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Q13009

- TIAM1_HUMAN

UniProt

Q13009 - TIAM1_HUMAN

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Protein

T-lymphoma invasion and metastasis-inducing protein 1

Gene

TIAM1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

GO - Molecular functioni

  1. phospholipid binding Source: Ensembl
  2. Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
  3. receptor signaling protein activity Source: InterPro
  4. Rho guanyl-nucleotide exchange factor activity Source: ProtInc

GO - Biological processi

  1. apoptotic signaling pathway Source: Reactome
  2. cell-matrix adhesion Source: UniProtKB
  3. cell migration Source: UniProtKB
  4. ephrin receptor signaling pathway Source: Ensembl
  5. neurotrophin TRK receptor signaling pathway Source: Reactome
  6. positive regulation of apoptotic process Source: Reactome
  7. positive regulation of axonogenesis Source: Ensembl
  8. positive regulation of Rac GTPase activity Source: GOC
  9. positive regulation of Rho GTPase activity Source: GOC
  10. Rac protein signal transduction Source: UniProtKB
  11. regulation of small GTPase mediated signal transduction Source: Reactome
  12. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
REACT_228085. EPHB-mediated forward signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.

Names & Taxonomyi

Protein namesi
Recommended name:
T-lymphoma invasion and metastasis-inducing protein 1
Short name:
TIAM-1
Gene namesi
Name:TIAM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:11805. TIAM1.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cell-cell contact zone Source: UniProtKB
  2. cell-cell junction Source: UniProtKB
  3. cytosol Source: Reactome
  4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi879 – 8791K → E: Strongly reduces affinity for SDC1. 1 Publication
Mutagenesisi912 – 9121K → E: Strongly reduces affinity for SDC1. 1 Publication

Organism-specific databases

PharmGKBiPA36514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedSequence Analysis
Chaini2 – 15911590T-lymphoma invasion and metastasis-inducing protein 1PRO_0000080976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence Analysis
Modified residuei231 – 2311Phosphoserine3 Publications
Modified residuei829 – 8291Phosphotyrosine; by NTRK2By similarity
Modified residuei1323 – 13231PhosphotyrosineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ13009.
PaxDbiQ13009.
PRIDEiQ13009.

PTM databases

PhosphoSiteiQ13009.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ13009.
CleanExiHS_TIAM1.
ExpressionAtlasiQ13009. baseline and differential.
GenevestigatoriQ13009.

Organism-specific databases

HPAiCAB010416.

Interactioni

Subunit structurei

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).By similarity7 Publications

Protein-protein interaction databases

BioGridi112930. 25 interactions.
DIPiDIP-38309N.
IntActiQ13009. 8 interactions.
MINTiMINT-1746272.
STRINGi9606.ENSP00000286827.

Structurei

Secondary structure

1
1591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi435 – 44915Combined sources
Turni450 – 4523Combined sources
Beta strandi453 – 4564Combined sources
Beta strandi463 – 4708Combined sources
Beta strandi473 – 4775Combined sources
Beta strandi481 – 4833Combined sources
Beta strandi492 – 4965Combined sources
Beta strandi501 – 5044Combined sources
Beta strandi512 – 5187Combined sources
Beta strandi520 – 5223Combined sources
Beta strandi524 – 5285Combined sources
Helixi532 – 55423Combined sources
Helixi559 – 58729Combined sources
Turni588 – 5903Combined sources
Helixi594 – 62936Combined sources
Helixi636 – 6405Combined sources
Helixi645 – 65410Combined sources
Helixi659 – 6679Combined sources
Beta strandi842 – 8498Combined sources
Turni855 – 8584Combined sources
Beta strandi859 – 8657Combined sources
Beta strandi867 – 8704Combined sources
Beta strandi872 – 8787Combined sources
Helixi883 – 8864Combined sources
Beta strandi894 – 8985Combined sources
Helixi903 – 9053Combined sources
Helixi908 – 9169Combined sources
Beta strandi917 – 92610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ13009.
SMRiQ13009. Positions 433-670, 835-935, 1034-1401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini434 – 549116PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini765 – 83268RBDPROSITE-ProRule annotationAdd
BLAST
Domaini845 – 90864PDZPROSITE-ProRule annotationAdd
BLAST
Domaini1040 – 1234195DHPROSITE-ProRule annotationAdd
BLAST
Domaini1261 – 1397137PH 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi595 – 5984Poly-Lys
Compositional biasi1445 – 14495Poly-Arg

Domaini

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

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

eggNOGiCOG5422.
GeneTreeiENSGT00760000118925.
HOGENOMiHOG000154573.
HOVERGENiHBG059279.
InParanoidiQ13009.
KOiK05731.
OMAiTVIWLNP.
OrthoDBiEOG7F24RZ.
PhylomeDBiQ13009.
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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR003116. Raf-like_ras-bd.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 1 hit.
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.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13009-1) [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
MGNAESQHVE HEFYGEKHAS LGRKHTSRSL RLSHKTRRTR HASSGKVIHR
60 70 80 90 100
NSEVSTRSSS TPSIPQSLAE NGLEPFSQDG TLEDFGSPIW VDRVDMGLRP
110 120 130 140 150
VSYTDSSVTP SVDSSIVLTA ASVQSMPDTE ESRLYGDDAT YLAEGGRRQH
160 170 180 190 200
SYTSNGPTFM ETASFKKKRS KSADIWREDS LEFSLSDLSQ EHLTSNEEIL
210 220 230 240 250
GSAEEKDCEE ARGMETRASP RQLSTCQRAN SLGDLYAQKN SGVTANGGPG
260 270 280 290 300
SKFAGYCRNL VSDIPNLANH KMPPAAAEET PPYSNYNTLP CRKSHCLSEG
310 320 330 340 350
ATNPQISHSN SMQGRRAKTT QDVNAGEGSE FADSGIEGAT TDTDLLSRRS
360 370 380 390 400
NATNSSYSPT TGRAFVGSDS GSSSTGDAAR QGVYENFRRE LEMSTTNSES
410 420 430 440 450
LEEAGSAHSD EQSSGTLSSP GQSDILLTAA QGTVRKAGAL AVKNFLVHKK
460 470 480 490 500
NKKVESATRR KWKHYWVSLK GCTLFFYESD GRSGIDHNSI PKHAVWVENS
510 520 530 540 550
IVQAVPEHPK KDFVFCLSNS LGDAFLFQTT SQTELENWIT AIHSACATAV
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 GETGVRRRTQ AMSRSASKRR SRFSSLWGLD
710 720 730 740 750
TTSKKKQGRP SINQVFGEGT EAVKKSLEGI FDDIVPDGKR EKEVVLPNVH
760 770 780 790 800
QHNPDCDIWV HEYFTPSWFC LPNNQPALTV VRPGDTARDT LELICKTHQL
810 820 830 840 850
DHSAHYLRLK FLIENKMQLY VPQPEEDIYE LLYKEIEICP KVTQSIHIEK
860 870 880 890 900
SDTAADTYGF SLSSVEEDGI RRLYVNSVKE TGLASKKGLK AGDEILEINN
910 920 930 940 950
RAADALNSSM LKDFLSQPSL GLLVRTYPEL EEGVELLESP PHRVDGPADL
960 970 980 990 1000
GESPLAFLTS NPGHSLCSEQ GSSAETAPEE TEGPDLESSD ETDHSSKSTE
1010 1020 1030 1040 1050
QVAAFCRSLH EMNPSDQSPS PQDSTGPQLA TMRQLSDADK 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 AQNPKQQHSS TLESYLIKPI QRILKYPLLL
1210 1220 1230 1240 1250
RELFALTDAE SEEHYHLDVA IKTMNKVASH INEMQKIHEE FGAVFDQLIA
1260 1270 1280 1290 1300
EQTGEKKEVA DLSMGDLLLH TTVIWLNPPA SLGKWKKEPE LAAFVFKTAV
1310 1320 1330 1340 1350
VLVYKDGSKQ KKKLVGSHRL SIYEDWDPFR FRHMIPTEAL QVRALASADA
1360 1370 1380 1390 1400
EANAVCEIVH VKSESEGRPE RVFHLCCSSP ESRKDFLKAV HSILRDKHRR
1410 1420 1430 1440 1450
QLLKTESLPS SQQYVPFGGK RLCALKGARP AMSRAVSAPS KSLGRRRRRL
1460 1470 1480 1490 1500
ARNRFTIDSD AVSASSPEKE SQQPPGGGDT DRWVEEQFDL AQYEEQDDIK
1510 1520 1530 1540 1550
ETDILSDDDE FCESVKGASV DRDLQERLQA TSISQRERGR KTLDSHASRM
1560 1570 1580 1590
AQLKKQAALS GINGGLESAS EEVIWVRRED FAPSRKLNTE I
Length:1,591
Mass (Da):177,508
Last modified:July 10, 2007 - v2
Checksum:i0DAFBEE9A84B3452
GO
Isoform 2 (identifier: Q13009-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     715-739: Missing.
     797-831: Missing.

Note: No experimental confirmation available.

Show »
Length:1,531
Mass (Da):170,580
Checksum:i8A5611505BD43336
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 252KH → ND in AAA98443. (PubMed:7731688)Curated
Sequence conflicti247 – 2471G → M in AAA98443. (PubMed:7731688)Curated
Sequence conflicti881 – 8811T → I in AAI43981. (PubMed:15489334)Curated
Sequence conflicti951 – 9511G → D in AAA98443. (PubMed:7731688)Curated
Sequence conflicti1018 – 10181S → N in AAA98443. (PubMed:7731688)Curated
Sequence conflicti1040 – 10412KL → NV in AAA98443. (PubMed:7731688)Curated
Sequence conflicti1148 – 11481S → I in AAA98443. (PubMed:7731688)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471G → R.
Corresponds to variant rs2070418 [ dbSNP | Ensembl ].
VAR_051991
Natural varianti247 – 2471G → V.
Corresponds to variant rs2070417 [ dbSNP | Ensembl ].
VAR_051992
Natural varianti678 – 6781R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035977
Natural varianti844 – 8441Q → H.1 Publication
Corresponds to variant rs16987932 [ dbSNP | Ensembl ].
VAR_051993
Natural varianti1007 – 10071R → H.1 Publication
Corresponds to variant rs77092908 [ dbSNP | Ensembl ].
VAR_067424
Natural varianti1023 – 10231D → V.1 Publication
Corresponds to variant rs75483199 [ dbSNP | Ensembl ].
VAR_071102
Natural varianti1339 – 13391A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035978

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei715 – 73925Missing in isoform 2. 1 PublicationVSP_055865Add
BLAST
Alternative sequencei797 – 83135Missing in isoform 2. 1 PublicationVSP_055866Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16296 mRNA. Translation: AAA98443.1.
AP000246 Genomic DNA. No translation available.
AP000247 Genomic DNA. No translation available.
AP000248 Genomic DNA. No translation available.
AP000249 Genomic DNA. No translation available.
AP000250 Genomic DNA. No translation available.
AP000251 Genomic DNA. No translation available.
AP000563 Genomic DNA. No translation available.
BC117192 mRNA. Translation: AAI17193.1.
BC117196 mRNA. Translation: AAI17197.1.
BC143980 mRNA. Translation: AAI43981.1.
CCDSiCCDS13609.1. [Q13009-1]
RefSeqiNP_003244.2. NM_003253.2. [Q13009-1]
XP_005261094.1. XM_005261037.1. [Q13009-1]
XP_005261095.1. XM_005261038.1. [Q13009-1]
XP_005261096.1. XM_005261039.2. [Q13009-1]
UniGeneiHs.517228.

Genome annotation databases

EnsembliENST00000286827; ENSP00000286827; ENSG00000156299. [Q13009-1]
ENST00000541036; ENSP00000441570; ENSG00000156299. [Q13009-2]
GeneIDi7074.
KEGGihsa:7074.
UCSCiuc002yow.1. human. [Q13009-1]

Polymorphism databases

DMDMi152031709.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16296 mRNA. Translation: AAA98443.1 .
AP000246 Genomic DNA. No translation available.
AP000247 Genomic DNA. No translation available.
AP000248 Genomic DNA. No translation available.
AP000249 Genomic DNA. No translation available.
AP000250 Genomic DNA. No translation available.
AP000251 Genomic DNA. No translation available.
AP000563 Genomic DNA. No translation available.
BC117192 mRNA. Translation: AAI17193.1 .
BC117196 mRNA. Translation: AAI17197.1 .
BC143980 mRNA. Translation: AAI43981.1 .
CCDSi CCDS13609.1. [Q13009-1 ]
RefSeqi NP_003244.2. NM_003253.2. [Q13009-1 ]
XP_005261094.1. XM_005261037.1. [Q13009-1 ]
XP_005261095.1. XM_005261038.1. [Q13009-1 ]
XP_005261096.1. XM_005261039.2. [Q13009-1 ]
UniGenei Hs.517228.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D8I NMR - A 835-935 [» ]
3KZD X-ray 1.30 A 841-930 [» ]
3KZE X-ray 1.80 A/B/C 841-930 [» ]
4GVC X-ray 1.54 A 841-930 [» ]
4GVD X-ray 1.85 A/B 841-930 [» ]
4K2O X-ray 2.15 A 429-702 [» ]
4K2P X-ray 1.98 A/B/C/D 429-702 [» ]
ProteinModelPortali Q13009.
SMRi Q13009. Positions 433-670, 835-935, 1034-1401.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112930. 25 interactions.
DIPi DIP-38309N.
IntActi Q13009. 8 interactions.
MINTi MINT-1746272.
STRINGi 9606.ENSP00000286827.

PTM databases

PhosphoSitei Q13009.

Polymorphism databases

DMDMi 152031709.

Proteomic databases

MaxQBi Q13009.
PaxDbi Q13009.
PRIDEi Q13009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000286827 ; ENSP00000286827 ; ENSG00000156299 . [Q13009-1 ]
ENST00000541036 ; ENSP00000441570 ; ENSG00000156299 . [Q13009-2 ]
GeneIDi 7074.
KEGGi hsa:7074.
UCSCi uc002yow.1. human. [Q13009-1 ]

Organism-specific databases

CTDi 7074.
GeneCardsi GC21M032490.
H-InvDB HIX0016054.
HGNCi HGNC:11805. TIAM1.
HPAi CAB010416.
MIMi 600687. gene.
neXtProti NX_Q13009.
PharmGKBi PA36514.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5422.
GeneTreei ENSGT00760000118925.
HOGENOMi HOG000154573.
HOVERGENi HBG059279.
InParanoidi Q13009.
KOi K05731.
OMAi TVIWLNP.
OrthoDBi EOG7F24RZ.
PhylomeDBi Q13009.
TreeFami TF319686.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
REACT_228085. EPHB-mediated forward signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

ChiTaRSi TIAM1. human.
EvolutionaryTracei Q13009.
GenomeRNAii 7074.
NextBioi 27667.
PROi Q13009.
SOURCEi Search...

Gene expression databases

Bgeei Q13009.
CleanExi HS_TIAM1.
ExpressionAtlasi Q13009. baseline and differential.
Genevestigatori Q13009.

Family and domain databases

Gene3Di 1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
2.30.42.10. 1 hit.
InterProi IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR003116. Raf-like_ras-bd.
[Graphical view ]
Pfami PF00595. PDZ. 1 hit.
PF00169. PH. 1 hit.
PF02196. RBD. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
SM00455. RBD. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEi PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50898. RBD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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.
    , 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] (ISOFORMS 1 AND 2), VARIANT VAL-1023.
  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. 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. 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.

Entry informationi

Entry nameiTIAM1_HUMAN
AccessioniPrimary (citable) accession number: Q13009
Secondary accession number(s): B7ZLR6, F5GZ53, Q17RT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 10, 2007
Last modified: November 26, 2014
This is version 137 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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