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Protein

SAM and SH3 domain-containing protein 3

Gene

SASH3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May function as a signaling adapter protein in lymphocytes.By similarity

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SAM and SH3 domain-containing protein 3
Alternative name(s):
SH3 protein expressed in lymphocytes homolog
Gene namesi
Name:SASH3
Synonyms:CXorf9, SLY
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:15975. SASH3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162402388.

Polymorphism and mutation databases

BioMutaiSASH3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380SAM and SH3 domain-containing protein 3PRO_0000071962Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Phosphoserine1 Publication
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei42 – 421PhosphoserineCombined sources
Modified residuei61 – 611PhosphothreonineCombined sources
Modified residuei97 – 971PhosphoserineCombined sources
Modified residuei103 – 1031PhosphothreonineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei112 – 1121PhosphothreonineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei116 – 1161PhosphotyrosineCombined sources
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei318 – 3181PhosphothreonineCombined sources
Modified residuei320 – 3201PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO75995.
MaxQBiO75995.
PaxDbiO75995.
PRIDEiO75995.

PTM databases

iPTMnetiO75995.
PhosphoSiteiO75995.

Expressioni

Gene expression databases

BgeeiO75995.
CleanExiHS_SASH3.
GenevisibleiO75995. HS.

Organism-specific databases

HPAiHPA001085.

Interactioni

Protein-protein interaction databases

BioGridi119956. 1 interaction.
IntActiO75995. 1 interaction.
STRINGi9606.ENSP00000349359.

Structurei

3D structure databases

ProteinModelPortaliO75995.
SMRiO75995. Positions 174-232, 247-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini176 – 23257SH3Add
BLAST
Domaini252 – 31665SAMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.Curated

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiENOG410INAS. Eukaryota.
ENOG410YC4U. LUCA.
GeneTreeiENSGT00390000014672.
HOGENOMiHOG000049202.
HOVERGENiHBG000461.
InParanoidiO75995.
OMAiEMGDTLE.
OrthoDBiEOG7KQ20X.
PhylomeDBiO75995.
TreeFamiTF350709.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR021090. rSAM/SH3_domain-containing.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF07647. SAM_2. 1 hit.
PF07653. SH3_2. 1 hit.
PF12485. SLY. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75995-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRRKPSNAS EKEPTQKKKL SLQRSSSFKD FAKSKPSSPV VSEKEFNLDD
60 70 80 90 100
NIPEDDSGVP TPEDAGKSGK KLGKKWRAVI SRTMNRKMGK MMVKALSEEM
110 120 130 140 150
ADTLEEGSAS PTSPDYSLDS PGPEKMALAF SEQEEHELPV LSRQASTGSE
160 170 180 190 200
LCSPSPGSGS FGEEPPAPQY TGPFCGRARV HTDFTPSPYD HDSLKLQKGD
210 220 230 240 250
VIQIIEKPPV GTWLGLLNGK VGSFKFIYVD VLPEEAVGHA RPSRRQSKGK
260 270 280 290 300
RPKPKTLHEL LERIGLEEHT STLLLNGYQT LEDFKELRET HLNELNIMDP
310 320 330 340 350
QHRAKLLTAA ELLLDYDTGS EEAEEGAESS QEPVAHTVSE PKVDIPRDSG
360 370 380
CFEGSESGRD DAELAGTEEQ LQGLSLAGAP
Length:380
Mass (Da):41,595
Last modified:May 1, 1999 - v2
Checksum:i6DF3FB7D44797DB3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791V → A in BAF84712 (PubMed:14702039).Curated
Sequence conflicti365 – 3651A → V in BAF84712 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049683 mRNA. Translation: CAB41255.1.
AK292023 mRNA. Translation: BAF84712.1.
AL023653 Genomic DNA. Translation: CAA19221.2.
CH471107 Genomic DNA. Translation: EAX11826.1.
BC051881 mRNA. Translation: AAH51881.1.
CCDSiCCDS14614.1.
RefSeqiNP_061863.1. NM_018990.3.
UniGeneiHs.61469.

Genome annotation databases

EnsembliENST00000356892; ENSP00000349359; ENSG00000122122.
GeneIDi54440.
KEGGihsa:54440.
UCSCiuc004euu.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049683 mRNA. Translation: CAB41255.1.
AK292023 mRNA. Translation: BAF84712.1.
AL023653 Genomic DNA. Translation: CAA19221.2.
CH471107 Genomic DNA. Translation: EAX11826.1.
BC051881 mRNA. Translation: AAH51881.1.
CCDSiCCDS14614.1.
RefSeqiNP_061863.1. NM_018990.3.
UniGeneiHs.61469.

3D structure databases

ProteinModelPortaliO75995.
SMRiO75995. Positions 174-232, 247-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119956. 1 interaction.
IntActiO75995. 1 interaction.
STRINGi9606.ENSP00000349359.

PTM databases

iPTMnetiO75995.
PhosphoSiteiO75995.

Polymorphism and mutation databases

BioMutaiSASH3.

Proteomic databases

EPDiO75995.
MaxQBiO75995.
PaxDbiO75995.
PRIDEiO75995.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356892; ENSP00000349359; ENSG00000122122.
GeneIDi54440.
KEGGihsa:54440.
UCSCiuc004euu.4. human.

Organism-specific databases

CTDi54440.
GeneCardsiSASH3.
HGNCiHGNC:15975. SASH3.
HPAiHPA001085.
MIMi300441. gene.
neXtProtiNX_O75995.
PharmGKBiPA162402388.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INAS. Eukaryota.
ENOG410YC4U. LUCA.
GeneTreeiENSGT00390000014672.
HOGENOMiHOG000049202.
HOVERGENiHBG000461.
InParanoidiO75995.
OMAiEMGDTLE.
OrthoDBiEOG7KQ20X.
PhylomeDBiO75995.
TreeFamiTF350709.

Miscellaneous databases

ChiTaRSiSASH3. human.
GenomeRNAii54440.
NextBioi56664.
PROiO75995.
SOURCEiSearch...

Gene expression databases

BgeeiO75995.
CleanExiHS_SASH3.
GenevisibleiO75995. HS.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR021090. rSAM/SH3_domain-containing.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF07647. SAM_2. 1 hit.
PF07653. SH3_2. 1 hit.
PF12485. SLY. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Rhodes S.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    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.
    , 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: Spleen.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Testis.
  6. "Approaches to define antigen receptor-induced serine kinase signal transduction pathways."
    Astoul E., Laurence A.D., Totty N., Beer S., Alexander D.R., Cantrell D.A.
    J. Biol. Chem. 278:9267-9275(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-27.
  7. "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-34; SER-42; THR-61; SER-97; THR-103; SER-110; THR-112; SER-113; TYR-116; SER-120; THR-318 AND SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSASH3_HUMAN
AccessioniPrimary (citable) accession number: O75995
Secondary accession number(s): A6NCH1, A8K7K8, Q5JZ38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: May 1, 1999
Last modified: March 16, 2016
This is version 118 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.