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O75674 (TM1L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TOM1-like protein 1
Alternative name(s):
Src-activating and signaling molecule protein
Target of Myb-like protein 1
Gene names
Name:TOM1L1
Synonyms:SRCASM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions By similarity.

Subunit structure

Interacts with FYN, GRB2 and PIK3R1 when phosphorylated By similarity. Interacts with LYN By similarity.

Subcellular location

Golgi apparatusGolgi stack. Endosome membrane Potential. Cytoplasm By similarity. Membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: A small proportion is membrane-associated By similarity.

Post-translational modification

Phosphorylated on tyrosines by FYN and LYN By similarity.

Sequence similarities

Belongs to the TOM1 family.

Contains 1 GAT domain.

Contains 1 VHS domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Endosome
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainSH3-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of protein kinase activity

Inferred from direct assay PubMed 16479011. Source: UniProtKB

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

negative regulation of mitosis

Inferred from direct assay PubMed 16479011. Source: UniProtKB

positive regulation of protein autophosphorylation

Inferred from direct assay PubMed 16479011. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 16479011. Source: UniProtKB

ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

Non-traceable author statement PubMed 15611048. Source: HGNC

   Cellular_componentGolgi stack

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 16412388. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 15611048. Source: HGNC

endosome

Inferred from direct assay PubMed 16412388. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionclathrin binding

Inferred from direct assay PubMed 16412388. Source: UniProtKB

protein kinase activator activity

Inferred from electronic annotation. Source: Ensembl

protein kinase binding

Inferred from physical interaction PubMed 16479011. Source: UniProtKB

ubiquitin binding

Traceable author statement PubMed 15611048. Source: HGNC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476TOM1-like protein 1
PRO_0000072566

Regions

Domain22 – 154133VHS
Domain200 – 28889GAT
Region392 – 3954Interaction with GRB2 By similarity
Region442 – 4454Interaction with PIK3R1 By similarity
Motif421 – 4255SH3-binding By similarity
Motif460 – 4634SH2-binding By similarity

Amino acid modifications

Modified residue3141Phosphoserine Ref.5
Modified residue3211Phosphoserine Ref.8
Modified residue3231Phosphoserine Ref.5 Ref.6 Ref.8 Ref.9
Modified residue4601Phosphotyrosine By similarity

Natural variations

Natural variant1081R → S.
Corresponds to variant rs16955377 [ dbSNP | Ensembl ].
VAR_047469

Experimental info

Sequence conflict481G → A in CAA08993. Ref.1

Secondary structure

......................... 476
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75674 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 47ED5FA1F40144C0

FASTA47652,989
        10         20         30         40         50         60 
MAFGKSHRDP YATSVGHLIE KATFAGVQTE DWGQFMHICD IINTTQDGPK DAVKALKKRI 

        70         80         90        100        110        120 
SKNYNHKEIQ LTLSLIDMCV QNCGPSFQSL IVKKEFVKEN LVKLLNPRYN LPLDIQNRIL 

       130        140        150        160        170        180 
NFIKTWSQGF PGGVDVSEVK EVYLDLVKKG VQFPPSEAEA ETARQETAQI SSNPPTSVPT 

       190        200        210        220        230        240 
APALSSVIAP KNSTVTLVPE QIGKLHSELD MVKMNVRVMS AILMENTPGS ENHEDIELLQ 

       250        260        270        280        290        300 
KLYKTGREMQ ERIMDLLVVV ENEDVTVELI QVNEDLNNAI LGYERFTRNQ QRILEQNKNQ 

       310        320        330        340        350        360 
KEATNTTSEP SAPSQDLLDL SPSPRMPRAT LGELNTMNNQ LSGLNFSLPS SDVTNNLKPS 

       370        380        390        400        410        420 
LHPQMNLLAL ENTEIPPFAQ RTSQNLTSSH AYDNFLEHSN SVFLQPVSLQ TIAAAPSNQS 

       430        440        450        460        470 
LPPLPSNHPA MTKSDLQPPN YYEVMEFDPL APAVTTEAIY EEIDAHQHKG AQNDGD 

« Hide

References

« Hide 'large scale' references
[1]"TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and encode proteins similar to the endosomal proteins HGS and STAM."
Seroussi E., Kedra D., Kost-Alimova M., Sandberg-Nordqvist A.-C., Fransson I., Jacobs J.F.M., Fu Y., Pan H.-Q., Roe B.A., Imreh S., Dumanski J.P.
Genomics 57:380-388(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Trachea.
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"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-321 AND SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"X-ray crystal structure of the VHS domain of human TOM1-like protein, Northeast structural genomics consortium target HR3050E."
Northeast structural genomics consortium (NESG)
Submitted (JUN-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 9-150.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ010071 mRNA. Translation: CAA08993.1.
AK315039 mRNA. Translation: BAG37522.1.
AK223125 mRNA. Translation: BAD96845.1.
CH471109 Genomic DNA. Translation: EAW94553.1.
RefSeqNP_005477.2. NM_005486.2.
UniGeneHs.153504.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RRUX-ray3.00A/B9-150[»]
ProteinModelPortalO75674.
SMRO75674. Positions 9-149, 159-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115352. 52 interactions.
IntActO75674. 30 interactions.
MINTMINT-1213299.
STRING9606.ENSP00000408958.

PTM databases

PhosphoSiteO75674.

Proteomic databases

PaxDbO75674.
PRIDEO75674.

Protocols and materials databases

DNASU10040.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000575882; ENSP00000460823; ENSG00000141198.
GeneID10040.
KEGGhsa:10040.
UCSCuc002iud.2. human.

Organism-specific databases

CTD10040.
GeneCardsGC17P052978.
H-InvDBHIX0014000.
HGNCHGNC:11983. TOM1L1.
HPAHPA022916.
MIM604701. gene.
neXtProtNX_O75674.
PharmGKBPA36667.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321220.
HOGENOMHOG000285970.
HOVERGENHBG025068.
InParanoidO75674.
OMAVTTEAIY.
OrthoDBEOG75B859.
PhylomeDBO75674.
TreeFamTF314105.

Gene expression databases

ArrayExpressO75674.
BgeeO75674.
CleanExHS_TOM1L1.
GenevestigatorO75674.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
InterProIPR008942. ENTH_VHS.
IPR004152. GAT.
IPR014645. TOM1.
IPR027428. TOM1L1.
IPR002014. VHS.
IPR018205. VHS_subgr.
[Graphical view]
PANTHERPTHR13856:SF28. PTHR13856:SF28. 1 hit.
PfamPF03127. GAT. 1 hit.
PF00790. VHS. 1 hit.
[Graphical view]
PIRSFPIRSF036948. TOM1. 1 hit.
SMARTSM00288. VHS. 1 hit.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS50909. GAT. 1 hit.
PS50179. VHS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTOM1L1. human.
GeneWikiTOM1L1.
GenomeRNAi10040.
NextBio37921.
PROO75674.
SOURCESearch...

Entry information

Entry nameTM1L1_HUMAN
AccessionPrimary (citable) accession number: O75674
Secondary accession number(s): Q53G06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 112 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 17

Human chromosome 17: entries, gene names and cross-references to MIM