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Protein

SAM and SH3 domain-containing protein 1

Gene

SASH1

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

Functioni

May have a role in a signaling pathway. Could act as a tumor suppressor.

GO - Molecular functioni

  • mitogen-activated protein kinase kinase kinase binding Source: MGI
  • protein complex scaffold Source: MGI
  • protein C-terminus binding Source: MGI
  • protein kinase binding Source: MGI

GO - Biological processi

  • positive regulation of angiogenesis Source: MGI
  • positive regulation of endothelial cell migration Source: MGI
  • positive regulation of JUN kinase activity Source: MGI
  • positive regulation of lipopolysaccharide-mediated signaling pathway Source: MGI
  • positive regulation of NIK/NF-kappaB signaling Source: MGI
  • positive regulation of p38MAPK cascade Source: MGI
  • protein polyubiquitination Source: MGI
  • regulation of protein autoubiquitination Source: MGI
  • regulation of protein K63-linked ubiquitination Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SAM and SH3 domain-containing protein 1
Alternative name(s):
Proline-glutamate repeat-containing protein
Gene namesi
Name:SASH1
Synonyms:KIAA0790, PEPE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:19182. SASH1.

Subcellular locationi

GO - Cellular componenti

  • protein complex Source: MGI
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134984521.

Polymorphism and mutation databases

BioMutaiSASH1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12471247SAM and SH3 domain-containing protein 1PRO_0000097597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei248 – 2481PhosphoserineBy similarity
Modified residuei407 – 4071PhosphoserineCombined sources
Modified residuei614 – 6141PhosphoserineCombined sources
Modified residuei821 – 8211PhosphoserineBy similarity
Modified residuei839 – 8391PhosphoserineBy similarity
Modified residuei858 – 8581PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO94885.
MaxQBiO94885.
PaxDbiO94885.
PeptideAtlasiO94885.
PRIDEiO94885.

PTM databases

iPTMnetiO94885.
PhosphoSiteiO94885.

Expressioni

Tissue specificityi

Expressed ubiquitously, with highest levels in lung, placenta, spleen and thymus. Down-regulated in the majority (74%) of breast tumors in comparison with corresponding normal breast epithelial tissues.1 Publication

Gene expression databases

BgeeiO94885.
CleanExiHS_SASH1.
ExpressionAtlasiO94885. baseline and differential.
GenevisibleiO94885. HS.

Organism-specific databases

HPAiHPA029947.
HPA029949.

Interactioni

GO - Molecular functioni

  • mitogen-activated protein kinase kinase kinase binding Source: MGI
  • protein complex scaffold Source: MGI
  • protein C-terminus binding Source: MGI
  • protein kinase binding Source: MGI

Protein-protein interaction databases

BioGridi116916. 12 interactions.
IntActiO94885. 7 interactions.
MINTiMINT-1195945.
STRINGi9606.ENSP00000356437.

Structurei

Secondary structure

1
1247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi556 – 5616Combined sources
Beta strandi582 – 5876Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi594 – 5974Combined sources
Beta strandi602 – 6054Combined sources
Beta strandi610 – 6123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DL0NMR-A1164-1247[»]
2EBPNMR-A555-614[»]
ProteinModelPortaliO94885.
SMRiO94885. Positions 555-614, 1166-1247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94885.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini557 – 61458SH3Add
BLAST
Domaini633 – 69765SAM 1PROSITE-ProRule annotationAdd
BLAST
Domaini1177 – 124165SAM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 3325Pro-richAdd
BLAST
Compositional biasi978 – 105982Pro-richAdd
BLAST

Sequence similaritiesi

Contains 2 SAM (sterile alpha motif) domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiENOG410INAU. Eukaryota.
ENOG410ZDYS. LUCA.
GeneTreeiENSGT00390000014672.
HOGENOMiHOG000139718.
HOVERGENiHBG058816.
InParanoidiO94885.
OMAiCETLEGP.
OrthoDBiEOG7KQ20X.
PhylomeDBiO94885.
TreeFamiTF350709.

Family and domain databases

Gene3Di1.10.150.50. 2 hits.
InterProiIPR021090. rSAM/SH3_domain-containing.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00536. SAM_1. 1 hit.
PF07647. SAM_2. 1 hit.
PF07653. SH3_2. 1 hit.
PF12485. SLY. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 2 hits.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94885-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDAGAAGPG PEPEPEPEPE PEPAPEPEPE PKPGAGTSEA FSRLWTDVMG
60 70 80 90 100
ILDGSLGNID DLAQQYADYY NTCFSDVCER MEELRKRRVS QDLEVEKPDA
110 120 130 140 150
SPTSLQLRSQ IEESLGFCSA VSTPEVERKN PLHKSNSEDS SVGKGDWKKK
160 170 180 190 200
NKYFWQNFRK NQKGIMRQTS KGEDVGYVAS EITMSDEERI QLMMMVKEKM
210 220 230 240 250
ITIEEALARL KEYEAQHRQS AALDPADWPD GSYPTFDGSS NCNSREQSDD
260 270 280 290 300
ETEESVKFKR LHKLVNSTRR VRKKLIRVEE MKKPSTEGGE EHVFENSPVL
310 320 330 340 350
DERSALYSGV HKKPLFFDGS PEKPPEDDSD SLTTSPSSSS LDTWGAGRKL
360 370 380 390 400
VKTFSKGESR GLIKPPKKMG TFFSYPEEEK AQKVSRSLTE GEMKKGLGSL
410 420 430 440 450
SHGRTCSFGG FDLTNRSLHV GSNNSDPMGK EGDFVYKEVI KSPTASRISL
460 470 480 490 500
GKKVKSVKET MRKRMSKKYS SSVSEQDSGL DGMPGSPPPS QPDPEHLDKP
510 520 530 540 550
KLKAGGSVES LRSSLSGQSS MSGQTVSTTD SSTSNRESVK SEDGDDEEPP
560 570 580 590 600
YRGPFCGRAR VHTDFTPSPY DTDSLKLKKG DIIDIISKPP MGTWMGLLNN
610 620 630 640 650
KVGTFKFIYV DVLSEDEEKP KRPTRRRRKG RPPQPKSVED LLDRINLKEH
660 670 680 690 700
MPTFLFNGYE DLDTFKLLEE EDLDELNIRD PEHRAVLLTA VELLQEYDSN
710 720 730 740 750
SDQSGSQEKL LVDSQGLSGC SPRDSGCYES SENLENGKTR KASLLSAKSS
760 770 780 790 800
TEPSLKSFSR NQLGNYPTLP LMKSGDALKQ GQEEGRLGGG LAPDTSKSCD
810 820 830 840 850
PPGVTGLNKN RRSLPVSICR SCETLEGPQT VDTWPRSHSL DDLQVEPGAE
860 870 880 890 900
QDVPTEVTEP PPQIVPEVPQ KTTASSTKAQ PLEQDSAVDN ALLLTQSKRF
910 920 930 940 950
SEPQKLTTKK LEGSIAASGR GLSPPQCLPR NYDAQPPGAK HGLARTPLEG
960 970 980 990 1000
HRKGHEFEGT HHPLGTKEGV DAEQRMQPKI PSQPPPVPAK KSRERLANGL
1010 1020 1030 1040 1050
HPVPMGPSGA LPSPDAPCLP VKRGSPASPT SPSDCPPALA PRPLSGQAPG
1060 1070 1080 1090 1100
SPPSTRPPPW LSELPENTSL QEHGVKLGPA LTRKVSCARG VDLETLTENK
1110 1120 1130 1140 1150
LHAEGIDLTE EPYSDKHGRC GIPEALVQRY AEDLDQPERD VAANMDQIRV
1160 1170 1180 1190 1200
KQLRKQHRMA IPSGGLTEIC RKPVSPGCIS SVSDWLISIG LPMYAGTLST
1210 1220 1230 1240
AGFSTLSQVP SLSHTCLQEA GITEERHIRK LLSAARLFKL PPGPEAM
Length:1,247
Mass (Da):136,653
Last modified:April 17, 2007 - v3
Checksum:i48A806B3AE32E563
GO

Sequence cautioni

The sequence BAA34510.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB14909.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti751 – 7511T → A in BAB14909 (PubMed:14702039).Curated
Sequence conflicti1157 – 11571H → R in BAB14909 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti298 – 2981P → Q.
Corresponds to variant rs35078400 [ dbSNP | Ensembl ].
VAR_031714
Natural varianti884 – 8841Q → R.3 Publications
Corresponds to variant rs208696 [ dbSNP | Ensembl ].
VAR_031715

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ507735 mRNA. Translation: CAD47811.1.
BN000088 mRNA. Translation: CAD92036.1.
AY351979
, AY351960, AY351961, AY351962, AY351963, AY351964, AY351965, AY351966, AY351967, AY351968, AY351969, AY351970, AY351971, AY351972, AY351973, AY351974, AY351975, AY351976, AY351977, AY351978 Genomic DNA. Translation: AAQ55463.1.
AB018333 mRNA. Translation: BAA34510.1. Different initiation.
AL513164, AL033378 Genomic DNA. Translation: CAH73449.1.
AL033378, AL513164 Genomic DNA. Translation: CAI20166.1.
AK024403 mRNA. Translation: BAB14909.1. Different initiation.
CH471051 Genomic DNA. Translation: EAW47815.1.
BC028303 mRNA. Translation: AAH28303.1.
CCDSiCCDS5212.1.
RefSeqiNP_056093.3. NM_015278.3.
UniGeneiHs.193133.

Genome annotation databases

EnsembliENST00000367467; ENSP00000356437; ENSG00000111961.
GeneIDi23328.
KEGGihsa:23328.
UCSCiuc003qme.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ507735 mRNA. Translation: CAD47811.1.
BN000088 mRNA. Translation: CAD92036.1.
AY351979
, AY351960, AY351961, AY351962, AY351963, AY351964, AY351965, AY351966, AY351967, AY351968, AY351969, AY351970, AY351971, AY351972, AY351973, AY351974, AY351975, AY351976, AY351977, AY351978 Genomic DNA. Translation: AAQ55463.1.
AB018333 mRNA. Translation: BAA34510.1. Different initiation.
AL513164, AL033378 Genomic DNA. Translation: CAH73449.1.
AL033378, AL513164 Genomic DNA. Translation: CAI20166.1.
AK024403 mRNA. Translation: BAB14909.1. Different initiation.
CH471051 Genomic DNA. Translation: EAW47815.1.
BC028303 mRNA. Translation: AAH28303.1.
CCDSiCCDS5212.1.
RefSeqiNP_056093.3. NM_015278.3.
UniGeneiHs.193133.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DL0NMR-A1164-1247[»]
2EBPNMR-A555-614[»]
ProteinModelPortaliO94885.
SMRiO94885. Positions 555-614, 1166-1247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116916. 12 interactions.
IntActiO94885. 7 interactions.
MINTiMINT-1195945.
STRINGi9606.ENSP00000356437.

PTM databases

iPTMnetiO94885.
PhosphoSiteiO94885.

Polymorphism and mutation databases

BioMutaiSASH1.

Proteomic databases

EPDiO94885.
MaxQBiO94885.
PaxDbiO94885.
PeptideAtlasiO94885.
PRIDEiO94885.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367467; ENSP00000356437; ENSG00000111961.
GeneIDi23328.
KEGGihsa:23328.
UCSCiuc003qme.2. human.

Organism-specific databases

CTDi23328.
GeneCardsiSASH1.
H-InvDBHIX0006282.
HGNCiHGNC:19182. SASH1.
HPAiHPA029947.
HPA029949.
MIMi607955. gene.
neXtProtiNX_O94885.
PharmGKBiPA134984521.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INAU. Eukaryota.
ENOG410ZDYS. LUCA.
GeneTreeiENSGT00390000014672.
HOGENOMiHOG000139718.
HOVERGENiHBG058816.
InParanoidiO94885.
OMAiCETLEGP.
OrthoDBiEOG7KQ20X.
PhylomeDBiO94885.
TreeFamiTF350709.

Miscellaneous databases

ChiTaRSiSASH1. human.
EvolutionaryTraceiO94885.
GeneWikiiSASH1.
GenomeRNAii23328.
PROiO94885.
SOURCEiSearch...

Gene expression databases

BgeeiO94885.
CleanExiHS_SASH1.
ExpressionAtlasiO94885. baseline and differential.
GenevisibleiO94885. HS.

Family and domain databases

Gene3Di1.10.150.50. 2 hits.
InterProiIPR021090. rSAM/SH3_domain-containing.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00536. SAM_1. 1 hit.
PF07647. SAM_2. 1 hit.
PF07653. SH3_2. 1 hit.
PF12485. SLY. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 2 hits.
SSF50044. SSF50044. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SASH1 - a candidate tumour suppressor gene on chromosome 6q24.3 is downregulated in breast cancer."
    Zeller C., Hinzmann B., Seitz S., Prokoph H., Burkhardt-Goettges E., Fischer J., Jandrig B., Estevez-Schwarz L., Rosenthal A., Scherneck S.
    Oncogene 22:2972-2983(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ARG-884.
  2. "PEPE1 is a candidate tumor suppressor gene on chromosome 6q24.3 involved in melanoma and ovarian cancer."
    Rice A.J., Shpak M., Fountain J.W., Dubeau L.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ARG-884.
  3. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-884.
    Tissue: Brain.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 181-1247.
    Tissue: Thyroid.
  7. "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] OF 1006-1247.
    Tissue: Placenta.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-614 AND THR-858, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Solution structure of the SH3 and SAM-domains from human SAM and SH3 domain-containing protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 555-614 AND 1164-1247.

Entry informationi

Entry nameiSASH1_HUMAN
AccessioniPrimary (citable) accession number: O94885
Secondary accession number(s): Q5TGN5, Q8TAI0, Q9H7R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: April 17, 2007
Last modified: July 6, 2016
This is version 138 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 6
    Human chromosome 6: 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

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.