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Q13239

- SLAP1_HUMAN

UniProt

Q13239 - SLAP1_HUMAN

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Protein

Src-like-adapter

Gene

SLA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. Involved in the negative regulation of positive selection and mitosis of T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins.2 Publications

GO - Molecular functioni

  1. SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

  1. positive regulation of signal transduction Source: GOC
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ13239.

Names & Taxonomyi

Protein namesi
Recommended name:
Src-like-adapter
Alternative name(s):
Src-like-adapter protein 1
Short name:
SLAP-1
Short name:
hSLAP
Gene namesi
Name:SLA
Synonyms:SLAP, SLAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:10902. SLA.

Subcellular locationi

Cytoplasm By similarity. Endosome By similarity
Note: Colocalizes with endosomes.By similarity

GO - Cellular componenti

  1. endosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi111 – 1111R → K: Strongly reduces interaction with ZAP70, CD3Z, SYK and LAT. 1 Publication
Mutagenesisi218 – 2181L → S: Abolishes interaction with CBL. Does not affect dimerization; when associated with S-224 and S-229. 1 Publication
Mutagenesisi224 – 2241L → S: Abolishes interaction with CBL. Does not affect dimerization; when associated with S-218 and S-229. 1 Publication
Mutagenesisi229 – 2291L → S: Abolishes interaction with CBL. Does not affect dimerization; when associated with S-218 and S-224. 1 Publication
Mutagenesisi237 – 2393LSL → QSQ: Abolishes interaction with CBL. Slightly affects dimerization. 1 Publication

Organism-specific databases

PharmGKBiPA35802.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 276275Src-like-adapterPRO_0000071946Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei273 – 2731PhosphotyrosineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ13239.
PaxDbiQ13239.
PRIDEiQ13239.

PTM databases

PhosphoSiteiQ13239.

Expressioni

Tissue specificityi

Expressed in lung and fetal brain. Weakly expressed in heart, adult brain, placenta, liver, skeletal muscle, kidney and pancreas.1 Publication

Inductioni

By all-trans retinoic acid (ATRA). Induction is indirect and is mediated through other proteins.1 Publication

Gene expression databases

BgeeiQ13239.
CleanExiHS_SLA.
ExpressionAtlasiQ13239. baseline and differential.
GenevestigatoriQ13239.

Organism-specific databases

HPAiHPA012296.

Interactioni

Subunit structurei

Interacts with EPHA2, VAV1, LCP2 and PDGFRB (By similarity). Homodimer. Homodimerization and interaction with phosphorylated CBL occurs via its C-terminal domain. Interacts with phosphorylated proteins ZAP70, CD3Z, SYK and LAT via its SH2 domain.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005332EBI-726214,EBI-297353
PDGFRBP096194EBI-726214,EBI-641237

Protein-protein interaction databases

BioGridi112394. 15 interactions.
IntActiQ13239. 6 interactions.
MINTiMINT-1404565.
STRINGi9606.ENSP00000394049.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 223Combined sources
Beta strandi26 – 316Combined sources
Turni36 – 383Combined sources
Beta strandi48 – 558Combined sources
Beta strandi58 – 636Combined sources
Turni64 – 663Combined sources
Beta strandi69 – 735Combined sources
Helixi74 – 763Combined sources
Beta strandi77 – 804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CUDNMR-A15-80[»]
ProteinModelPortaliQ13239.
SMRiQ13239. Positions 13-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13239.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 8261SH3PROSITE-ProRule annotationAdd
BLAST
Domaini84 – 17592SH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni212 – 27665SLA C-terminalAdd
BLAST

Domaini

The C-terminal domain is essential for the homodimerization and the interaction with CBL. While the interaction with CBL is apparently mediated via the hydrophobic region of this domain, the highly charged region is apparently required for the homodimerization.

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG151065.
GeneTreeiENSGT00390000001681.
HOGENOMiHOG000234240.
HOVERGENiHBG054908.
InParanoidiQ13239.
OrthoDBiEOG7DVDBX.
PhylomeDBiQ13239.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13239-1) [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
MGNSMKSTPA PAERPLPNPE GLDSDFLAVL SDYPSPDISP PIFRRGEKLR
60 70 80 90 100
VISDEGGWWK AISLSTGRES YIPGICVARV YHGWLFEGLG RDKAEELLQL
110 120 130 140 150
PDTKVGSFMI RESETKKGFY SLSVRHRQVK HYRIFRLPNN WYYISPRLTF
160 170 180 190 200
QCLEDLVNHY SEVADGLCCV LTTPCLTQST AAPAVRASSS PVTLRQKTVD
210 220 230 240 250
WRRVSRLQED PEGTENPLGV DESLFSYGLR ESIASYLSLT SEDNTSFDRK
260 270
KKSISLMYGG SKRKSSFFSS PPYFED
Length:276
Mass (Da):31,156
Last modified:January 23, 2007 - v3
Checksum:iB0FCC7D7B2ECA378
GO
Isoform 2 (identifier: Q13239-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Note: No experimental confirmation available.

Show »
Length:168
Mass (Da):19,285
Checksum:i0BC12A843F32869D
GO
Isoform 3 (identifier: Q13239-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLHRLWASPAAPGKKKEM

Note: No experimental confirmation available.

Show »
Length:293
Mass (Da):33,059
Checksum:i6721FE5A9562C6DC
GO
Isoform 4 (identifier: Q13239-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLHRLWASPAAPGKKKEM
     118-161: Missing.

Note: No experimental confirmation available.

Show »
Length:249
Mass (Da):27,558
Checksum:iD072FF483DAA2778
GO
Isoform 5 (identifier: Q13239-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSKLGHSPLGGLRARLTFPVCLLYHRLWASPAAPGKKKEM

Note: No experimental confirmation available.

Show »
Length:316
Mass (Da):35,540
Checksum:i93C3155474168A96
GO

Sequence cautioni

The sequence AAH07042.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG35478.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711Y → D in CAB53536. (PubMed:11179692)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151P → T.
Corresponds to variant rs4486183 [ dbSNP | Ensembl ].
VAR_061706

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 108108Missing in isoform 2. 1 PublicationVSP_055122Add
BLAST
Alternative sequencei1 – 11M → MLHRLWASPAAPGKKKEM in isoform 3 and isoform 4. 1 PublicationVSP_055123
Alternative sequencei1 – 11M → MLSKLGHSPLGGLRARLTFP VCLLYHRLWASPAAPGKKKE M in isoform 5. 1 PublicationVSP_055124
Alternative sequencei118 – 16144Missing in isoform 4. 1 PublicationVSP_055125Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30473 mRNA. Translation: AAC50357.1.
D89077 mRNA. Translation: BAA13758.1.
U44403 mRNA. Translation: AAC27662.1.
CR536537 mRNA. Translation: CAG38774.1.
AK297423 mRNA. Translation: BAH12578.1.
AK297519 mRNA. Translation: BAH12602.1.
AK312584 mRNA. Translation: BAG35478.1. Different initiation.
AF235100 Genomic DNA. No translation available.
AF305872 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW92159.1.
BC007042 mRNA. Translation: AAH07042.1. Different initiation.
AJ238591 mRNA. Translation: CAB53536.1.
CCDSiCCDS47922.1. [Q13239-3]
CCDS47923.1. [Q13239-5]
CCDS6370.1. [Q13239-1]
CCDS64977.1. [Q13239-2]
CCDS64978.1. [Q13239-4]
RefSeqiNP_001039021.1. NM_001045556.2. [Q13239-1]
NP_001039022.2. NM_001045557.2. [Q13239-3]
NP_001269893.1. NM_001282964.1. [Q13239-4]
NP_001269894.1. NM_001282965.1. [Q13239-2]
NP_006739.2. NM_006748.3. [Q13239-5]
UniGeneiHs.75367.

Genome annotation databases

EnsembliENST00000338087; ENSP00000337548; ENSG00000155926. [Q13239-1]
ENST00000395352; ENSP00000378759; ENSG00000155926. [Q13239-3]
ENST00000427060; ENSP00000394049; ENSG00000155926. [Q13239-5]
ENST00000517648; ENSP00000428559; ENSG00000155926. [Q13239-4]
ENST00000524345; ENSP00000427928; ENSG00000155926. [Q13239-2]
GeneIDi6503.
KEGGihsa:6503.
UCSCiuc003ytz.3. human. [Q13239-1]
uc011ljg.2. human.

Polymorphism databases

DMDMi30173237.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30473 mRNA. Translation: AAC50357.1 .
D89077 mRNA. Translation: BAA13758.1 .
U44403 mRNA. Translation: AAC27662.1 .
CR536537 mRNA. Translation: CAG38774.1 .
AK297423 mRNA. Translation: BAH12578.1 .
AK297519 mRNA. Translation: BAH12602.1 .
AK312584 mRNA. Translation: BAG35478.1 . Different initiation.
AF235100 Genomic DNA. No translation available.
AF305872 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW92159.1 .
BC007042 mRNA. Translation: AAH07042.1 . Different initiation.
AJ238591 mRNA. Translation: CAB53536.1 .
CCDSi CCDS47922.1. [Q13239-3 ]
CCDS47923.1. [Q13239-5 ]
CCDS6370.1. [Q13239-1 ]
CCDS64977.1. [Q13239-2 ]
CCDS64978.1. [Q13239-4 ]
RefSeqi NP_001039021.1. NM_001045556.2. [Q13239-1 ]
NP_001039022.2. NM_001045557.2. [Q13239-3 ]
NP_001269893.1. NM_001282964.1. [Q13239-4 ]
NP_001269894.1. NM_001282965.1. [Q13239-2 ]
NP_006739.2. NM_006748.3. [Q13239-5 ]
UniGenei Hs.75367.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CUD NMR - A 15-80 [» ]
ProteinModelPortali Q13239.
SMRi Q13239. Positions 13-177.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112394. 15 interactions.
IntActi Q13239. 6 interactions.
MINTi MINT-1404565.
STRINGi 9606.ENSP00000394049.

PTM databases

PhosphoSitei Q13239.

Polymorphism databases

DMDMi 30173237.

Proteomic databases

MaxQBi Q13239.
PaxDbi Q13239.
PRIDEi Q13239.

Protocols and materials databases

DNASUi 6503.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338087 ; ENSP00000337548 ; ENSG00000155926 . [Q13239-1 ]
ENST00000395352 ; ENSP00000378759 ; ENSG00000155926 . [Q13239-3 ]
ENST00000427060 ; ENSP00000394049 ; ENSG00000155926 . [Q13239-5 ]
ENST00000517648 ; ENSP00000428559 ; ENSG00000155926 . [Q13239-4 ]
ENST00000524345 ; ENSP00000427928 ; ENSG00000155926 . [Q13239-2 ]
GeneIDi 6503.
KEGGi hsa:6503.
UCSCi uc003ytz.3. human. [Q13239-1 ]
uc011ljg.2. human.

Organism-specific databases

CTDi 6503.
GeneCardsi GC08M134048.
HGNCi HGNC:10902. SLA.
HPAi HPA012296.
MIMi 601099. gene.
neXtProti NX_Q13239.
PharmGKBi PA35802.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG151065.
GeneTreei ENSGT00390000001681.
HOGENOMi HOG000234240.
HOVERGENi HBG054908.
InParanoidi Q13239.
OrthoDBi EOG7DVDBX.
PhylomeDBi Q13239.

Enzyme and pathway databases

SignaLinki Q13239.

Miscellaneous databases

EvolutionaryTracei Q13239.
GenomeRNAii 6503.
NextBioi 25281.
PROi Q13239.
SOURCEi Search...

Gene expression databases

Bgeei Q13239.
CleanExi HS_SLA.
ExpressionAtlasi Q13239. baseline and differential.
Genevestigatori Q13239.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Chromosomal localization of the mouse Src-like adapter protein (Slap) gene and its putative human homolog SLA."
    Angrist M., Wells D.E., Chakravarti A., Pandey A.
    Genomics 30:623-625(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Expression of Src-like adapter protein mRNA is induced by all-trans retinoic acid."
    Ohtsuki T., Hatake K., Ikeda M., Tomizuka H., Terui Y., Uwai M., Miura Y.
    Biochem. Biophys. Res. Commun. 230:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION BY ATRA.
    Tissue: Histiocytic lymphoma.
  3. "The gene for the human Src-like adaptor protein (hSLAP) is located within the 64-kb intron of the thyroglobulin gene."
    Meijerink P.H.S., Yanakiev P., Zorn I., Grierson A.J., Bikker H., Dye D., Kalaydjieva L., Baas F.
    Eur. J. Biochem. 254:297-303(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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.
    , 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] (ISOFORMS 2; 3 AND 4).
    Tissue: Brain.
  7. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 5).
    Tissue: Bone marrow.
  10. "Characterization of promoter region and genomic structure of the murine and human genes encoding Src like adapter protein."
    Kratchmarova I., Sosinowski T., Weiss A., Witter K., Vincenz C., Pandey A.
    Gene 262:267-273(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-72.
  11. "SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling."
    Tang J., Sawasdikosol S., Chang J.-H., Burakoff S.J.
    Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, PHOSPHORYLATION, INTERACTION WITH CBL; ZAP70; CD3Z; SYK AND LAT, MUTAGENESIS OF ARG-111; LEU-218; LEU-224; LEU-229 AND 237-LEU--LEU-239.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Solution structure of the SH3 domain of the human Src-like adapter protein (SLAP)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 15-80.

Entry informationi

Entry nameiSLAP1_HUMAN
AccessioniPrimary (citable) accession number: Q13239
Secondary accession number(s): B7Z4J2
, B7Z4L6, Q6FI01, Q9UMQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 132 of the entry and version 3 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 8
    Human chromosome 8: 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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