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Protein

Serine-threonine kinase receptor-associated protein

Gene

STRAP

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

Functioni

The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein.2 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • maintenance of gastrointestinal epithelium Source: UniProtKB
  • negative regulation of epithelial cell migration Source: UniProtKB
  • negative regulation of epithelial cell proliferation Source: UniProtKB
  • negative regulation of epithelial to mesenchymal transition Source: UniProtKB
  • negative regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • spliceosomal snRNP assembly Source: UniProtKB
  • transforming growth factor beta receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-HSA-2173788. Downregulation of TGF-beta receptor signaling.
SignaLinkiQ9Y3F4.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine-threonine kinase receptor-associated protein
Alternative name(s):
MAP activator with WD repeats
UNR-interacting protein
WD-40 repeat protein PT-WD
Gene namesi
Name:STRAP
Synonyms:MAWD, UNRIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:30796. STRAP.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Localized predominantly in the cytoplasm but also found in the nucleus.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • SMN complex Source: UniProtKB
  • SMN-Sm protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134867032.

Polymorphism and mutation databases

BioMutaiSTRAP.
DMDMi12643951.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Serine-threonine kinase receptor-associated proteinPRO_0000051230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei335 – 3351PhosphoserineCombined sources
Modified residuei338 – 3381PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y3F4.
MaxQBiQ9Y3F4.
PaxDbiQ9Y3F4.
PeptideAtlasiQ9Y3F4.
PRIDEiQ9Y3F4.
TopDownProteomicsiQ9Y3F4-1. [Q9Y3F4-1]

2D gel databases

OGPiQ9Y3F4.

PTM databases

iPTMnetiQ9Y3F4.
PhosphoSiteiQ9Y3F4.
SwissPalmiQ9Y3F4.

Expressioni

Gene expression databases

BgeeiQ9Y3F4.
CleanExiHS_STRAP.
ExpressionAtlasiQ9Y3F4. baseline and differential.
GenevisibleiQ9Y3F4. HS.

Organism-specific databases

HPAiHPA027320.
HPA055557.

Interactioni

Subunit structurei

Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN6 and GEMIN7. Associates with the SMN complex in the cytoplasm but not in the nucleus. Also interacts with CSDE1/UNR and MAWBP. Interacts with PDPK1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NME1P155319EBI-727414,EBI-741141

Protein-protein interaction databases

BioGridi116342. 85 interactions.
IntActiQ9Y3F4. 30 interactions.
MINTiMINT-1346033.
STRINGi9606.ENSP00000392270.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3F4.
SMRiQ9Y3F4. Positions 9-301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati12 – 5645WD 1Add
BLAST
Repeati57 – 9640WD 2Add
BLAST
Repeati98 – 13740WD 3Add
BLAST
Repeati141 – 17939WD 4Add
BLAST
Repeati180 – 21233WD 5Add
BLAST
Repeati221 – 26242WD 6Add
BLAST
Repeati263 – 30240WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat STRAP family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0278. Eukaryota.
ENOG410XPJ4. LUCA.
GeneTreeiENSGT00630000089849.
HOGENOMiHOG000174258.
HOVERGENiHBG055228.
InParanoidiQ9Y3F4.
KOiK13137.
OMAiHGPIWSI.
PhylomeDBiQ9Y3F4.
TreeFamiTF323287.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y3F4-1) [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
MAMRQTPLTC SGHTRPVVDL AFSGITPYGY FLISACKDGK PMLRQGDTGD
60 70 80 90 100
WIGTFLGHKG AVWGATLNKD ATKAATAAAD FTAKVWDAVS GDELMTLAHK
110 120 130 140 150
HIVKTVDFTQ DSNYLLTGGQ DKLLRIYDLN KPEAEPKEIS GHTSGIKKAL
160 170 180 190 200
WCSEDKQILS ADDKTVRLWD HATMTEVKSL NFNMSVSSME YIPEGEILVI
210 220 230 240 250
TYGRSIAFHS AVSLDPIKSF EAPATINSAS LHPEKEFLVA GGEDFKLYKY
260 270 280 290 300
DYNSGEELES YKGHFGPIHC VRFSPDGELY ASGSEDGTLR LWQTVVGKTY
310 320 330 340 350
GLWKCVLPEE DSGELAKPKI GFPETTEEEL EEIASENSDC IFPSAPDVKA
Length:350
Mass (Da):38,438
Last modified:November 1, 1999 - v1
Checksum:iCFCB34D3946290E2
GO
Isoform 2 (identifier: Q9Y3F4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-37: K → KGAGQHLPRLSGQH

Note: No experimental confirmation available.
Show »
Length:363
Mass (Da):39,778
Checksum:i13EA50904C5F24BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241G → D in BAA75544 (PubMed:10646843).Curated
Sequence conflicti332 – 3321E → A in AAV38848 (Ref. 6) Curated
Sequence conflicti339 – 3391D → E in CAB66626 (PubMed:11230166).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei37 – 371K → KGAGQHLPRLSGQH in isoform 2. 1 PublicationVSP_056873

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010025 mRNA. Translation: CAB38041.1.
AB024327 mRNA. Translation: BAA75544.1.
AF161496 mRNA. Translation: AAF29111.1.
AY049776 mRNA. Translation: AAL15433.1.
AL136691 mRNA. Translation: CAB66626.1.
BT020044 mRNA. Translation: AAV38847.1.
BT020045 mRNA. Translation: AAV38848.1.
AK297942 mRNA. Translation: BAG60258.1.
AK312295 mRNA. Translation: BAG35222.1.
AC022073 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96356.1.
BC000162 mRNA. Translation: AAH00162.1.
BC062306 mRNA. Translation: AAH62306.1.
CCDSiCCDS8676.1. [Q9Y3F4-1]
RefSeqiNP_009109.3. NM_007178.3. [Q9Y3F4-1]
UniGeneiHs.743971.

Genome annotation databases

EnsembliENST00000025399; ENSP00000025399; ENSG00000023734. [Q9Y3F4-2]
ENST00000419869; ENSP00000392270; ENSG00000023734. [Q9Y3F4-1]
GeneIDi11171.
KEGGihsa:11171.
UCSCiuc001rdc.5. human. [Q9Y3F4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010025 mRNA. Translation: CAB38041.1.
AB024327 mRNA. Translation: BAA75544.1.
AF161496 mRNA. Translation: AAF29111.1.
AY049776 mRNA. Translation: AAL15433.1.
AL136691 mRNA. Translation: CAB66626.1.
BT020044 mRNA. Translation: AAV38847.1.
BT020045 mRNA. Translation: AAV38848.1.
AK297942 mRNA. Translation: BAG60258.1.
AK312295 mRNA. Translation: BAG35222.1.
AC022073 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96356.1.
BC000162 mRNA. Translation: AAH00162.1.
BC062306 mRNA. Translation: AAH62306.1.
CCDSiCCDS8676.1. [Q9Y3F4-1]
RefSeqiNP_009109.3. NM_007178.3. [Q9Y3F4-1]
UniGeneiHs.743971.

3D structure databases

ProteinModelPortaliQ9Y3F4.
SMRiQ9Y3F4. Positions 9-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116342. 85 interactions.
IntActiQ9Y3F4. 30 interactions.
MINTiMINT-1346033.
STRINGi9606.ENSP00000392270.

PTM databases

iPTMnetiQ9Y3F4.
PhosphoSiteiQ9Y3F4.
SwissPalmiQ9Y3F4.

Polymorphism and mutation databases

BioMutaiSTRAP.
DMDMi12643951.

2D gel databases

OGPiQ9Y3F4.

Proteomic databases

EPDiQ9Y3F4.
MaxQBiQ9Y3F4.
PaxDbiQ9Y3F4.
PeptideAtlasiQ9Y3F4.
PRIDEiQ9Y3F4.
TopDownProteomicsiQ9Y3F4-1. [Q9Y3F4-1]

Protocols and materials databases

DNASUi11171.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000025399; ENSP00000025399; ENSG00000023734. [Q9Y3F4-2]
ENST00000419869; ENSP00000392270; ENSG00000023734. [Q9Y3F4-1]
GeneIDi11171.
KEGGihsa:11171.
UCSCiuc001rdc.5. human. [Q9Y3F4-1]

Organism-specific databases

CTDi11171.
GeneCardsiSTRAP.
HGNCiHGNC:30796. STRAP.
HPAiHPA027320.
HPA055557.
MIMi605986. gene.
neXtProtiNX_Q9Y3F4.
PharmGKBiPA134867032.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0278. Eukaryota.
ENOG410XPJ4. LUCA.
GeneTreeiENSGT00630000089849.
HOGENOMiHOG000174258.
HOVERGENiHBG055228.
InParanoidiQ9Y3F4.
KOiK13137.
OMAiHGPIWSI.
PhylomeDBiQ9Y3F4.
TreeFamiTF323287.

Enzyme and pathway databases

ReactomeiR-HSA-2173788. Downregulation of TGF-beta receptor signaling.
SignaLinkiQ9Y3F4.

Miscellaneous databases

ChiTaRSiSTRAP. human.
GeneWikiiSTRAP.
GenomeRNAii11171.
NextBioi35473629.
PROiQ9Y3F4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3F4.
CleanExiHS_STRAP.
ExpressionAtlasiQ9Y3F4. baseline and differential.
GenevisibleiQ9Y3F4. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA."
    Hunt S.L., Hsuan J.J., Totty N., Jackson R.J.
    Genes Dev. 13:437-448(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CSDE1.
  2. "Molecular cloning and characterization of human MAWD, a novel protein containing WD-40 repeats frequently overexpressed in breast cancer."
    Matsuda S., Katsumata R., Okuda T., Yamamoto T., Miyazaki K., Senga T., Machida K., Thant A.A., Nakatsugawa S., Hamaguchi M.
    Cancer Res. 60:13-17(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. Ye M., Zhang Q.H., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L., Fan H.Y., Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Blood.
  4. Liu J., Zhou Y., Peng X., Yuan J., Qiang B.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "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 1 AND 2).
    Tissue: Cerebellum.
  8. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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 1).
    Tissue: Placenta and Retina.
  11. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 250-262 AND 273-290, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  12. Cited for: IDENTIFICATION IN SMN COMPLEX, INTERACTION WITH GEMIN6 AND GEMIN7, SUBCELLULAR LOCATION.
  13. "Unrip, a factor implicated in cap-independent translation, associates with the cytosolic SMN complex and influences its intracellular localization."
    Grimmler M., Otter S., Peter C., Mueller F., Chari A., Fischer U.
    Hum. Mol. Genet. 14:3099-3111(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SMN COMPLEX, SUBCELLULAR LOCATION.
  14. "Regulation of transforming growth factor-beta signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein."
    Seong H.A., Jung H., Choi H.S., Kim K.T., Ha H.
    J. Biol. Chem. 280:42897-42908(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PDPK1.
  15. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
    Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
    Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-335 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSTRAP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3F4
Secondary accession number(s): B2R5S5
, B4DNJ6, Q5TZT4, Q9NTK0, Q9UQC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 156 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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.