAP2. Interacts with EPHA8; regulates clathrin-mediated endocytosis of EPHA8. Interacts with PARD3. Interacts (via PDZ domain) with CNTNAP4, SDC1 and SDC3 (via C-terminus). Ref.4 Ref.6 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16

Subcellular location

Cell junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Detected at the boundary between cells with actin-rich protrusions By similarity. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction. Ref.10 Ref.14

Tissue specificity

Found in virtually all analyzed tumor cell lines including B- and T-lymphomas, neuroblastomas, melanomas and carcinomas.

Domain

The first PH domain mediates interaction with membranes enriched in phosphoinositides By similarity.

Sequence similarities

Belongs to the TIAM family.

Contains 1 DH (DBL-homology) domain.

Contains 1 PDZ (DHR) domain.

Contains 2 PH domains.

Contains 1 RBD (Ras-binding) domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandLipid-binding
   Molecular functionGuanine-nucleotide releasing factor
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from mutant phenotype Ref.14. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement. Source: Reactome

cell migration

Inferred from mutant phenotype Ref.14. Source: UniProtKB

cell-matrix adhesion

Inferred from mutant phenotype Ref.14. Source: UniProtKB

ephrin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of Rac GTPase activity

Inferred from mutant phenotype Ref.14. Source: GOC

regulation of Rho GTPase activity

Traceable author statement PubMed 10835422. Source: GOC

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcell-cell contact zone

Inferred from direct assay Ref.14. Source: UniProtKB

cell-cell junction

Inferred from direct assay Ref.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionRac guanyl-nucleotide exchange factor activity

Inferred from mutant phenotype Ref.14. Source: UniProtKB

Rho guanyl-nucleotide exchange factor activity

Traceable author statement PubMed 10835422. Source: ProtInc

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

receptor signaling protein activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 15911590T-lymphoma invasion and metastasis-inducing protein 1
PRO_0000080976

Regions

Domain434 – 549116PH 1
Domain765 – 83268RBD
Domain845 – 90864PDZ
Domain1040 – 1234195DH
Domain1261 – 1397137PH 2
Compositional bias595 – 5984Poly-Lys
Compositional bias1445 – 14495Poly-Arg

Amino acid modifications

Modified residue2311Phosphoserine Ref.8 Ref.9 Ref.12
Modified residue8291Phosphotyrosine; by NTRK2 By similarity
Modified residue13231Phosphotyrosine By similarity
Lipidation21N-myristoyl glycine Potential

Natural variations

Natural variant2471G → R.
Corresponds to variant rs2070418 [ dbSNP | Ensembl ].
VAR_051991
Natural variant2471G → V.
Corresponds to variant rs2070417 [ dbSNP | Ensembl ].
VAR_051992
Natural variant6781R → C in a colorectal cancer sample; somatic mutation. Ref.17
VAR_035977
Natural variant8441Q → H. Ref.1
Corresponds to variant rs16987932 [ dbSNP | Ensembl ].
VAR_051993
Natural variant10071R → H. Ref.18
Corresponds to variant rs77092908 [ dbSNP | Ensembl ].
VAR_067424
Natural variant13391A → V in a colorectal cancer sample; somatic mutation. Ref.17
VAR_035978

Experimental info

Mutagenesis8791K → E: Strongly reduces affinity for SDC1. Ref.16
Mutagenesis9121K → E: Strongly reduces affinity for SDC1. Ref.16
Sequence conflict24 – 252KH → ND in AAA98443. Ref.1
Sequence conflict2471G → M in AAA98443. Ref.1
Sequence conflict9511G → D in AAA98443. Ref.1
Sequence conflict10181S → N in AAA98443. Ref.1
Sequence conflict1040 – 10412KL → NV in AAA98443. Ref.1
Sequence conflict11481S → I in AAA98443. Ref.1

Secondary structure

.................................................... 1591
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13009 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 0DAFBEE9A84B3452

FASTA1,591177,508
        10         20         30         40         50         60 
MGNAESQHVE HEFYGEKHAS LGRKHTSRSL RLSHKTRRTR HASSGKVIHR NSEVSTRSSS 

        70         80         90        100        110        120 
TPSIPQSLAE NGLEPFSQDG TLEDFGSPIW VDRVDMGLRP VSYTDSSVTP SVDSSIVLTA 

       130        140        150        160        170        180 
ASVQSMPDTE ESRLYGDDAT YLAEGGRRQH SYTSNGPTFM ETASFKKKRS KSADIWREDS 

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

       250        260        270        280        290        300 
SGVTANGGPG SKFAGYCRNL VSDIPNLANH KMPPAAAEET PPYSNYNTLP CRKSHCLSEG 

       310        320        330        340        350        360 
ATNPQISHSN SMQGRRAKTT QDVNAGEGSE FADSGIEGAT TDTDLLSRRS NATNSSYSPT 

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

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

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

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

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

       670        680        690        700        710        720 
SFHALVAART GETGVRRRTQ AMSRSASKRR SRFSSLWGLD TTSKKKQGRP SINQVFGEGT 

       730        740        750        760        770        780 
EAVKKSLEGI FDDIVPDGKR EKEVVLPNVH QHNPDCDIWV HEYFTPSWFC LPNNQPALTV 

       790        800        810        820        830        840 
VRPGDTARDT LELICKTHQL DHSAHYLRLK FLIENKMQLY VPQPEEDIYE LLYKEIEICP 

       850        860        870        880        890        900 
KVTQSIHIEK SDTAADTYGF SLSSVEEDGI RRLYVNSVKE TGLASKKGLK AGDEILEINN 

       910        920        930        940        950        960 
RAADALNSSM LKDFLSQPSL GLLVRTYPEL EEGVELLESP PHRVDGPADL GESPLAFLTS 

       970        980        990       1000       1010       1020 
NPGHSLCSEQ GSSAETAPEE TEGPDLESSD ETDHSSKSTE QVAAFCRSLH EMNPSDQSPS 

      1030       1040       1050       1060       1070       1080 
PQDSTGPQLA TMRQLSDADK 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 AQNPKQQHSS TLESYLIKPI QRILKYPLLL 

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

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

      1330       1340       1350       1360       1370       1380 
SIYEDWDPFR FRHMIPTEAL QVRALASADA EANAVCEIVH VKSESEGRPE RVFHLCCSSP 

      1390       1400       1410       1420       1430       1440 
ESRKDFLKAV HSILRDKHRR QLLKTESLPS SQQYVPFGGK RLCALKGARP AMSRAVSAPS 

      1450       1460       1470       1480       1490       1500 
KSLGRRRRRL ARNRFTIDSD AVSASSPEKE SQQPPGGGDT DRWVEEQFDL AQYEEQDDIK 

      1510       1520       1530       1540       1550       1560 
ETDILSDDDE FCESVKGASV DRDLQERLQA TSISQRERGR KTLDSHASRM AQLKKQAALS 

      1570       1580       1590 
GINGGLESAS EEVIWVRRED FAPSRKLNTE I 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the human invasion-inducing TIAM1 gene, its conservation in evolution and its expression in tumor cell lines of different tissue origin."
Habets G.G.M., van der Kammen R.A., Stam J.C., Michiels F., Collard J.G.
Oncogene 10:1371-1376(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-844.
Tissue: Fetal brain.
[2]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [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].
[4]"A role for Rac in Tiam1-induced membrane ruffling and invasion."
Michiels F., Habets G.G.M., Stam J.C., van der Kammen R.A., Collard J.G.
Nature 375:338-340(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAC.
Tissue: Brain.
[5]"The invasion-inducing TIAM1 gene maps to human chromosome band 21q22 and mouse chromosome 16."
Habets G.G.M., van der Kammen R.A., Jenkins N.A., Gilbert D.J., Copeland N.G., Hagemeijer A., Collard J.G.
Cytogenet. Cell Genet. 70:48-51(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL LOCATION.
[6]"Tiam1-IRSp53 complex formation directs specificity of rac-mediated actin cytoskeleton regulation."
Connolly B.A., Rice J., Feig L.A., Buchsbaum R.J.
Mol. Cell. Biol. 25:4602-4614(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP2.
[7]"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].
[8]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"CCM1 regulates vascular-lumen organization by inducing endothelial polarity."
Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G., Chapon F., Dejana E.
J. Cell Sci. 123:1073-1080(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[11]"EphA8-ephrinA5 signaling and clathrin-mediated endocytosis is regulated by Tiam-1, a Rac-specific guanine nucleotide exchange factor."
Yoo S., Shin J., Park S.
Mol. Cells 29:603-609(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHA8.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Solution structure of the PDZ domain of T-cell lymphoma invasion and metastasis 1 variant."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 835-935.
[14]"The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion."
Shepherd T.R., Klaus S.M., Liu X., Ramaswamy S., DeMali K.A., Fuentes E.J.
J. Mol. Biol. 398:730-746(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 841-930 IN COMPLEX WITH SYNTHETIC MODEL PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SDC1 AND CNTNAP4.
[15]"High-resolution structure of the Tiam1 PHn-CC-Ex domain."
Joshi M., Gakhar L., Fuentes E.J.
Acta Crystallogr. F 69:744-752(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 429-702, INTERACTION WITH PARD3.
[16]"The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics."
Liu X., Shepherd T.R., Murray A.M., Xu Z., Fuentes E.J.
Structure 21:342-354(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 841-930 IN COMPLEX WITH SDC1, MUTAGENESIS OF LYS-879 AND LYS-912, INTERACTION WITH CNTNAP4; SDC1 AND SDC3.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-678 AND VAL-1339.
[18]"Recessive mutations in ELOVL4 cause ichthyosis, intellectual disability, and spastic quadriplegia."
Aldahmesh M.A., Mohamed J.Y., Alkuraya H.S., Verma I.C., Puri R.D., Alaiya A.A., Rizzo W.B., Alkuraya F.S.
Am. J. Hum. Genet. 89:745-750(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-1007.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16296 mRNA. Translation: AAA98443.1.
AP000246 Genomic DNA. No translation available.
AP000247 Genomic DNA. No translation available.
BC117192 mRNA. Translation: AAI17193.1.
BC117196 mRNA. Translation: AAI17197.1.
CCDSCCDS13609.1.
RefSeqNP_003244.2. NM_003253.2.
XP_005261094.1. XM_005261037.1.
XP_005261095.1. XM_005261038.1.
XP_005261096.1. XM_005261039.2.
UniGeneHs.517228.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8INMR-A835-935[»]
3KZDX-ray1.30A841-930[»]
3KZEX-ray1.80A/B/C841-930[»]
4GVCX-ray1.54A841-930[»]
4GVDX-ray1.85A/B841-930[»]
4K2OX-ray2.15A429-702[»]
4K2PX-ray1.98A/B/C/D429-702[»]
ProteinModelPortalQ13009.
SMRQ13009. Positions 433-670, 835-935, 1034-1401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112930. 22 interactions.
DIPDIP-38309N.
IntActQ13009. 8 interactions.
MINTMINT-1746272.
STRING9606.ENSP00000286827.

PTM databases

PhosphoSiteQ13009.

Polymorphism databases

DMDM152031709.

Proteomic databases

MaxQBQ13009.
PaxDbQ13009.
PRIDEQ13009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286827; ENSP00000286827; ENSG00000156299.
GeneID7074.
KEGGhsa:7074.
UCSCuc002yow.1. human.

Organism-specific databases

CTD7074.
GeneCardsGC21M032490.
H-InvDBHIX0016054.
HGNCHGNC:11805. TIAM1.
HPACAB010416.
MIM600687. gene.
neXtProtNX_Q13009.
PharmGKBPA36514.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5422.
HOGENOMHOG000154573.
HOVERGENHBG059279.
InParanoidQ13009.
KOK05731.
OMATVIWLNP.
OrthoDBEOG7F24RZ.
PhylomeDBQ13009.
TreeFamTF319686.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ13009.
BgeeQ13009.
CleanExHS_TIAM1.
GenevestigatorQ13009.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
2.30.42.10. 1 hit.
InterProIPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR003116. Raf-like_ras-bd.
[Graphical view]
PfamPF00595. PDZ. 1 hit.
PF00169. PH. 1 hit.
PF02196. RBD. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
SM00455. RBD. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMSSF48065. SSF48065. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50898. RBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13009.
GenomeRNAi7074.
NextBio27667.
PROQ13009.
SOURCESearch...

Entry information

Entry nameTIAM1_HUMAN
AccessionPrimary (citable) accession number: Q13009
Secondary accession number(s): Q17RT7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 133 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM