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P16949 (STMN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stathmin
Alternative name(s):
Leukemia-associated phosphoprotein p18
Metablastin
Oncoprotein 18
Short name=Op18
Phosphoprotein p19
Short name=pp19
Prosolin
Protein Pr22
pp17
Gene names
Name:STMN1
Synonyms:C1orf215, LAP18, OP18
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear By similarity.

Subunit structure

Binds to two alpha/beta-tubulin heterodimers. Interacts with KIST. Ref.15 Ref.16

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Ubiquitous. Expression is strongest in fetal and adult brain, spinal cord, and cerebellum, followed by thymus, bone marrow, testis, and fetal liver. Expression is intermediate in colon, ovary, placenta, uterus, and trachea, and is readily detected at substantially lower levels in all other tissues examined. Lowest expression is found in adult liver. Present in much greater abundance in cells from patients with acute leukemia of different subtypes than in normal peripheral blood lymphocytes, non-leukemic proliferating lymphoid cells, bone marrow cells, or cells from patients with chronic lymphoid or myeloid leukemia. Ref.3 Ref.18

Induction

Down-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.20

Post-translational modification

Many different phosphorylated forms are observed depending on specific combinations among the sites which can be phosphorylated. MAPK is responsible for the phosphorylation of stathmin in response to NGF. Phosphorylation at Ser-16 seems to be required for neuron polarization By similarity. Phosphorylation at Ser-63 reduces tubulin binding 10-fold and suppresses the MT polymerization inhibition activity. Ref.11 Ref.12 Ref.13 Ref.14 Ref.17

Sequence similarities

Belongs to the stathmin family.

Contains 1 SLD (stathmin-like) domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Traceable author statement PubMed 2917975. Source: ProtInc

microtubule depolymerization

Inferred from direct assay PubMed 9880330. Source: MGI

mitotic spindle organization

Inferred from direct assay PubMed 9271428. Source: MGI

negative regulation of microtubule polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular component movement

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from expression pattern Ref.20. Source: UniProtKB

signal transduction

Non-traceable author statement PubMed 8003023. Source: ProtInc

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

intracellular

Inferred from direct assay. Source: LIFEdb

membrane

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionsignal transducer activity

Traceable author statement PubMed 2917975PubMed 8003023. Source: ProtInc

tubulin binding

Inferred from direct assay Ref.15. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P16949-1)

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.
Isoform 2 (identifier: P16949-2)

The sequence of this isoform differs from the canonical sequence as follows:
     127-149: DKHIEEVRKNKESKDPADETEAD → MYFWTHGPGAHPAQISAEQSCLHSVPALCPALGLQSALITWSDLSHHH
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 149148Stathmin
PRO_0000182389

Regions

Domain4 – 145142SLD
Coiled coil41 – 140100 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.11 Ref.26 Ref.28 Ref.32 Ref.33
Modified residue91N6-acetyllysine Ref.28
Modified residue161Phosphoserine Ref.13 Ref.14 Ref.19 Ref.21 Ref.22 Ref.24 Ref.27 Ref.29 Ref.31
Modified residue251Phosphoserine; by CDK1, MAPK1 and MAPK3 Ref.11 Ref.12 Ref.13 Ref.14 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.27 Ref.29 Ref.31
Modified residue311Phosphoserine Ref.31
Modified residue381Phosphoserine; by CDK1, MAPK1 and MAPK3 Ref.11 Ref.12 Ref.13 Ref.14 Ref.21 Ref.22 Ref.23 Ref.25 Ref.27 Ref.29 Ref.31
Modified residue631Phosphoserine; by PKA Ref.17 Ref.19 Ref.22 Ref.29 Ref.31
Modified residue1001N6-acetyllysine Ref.28
Modified residue1191N6-acetyllysine Ref.28

Natural variations

Alternative sequence127 – 14923DKHIE…ETEAD → MYFWTHGPGAHPAQISAEQS CLHSVPALCPALGLQSALIT WSDLSHHH in isoform 2.
VSP_041377

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 316426F60DABCD01

FASTA14917,303
        10         20         30         40         50         60 
MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER 

        70         80         90        100        110        120 
RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL 

       130        140 
ERLREKDKHI EEVRKNKESK DPADETEAD 

« Hide

Isoform 2 [UniParc].

Checksum: 7F66FFAB6C32A5AB
Show »

FASTA17419,824

References

« Hide 'large scale' references
[1]"Molecular cloning of a novel human leukemia-associated gene. Evidence of conservation in animal species."
Zhu X.-X., Kozarsky K., Strahler J.R., Eckerskorn C., Lottspeich F., Melhem R., Lowe J., Fox D.A., Hanash S.M., Atweh G.F.
J. Biol. Chem. 264:14556-14560(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 45-61.
[2]"A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations."
Maucuer A., Doye V., Sobel A.
FEBS Lett. 264:275-278(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Characterization of the gene for a proliferation-related phosphoprotein (oncoprotein 18) expressed in high amounts in acute leukemia."
Melhem R.F., Zhu X., Hailat N., Strahler J.R., Hanash S.M.
J. Biol. Chem. 266:17747-17753(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[4]"Transcriptional and post-transcriptional regulation of pr22 (Op18) with proliferation control."
Hosoya H., Ishikawa K., Dohi N., Marunouchi T.
Cell Struct. Funct. 21:237-243(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"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. expand/collapse author list , 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: Kidney and Testis.
[6]"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. expand/collapse author list , 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].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Lung.
[9]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 14-41 AND 44-52, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"Ca2+-dependent and cAMP-dependent control of nicotinic acetylcholine receptor phosphorylation in muscle cells."
Hanash S.M., Strahler J.R., Kuick R., Chu E.H.Y., Nichols D.
J. Biol. Chem. 264:12813-12819(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 87-96.
[11]"Analysis of phosphoprotein p19 by liquid chromatography/mass spectrometry. Identification of two proline-directed serine phosphorylation sites and a blocked amino terminus."
Labdon J.E., Nieves E., Schubart U.K.
J. Biol. Chem. 267:3506-3513(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-25 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase."
Marklund U., Brattsand G., Shingler V., Gullberg M.
J. Biol. Chem. 268:15039-15047(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-25 AND SER-38.
[13]"Multiple signal transduction pathways induce phosphorylation of serines 16, 25, and 38 of oncoprotein 18 in T lymphocytes."
Marklund U., Brattsand G., Osterman O., Ohlsson P.-I., Gullberg M.
J. Biol. Chem. 268:25671-25680(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-16; SER-25 AND SER-38.
[14]"Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16, Ser25 and Ser38."
Brattsand G., Marklund U., Nylander K., Roos G., Gullberg M.
Eur. J. Biochem. 220:359-368(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-16; SER-25 AND SER-38.
[15]"Op18/stathmin caps a kinked protofilament-like tubulin tetramer."
Steinmetz M.O., Kammerer R.A., Jahnke W., Goldie K.N., Lustig A., van Oostrum J.
EMBO J. 19:572-580(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TUBULIN.
[16]"Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry."
Redeker V., Lachkar S., Siavoshian S., Charbaut E., Rossier J., Sobel A., Curmi P.A.
J. Biol. Chem. 275:6841-6849(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TUBULIN.
[17]"Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin."
Steinmetz M.O., Jahnke W., Towbin H., Garcia-Echeverria C., Voshol H., Mueller D., van Oostrum J.
EMBO Rep. 2:505-510(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: EFFECT OF PHOSPHORYLATION AT SER-63 ON TUBULIN BINDING.
[18]"Expression of stathmin family genes in human tissues: non-neural-restricted expression for SCLIP."
Bieche I., Maucuer A., Laurendeau I., Lachkar S., Spano A.J., Frankfurter A., Levy P., Manceau V., Sobel A., Vidaud M., Curmi P.A.
Genomics 81:400-410(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[19]"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-16; SER-25 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
Leong W.F., Chow V.T.
Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[24]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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-16; SER-25 AND SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[28]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-9; LYS-100 AND LYS-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"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-16; SER-25; SER-38 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[30]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"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-16; SER-25; SER-31; SER-38 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04991 mRNA. Translation: AAA59980.1.
M31303 Genomic DNA. Translation: AAA59971.1.
X53305 mRNA. Translation: CAA37391.1.
Z11566 mRNA. Translation: CAA77660.1.
X94912 Genomic DNA. Translation: CAA64398.1.
AK303692 mRNA. Translation: BAH14020.1.
AK311801 mRNA. Translation: BAG34744.1.
AL033528 Genomic DNA. Translation: CAC16020.1.
CH471059 Genomic DNA. Translation: EAX07854.1.
CH471059 Genomic DNA. Translation: EAX07855.1.
CH471059 Genomic DNA. Translation: EAX07856.1.
CH471059 Genomic DNA. Translation: EAX07857.1.
CH471059 Genomic DNA. Translation: EAX07858.1.
CH471059 Genomic DNA. Translation: EAX07859.1.
CH471059 Genomic DNA. Translation: EAX07860.1.
BC082228 mRNA. Translation: AAH82228.1.
CCDSCCDS269.1. [P16949-1]
CCDS44090.1. [P16949-2]
PIRA40936.
RefSeqNP_001138926.1. NM_001145454.2. [P16949-2]
NP_005554.1. NM_005563.3. [P16949-1]
NP_981944.1. NM_203399.1. [P16949-1]
NP_981946.1. NM_203401.1. [P16949-1]
UniGeneHs.209983.

3D structure databases

DisProtDP00174.
ProteinModelPortalP16949.
SMRP16949. Positions 6-141.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110119. 27 interactions.
IntActP16949. 11 interactions.
MINTMINT-2860454.
STRING9606.ENSP00000410452.

PTM databases

PhosphoSiteP16949.

Polymorphism databases

DMDM134973.

2D gel databases

DOSAC-COBS-2DPAGEP16949.
REPRODUCTION-2DPAGEIPI00479997.
SWISS-2DPAGEP16949.
UCD-2DPAGEP16949.

Proteomic databases

MaxQBP16949.
PaxDbP16949.
PeptideAtlasP16949.
PRIDEP16949.

Protocols and materials databases

DNASU3925.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357865; ENSP00000350531; ENSG00000117632. [P16949-1]
ENST00000374291; ENSP00000363409; ENSG00000117632. [P16949-1]
ENST00000399728; ENSP00000382633; ENSG00000117632. [P16949-1]
ENST00000426559; ENSP00000410452; ENSG00000117632. [P16949-2]
ENST00000455785; ENSP00000387858; ENSG00000117632. [P16949-1]
GeneID3925.
KEGGhsa:3925.
UCSCuc001bkz.3. human. [P16949-1]
uc010oev.2. human. [P16949-2]

Organism-specific databases

CTD3925.
GeneCardsGC01M026211.
HGNCHGNC:6510. STMN1.
HPACAB010107.
MIM151442. gene.
neXtProtNX_P16949.
PharmGKBPA35491.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG75290.
HOGENOMHOG000013197.
HOVERGENHBG054037.
InParanoidP16949.
KOK04381.
OMAKECARIA.
OrthoDBEOG744TBN.
PhylomeDBP16949.
TreeFamTF326935.

Enzyme and pathway databases

SignaLinkP16949.

Gene expression databases

ArrayExpressP16949.
BgeeP16949.
CleanExHS_STMN1.
GenevestigatorP16949.

Family and domain databases

InterProIPR000956. Stathmin_fam.
[Graphical view]
PANTHERPTHR10104. PTHR10104. 1 hit.
PfamPF00836. Stathmin. 1 hit.
[Graphical view]
PIRSFPIRSF002285. Stathmin. 1 hit.
PRINTSPR00345. STATHMIN.
SUPFAMSSF101494. SSF101494. 1 hit.
PROSITEPS00563. STATHMIN_1. 1 hit.
PS01041. STATHMIN_2. 1 hit.
PS51663. STATHMIN_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTMN1. human.
GeneWikiStathmin.
GenomeRNAi3925.
NextBio15415.
PROP16949.
SOURCESearch...

Entry information

Entry nameSTMN1_HUMAN
AccessionPrimary (citable) accession number: P16949
Secondary accession number(s): A2A2D1 expand/collapse secondary AC list , B2R4E7, B7Z8N4, D3DPJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM