Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13009

- TIAM1_HUMAN

UniProt

Q13009 - TIAM1_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (10 Jul 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: InterPro

    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

    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.

    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

    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

    ArrayExpressiQ13009.
    BgeeiQ13009.
    CleanExiHS_TIAM1.
    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. 22 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 – 44915
    Turni450 – 4523
    Beta strandi453 – 4564
    Beta strandi463 – 4708
    Beta strandi473 – 4775
    Beta strandi481 – 4833
    Beta strandi492 – 4965
    Beta strandi501 – 5044
    Beta strandi512 – 5187
    Beta strandi520 – 5223
    Beta strandi524 – 5285
    Helixi532 – 55423
    Helixi559 – 58729
    Turni588 – 5903
    Helixi594 – 62936
    Helixi636 – 6405
    Helixi645 – 65410
    Helixi659 – 6679
    Beta strandi842 – 8498
    Turni855 – 8584
    Beta strandi859 – 8657
    Beta strandi867 – 8704
    Beta strandi872 – 8787
    Helixi883 – 8864
    Beta strandi894 – 8985
    Helixi903 – 9053
    Helixi908 – 9169
    Beta strandi917 – 92610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MGNAESQHVE HEFYGEKHAS LGRKHTSRSL RLSHKTRRTR HASSGKVIHR     50
    NSEVSTRSSS TPSIPQSLAE NGLEPFSQDG TLEDFGSPIW VDRVDMGLRP 100
    VSYTDSSVTP SVDSSIVLTA ASVQSMPDTE ESRLYGDDAT YLAEGGRRQH 150
    SYTSNGPTFM ETASFKKKRS KSADIWREDS LEFSLSDLSQ EHLTSNEEIL 200
    GSAEEKDCEE ARGMETRASP RQLSTCQRAN SLGDLYAQKN SGVTANGGPG 250
    SKFAGYCRNL VSDIPNLANH KMPPAAAEET PPYSNYNTLP CRKSHCLSEG 300
    ATNPQISHSN SMQGRRAKTT QDVNAGEGSE FADSGIEGAT TDTDLLSRRS 350
    NATNSSYSPT TGRAFVGSDS GSSSTGDAAR QGVYENFRRE LEMSTTNSES 400
    LEEAGSAHSD EQSSGTLSSP GQSDILLTAA QGTVRKAGAL AVKNFLVHKK 450
    NKKVESATRR KWKHYWVSLK GCTLFFYESD GRSGIDHNSI PKHAVWVENS 500
    IVQAVPEHPK KDFVFCLSNS LGDAFLFQTT SQTELENWIT AIHSACATAV 550
    ARHHHKEDTL RLLKSEIKKL EQKIDMDEKM KKMGEMQLSS VTDSKKKKTI 600
    LDQIFVWEQN LEQFQMDLFR FRCYLASLQG GELPNPKRLL AFASRPTKVA 650
    MGRLGIFSVS SFHALVAART GETGVRRRTQ AMSRSASKRR SRFSSLWGLD 700
    TTSKKKQGRP SINQVFGEGT EAVKKSLEGI FDDIVPDGKR EKEVVLPNVH 750
    QHNPDCDIWV HEYFTPSWFC LPNNQPALTV VRPGDTARDT LELICKTHQL 800
    DHSAHYLRLK FLIENKMQLY VPQPEEDIYE LLYKEIEICP KVTQSIHIEK 850
    SDTAADTYGF SLSSVEEDGI RRLYVNSVKE TGLASKKGLK AGDEILEINN 900
    RAADALNSSM LKDFLSQPSL GLLVRTYPEL EEGVELLESP PHRVDGPADL 950
    GESPLAFLTS NPGHSLCSEQ GSSAETAPEE TEGPDLESSD ETDHSSKSTE 1000
    QVAAFCRSLH EMNPSDQSPS PQDSTGPQLA TMRQLSDADK LRKVICELLE 1050
    TERTYVKDLN CLMERYLKPL QKETFLTQDE LDVLFGNLTE MVEFQVEFLK 1100
    TLEDGVRLVP DLEKLEKVDQ FKKVLFSLGG SFLYYADRFK LYSAFCASHT 1150
    KVPKVLVKAK TDTAFKAFLD AQNPKQQHSS TLESYLIKPI QRILKYPLLL 1200
    RELFALTDAE SEEHYHLDVA IKTMNKVASH INEMQKIHEE FGAVFDQLIA 1250
    EQTGEKKEVA DLSMGDLLLH TTVIWLNPPA SLGKWKKEPE LAAFVFKTAV 1300
    VLVYKDGSKQ KKKLVGSHRL SIYEDWDPFR FRHMIPTEAL QVRALASADA 1350
    EANAVCEIVH VKSESEGRPE RVFHLCCSSP ESRKDFLKAV HSILRDKHRR 1400
    QLLKTESLPS SQQYVPFGGK RLCALKGARP AMSRAVSAPS KSLGRRRRRL 1450
    ARNRFTIDSD AVSASSPEKE SQQPPGGGDT DRWVEEQFDL AQYEEQDDIK 1500
    ETDILSDDDE FCESVKGASV DRDLQERLQA TSISQRERGR KTLDSHASRM 1550
    AQLKKQAALS GINGGLESAS EEVIWVRRED FAPSRKLNTE I 1591
    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:
    EMBL
    GenBank
    DDBJ
    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.
    RefSeqiNP_003244.2. NM_003253.2.
    XP_005261094.1. XM_005261037.1.
    XP_005261095.1. XM_005261038.1.
    XP_005261096.1. XM_005261039.2.
    UniGeneiHs.517228.

    Genome annotation databases

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

    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:
    EMBL
    GenBank
    DDBJ
    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.
    RefSeqi NP_003244.2. NM_003253.2.
    XP_005261094.1. XM_005261037.1.
    XP_005261095.1. XM_005261038.1.
    XP_005261096.1. XM_005261039.2.
    UniGenei Hs.517228.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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. 22 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.

    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.
    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.

    Miscellaneous databases

    EvolutionaryTracei Q13009.
    GenomeRNAii 7074.
    NextBioi 27667.
    PROi Q13009.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13009.
    Bgeei Q13009.
    CleanExi HS_TIAM1.
    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

    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: October 1, 2014
    This is version 135 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

    Dasty 3