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Q5VSL9

- STRP1_HUMAN

UniProt

Q5VSL9 - STRP1_HUMAN

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Protein

Striatin-interacting protein 1

Gene

STRIP1

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

Functioni

Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape.1 Publication

GO - Biological processi

  1. cortical actin cytoskeleton organization Source: UniProtKB
  2. regulation of cell morphogenesis Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Striatin-interacting protein 1
Alternative name(s):
Protein FAM40A
Gene namesi
Name:STRIP1
Synonyms:FAM40A, KIAA1761
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:25916. STRIP1.

Subcellular locationi

Cytoplasm 1 Publication
Note: Enriched on the plasma membrane.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134939426.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 837837Striatin-interacting protein 1PRO_0000187017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei335 – 3351Phosphoserine8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5VSL9.
PaxDbiQ5VSL9.
PRIDEiQ5VSL9.

PTM databases

PhosphoSiteiQ5VSL9.

Expressioni

Gene expression databases

BgeeiQ5VSL9.
CleanExiHS_FAM40A.
GenevestigatoriQ5VSL9.

Organism-specific databases

HPAiHPA060302.

Interactioni

Subunit structurei

Component of striatin-interacting phosphatase and kinase (STRIPAK) complex By similarity. Interacts with CTTNBP2NL.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CTTNBP2NLQ9P2B44EBI-1773588,EBI-1774273
MST4Q9P2892EBI-1773588,EBI-618239
TRAF3IP3Q9Y2282EBI-1773588,EBI-765817

Protein-protein interaction databases

BioGridi124497. 37 interactions.
IntActiQ5VSL9. 27 interactions.
STRINGi9606.ENSP00000358810.

Structurei

3D structure databases

ProteinModelPortaliQ5VSL9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 3634Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the STRIP family.Curated

Phylogenomic databases

eggNOGiNOG247682.
GeneTreeiENSGT00400000022095.
HOVERGENiHBG081506.
InParanoidiQ5VSL9.
OMAiLIMNNKQ.
OrthoDBiEOG7W1536.
PhylomeDBiQ5VSL9.
TreeFamiTF314205.

Family and domain databases

InterProiIPR021819. DUF3402.
IPR012486. N1221.
[Graphical view]
PfamiPF11882. DUF3402. 1 hit.
PF07923. N1221. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5VSL9-1) [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
MEPAVGGPGP LIVNNKQPQP PPPPPPAAAQ PPPGAPRAAA GLLPGGKARE
60 70 80 90 100
FNRNQRKDSE GYSESPDLEF EYADTDKWAA ELSELYSYTE GPEFLMNRKC
110 120 130 140 150
FEEDFRIHVT DKKWTELDTN QHRTHAMRLL DGLEVTAREK RLKVARAILY
160 170 180 190 200
VAQGTFGECS SEAEVQSWMR YNIFLLLEVG TFNALVELLN MEIDNSAACS
210 220 230 240 250
SAVRKPAISL ADSTDLRVLL NIMYLIVETV HQECEGDKAE WRTMRQTFRA
260 270 280 290 300
ELGSPLYNNE PFAIMLFGMV TKFCSGHAPH FPMKKVLLLL WKTVLCTLGG
310 320 330 340 350
FEELQSMKAE KRSILGLPPL PEDSIKVIRN MRAASPPASA SDLIEQQQKR
360 370 380 390 400
GRREHKALIK QDNLDAFNER DPYKADDSRE EEEENDDDNS LEGETFPLER
410 420 430 440 450
DEVMPPPLQH PQTDRLTCPK GLPWAPKVRE KDIEMFLESS RSKFIGYTLG
460 470 480 490 500
SDTNTVVGLP RPIHESIKTL KQHKYTSIAE VQAQMEEEYL RSPLSGGEEE
510 520 530 540 550
VEQVPAETLY QGLLPSLPQY MIALLKILLA AAPTSKAKTD SINILADVLP
560 570 580 590 600
EEMPTTVLQS MKLGVDVNRH KEVIVKAISA VLLLLLKHFK LNHVYQFEYM
610 620 630 640 650
AQHLVFANCI PLILKFFNQN IMSYITAKNS ISVLDYPHCV VHELPELTAE
660 670 680 690 700
SLEAGDSNQF CWRNLFSCIN LLRILNKLTK WKHSRTMMLV VFKSAPILKR
710 720 730 740 750
ALKVKQAMMQ LYVLKLLKVQ TKYLGRQWRK SNMKTMSAIY QKVRHRLNDD
760 770 780 790 800
WAYGNDLDAR PWDFQAEECA LRANIERFNA RRYDRAHSNP DFLPVDNCLQ
810 820 830
SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ
Length:837
Mass (Da):95,576
Last modified:December 7, 2004 - v1
Checksum:i5F9BA1D4C7DE6925
GO
Isoform 2 (identifier: Q5VSL9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-95: Missing.

Note: No experimental confirmation available.

Show »
Length:742
Mass (Da):85,451
Checksum:iA4C208A05F910919
GO
Isoform 3 (identifier: Q5VSL9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-264: Missing.
     596-596: Q → QVPTGLSLLS...FFFFFSCWLQ
     630-630: S → R
     631-837: Missing.

Note: No experimental confirmation available.

Show »
Length:440
Mass (Da):49,699
Checksum:iB1ADA0F87A30303E
GO
Isoform 4 (identifier: Q5VSL9-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     194-212: DNSAACSSAVRKPAISLAD → EHCCVRPAVSALAGGQAQD
     213-837: Missing.

Note: No experimental confirmation available.

Show »
Length:212
Mass (Da):23,540
Checksum:i636A065B51CB3595
GO

Sequence cautioni

The sequence AAH32644.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971P → L in BAC86034. (PubMed:14702039)Curated
Sequence conflicti744 – 7441R → Q in BAB55265. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 264264Missing in isoform 3. 1 PublicationVSP_014856Add
BLAST
Alternative sequencei1 – 9595Missing in isoform 2. 1 PublicationVSP_014857Add
BLAST
Alternative sequencei194 – 21219DNSAA…ISLAD → EHCCVRPAVSALAGGQAQD in isoform 4. 1 PublicationVSP_014858Add
BLAST
Alternative sequencei213 – 837625Missing in isoform 4. 1 PublicationVSP_014859Add
BLAST
Alternative sequencei596 – 5961Q → QVPTGLSLLSCGLGPRALLL LQPTRTGALAFDPLELCMNV LRHGPSAKAFHPWRKEGKVP RAAPFFFFFFSCWLQ in isoform 3. 1 PublicationVSP_014860
Alternative sequencei630 – 6301S → R in isoform 3. 1 PublicationVSP_014861
Alternative sequencei631 – 837207Missing in isoform 3. 1 PublicationVSP_014862Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB051548 mRNA. Translation: BAB21852.2.
AK027649 mRNA. Translation: BAB55265.1.
AK125054 mRNA. Translation: BAC86034.1.
AL834196 mRNA. Translation: CAH56368.1.
AL772411, AL160006 Genomic DNA. Translation: CAH70967.1.
AL772411, AL160006 Genomic DNA. Translation: CAH70968.1.
AL160006, AL772411 Genomic DNA. Translation: CAI22715.1.
AL160006, AL772411 Genomic DNA. Translation: CAI22716.1.
BC032644 mRNA. Translation: AAH32644.1. Different initiation.
BC094786 mRNA. Translation: AAH94786.1.
BC119814 mRNA. Translation: AAI19815.1.
BC121793 mRNA. Translation: AAI21794.1.
CCDSiCCDS30798.1. [Q5VSL9-1]
CCDS59197.1. [Q5VSL9-2]
RefSeqiNP_001257697.1. NM_001270768.1. [Q5VSL9-2]
NP_149079.2. NM_033088.3. [Q5VSL9-1]
UniGeneiHs.584996.

Genome annotation databases

EnsembliENST00000369795; ENSP00000358810; ENSG00000143093. [Q5VSL9-1]
ENST00000369796; ENSP00000358811; ENSG00000143093. [Q5VSL9-2]
ENST00000485775; ENSP00000476025; ENSG00000143093. [Q5VSL9-4]
GeneIDi85369.
KEGGihsa:85369.
UCSCiuc001dyz.1. human. [Q5VSL9-1]

Polymorphism databases

DMDMi71648671.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB051548 mRNA. Translation: BAB21852.2 .
AK027649 mRNA. Translation: BAB55265.1 .
AK125054 mRNA. Translation: BAC86034.1 .
AL834196 mRNA. Translation: CAH56368.1 .
AL772411 , AL160006 Genomic DNA. Translation: CAH70967.1 .
AL772411 , AL160006 Genomic DNA. Translation: CAH70968.1 .
AL160006 , AL772411 Genomic DNA. Translation: CAI22715.1 .
AL160006 , AL772411 Genomic DNA. Translation: CAI22716.1 .
BC032644 mRNA. Translation: AAH32644.1 . Different initiation.
BC094786 mRNA. Translation: AAH94786.1 .
BC119814 mRNA. Translation: AAI19815.1 .
BC121793 mRNA. Translation: AAI21794.1 .
CCDSi CCDS30798.1. [Q5VSL9-1 ]
CCDS59197.1. [Q5VSL9-2 ]
RefSeqi NP_001257697.1. NM_001270768.1. [Q5VSL9-2 ]
NP_149079.2. NM_033088.3. [Q5VSL9-1 ]
UniGenei Hs.584996.

3D structure databases

ProteinModelPortali Q5VSL9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124497. 37 interactions.
IntActi Q5VSL9. 27 interactions.
STRINGi 9606.ENSP00000358810.

PTM databases

PhosphoSitei Q5VSL9.

Polymorphism databases

DMDMi 71648671.

Proteomic databases

MaxQBi Q5VSL9.
PaxDbi Q5VSL9.
PRIDEi Q5VSL9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369795 ; ENSP00000358810 ; ENSG00000143093 . [Q5VSL9-1 ]
ENST00000369796 ; ENSP00000358811 ; ENSG00000143093 . [Q5VSL9-2 ]
ENST00000485775 ; ENSP00000476025 ; ENSG00000143093 . [Q5VSL9-4 ]
GeneIDi 85369.
KEGGi hsa:85369.
UCSCi uc001dyz.1. human. [Q5VSL9-1 ]

Organism-specific databases

CTDi 85369.
GeneCardsi GC01P110579.
H-InvDB HIX0199796.
HGNCi HGNC:25916. STRIP1.
HPAi HPA060302.
neXtProti NX_Q5VSL9.
PharmGKBi PA134939426.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG247682.
GeneTreei ENSGT00400000022095.
HOVERGENi HBG081506.
InParanoidi Q5VSL9.
OMAi LIMNNKQ.
OrthoDBi EOG7W1536.
PhylomeDBi Q5VSL9.
TreeFami TF314205.

Miscellaneous databases

GeneWikii FAM40A.
GenomeRNAii 85369.
NextBioi 75905.
PROi Q5VSL9.

Gene expression databases

Bgeei Q5VSL9.
CleanExi HS_FAM40A.
Genevestigatori Q5VSL9.

Family and domain databases

InterProi IPR021819. DUF3402.
IPR012486. N1221.
[Graphical view ]
Pfami PF11882. DUF3402. 1 hit.
PF07923. N1221. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. Ohara O., Nagase T., Kikuno R.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "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 AND 3).
    Tissue: Thalamus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Amygdala.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 Uterus.
  7. "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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
    Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
    Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTTNBP2NL.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
    Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
    BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTRP1_HUMAN
AccessioniPrimary (citable) accession number: Q5VSL9
Secondary accession number(s): Q0V925
, Q5VSL8, Q658K2, Q6ZV31, Q8N598, Q96SN2, Q9C0A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: December 7, 2004
Last modified: October 29, 2014
This is version 91 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3