P16949 (STMN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton.
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.22
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 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31
Sequence similarities	Belongs to the stathmin family.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW intracellular signal transduction Traceable author statement. Source: ProtInc microtubule depolymerization Inferred from direct assay. Source: MGI mitotic spindle organization Inferred from direct assay. Source: MGI nervous system development Inferred from electronic annotation. Source: UniProtKB-KW response to virus Inferred from expression pattern Ref.22. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	signal transducer activity Traceable author statement. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 149	148	Stathmin		PRO_0000182389
Regions
	Coiled coil	41 – 140	100	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.11 Ref.30
	Modified residue	9	1	N6-acetyllysine Ref.32
	Modified residue	16	1	Phosphoserine Ref.13 Ref.14 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31
	Modified residue	25	1	Phosphoserine; by CDK1, MAPK1 and MAPK3 Ref.11 Ref.12 Ref.13 Ref.14 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31
	Modified residue	28	1	Phosphoserine Ref.26
	Modified residue	38	1	Phosphoserine; by CDK1, MAPK1 and MAPK3 Ref.11 Ref.12 Ref.13 Ref.14 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31
	Modified residue	46	1	Phosphoserine By similarity
	Modified residue	63	1	Phosphoserine; by PKA Ref.17 Ref.21 Ref.24 Ref.26 Ref.29
	Modified residue	80	1	N6-acetyllysine Ref.32
	Modified residue	95	1	N6-acetyllysine Ref.32
	Modified residue	100	1	N6-acetyllysine Ref.32
	Modified residue	119	1	N6-acetyllysine Ref.32
	Modified residue	128	1	N6-acetyllysine Ref.32
	Modified residue	146	1	Phosphothreonine Ref.26
Natural variations
	Alternative sequence	127 – 149	23	DKHIE…ETEAD → MYFWTHGPGAHPAQISAEQS CLHSVPALCPALGLQSALIT WSDLSHHH in isoform 2.		VSP_041377

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 316426F60DABCD01	FASTA	149	17,303
	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
	Isoform 2 [UniParc]. Checksum: 7F66FFAB6C32A5AB	FASTA	174	19,824
	10 20 30 40 50 60 MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER 70 80 90 100 110 120 RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL 130 140 150 160 170 ERLREKMYFW THGPGAHPAQ ISAEQSCLHS VPALCPALGL QSALITWSDL SHHH

References

	« Hide 'large scale' referencesShow '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: 2760073] [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: 2358074] [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: 1917919] [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: 8906359] [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. , 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: 14702039] [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. , 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: 16710414] [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. , 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: 15489334] [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, 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: 2546936] [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: 1737801] [Abstract] Cited for: ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-25 AND SER-38, 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: 8325880] [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: 8245003] [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: 8125092] [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: 10675326] [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: 10702243] [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: 11415983] [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: 12676564] [Abstract] Cited for: TISSUE SPECIFICITY.
[19]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[20]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND SER-63, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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: 16548883] [Abstract] Cited for: INDUCTION, MASS SPECTROMETRY.
[23]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND SER-63, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[26]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-28; SER-38; SER-63 AND THR-146, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[27]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-25, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25; SER-38 AND SER-63, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[31]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-25 AND SER-38, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[32]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-80; LYS-95; LYS-100; LYS-119 AND LYS-128, MASS SPECTROMETRY.
[33]	"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: 21269460] [Abstract] Cited for: 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.
IPI	IPI00479997. IPI00921996.
PIR	A40936.
RefSeq	NP_001138926.1. NM_001145454.1. NP_005554.1. NM_005563.3. NP_981944.1. NM_203399.1. NP_981946.1. NM_203401.1.
UniGene	Hs.209983.
3D structure databases
ProteinModelPortal	P16949.
SMR	P16949. Positions 6-141.
DisProt	DP00174.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16949. 6 interactions.
MINT	MINT-2860454.
STRING	P16949.
PTM databases
PhosphoSite	P16949.
Polymorphism databases
DMDM	134973.
2D gel databases
SWISS-2DPAGE	P16949.
DOSAC-COBS-2DPAGE	P16949.
REPRODUCTION-2DPAGE	IPI00479997.
UCD-2DPAGE	P16949.
Proteomic databases
PeptideAtlas	P16949.
PRIDE	P16949.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357865; ENSP00000350531; ENSG00000117632. ENST00000374291; ENSP00000363409; ENSG00000117632. ENST00000399728; ENSP00000382633; ENSG00000117632. ENST00000455785; ENSP00000387858; ENSG00000117632.
GeneID	3925.
KEGG	hsa:3925.
UCSC	uc001bkz.1. human.
Organism-specific databases
CTD	3925.
GeneCards	GC01M026211.
H-InvDB	HIX0000281.
HGNC	HGNC:6510. STMN1.
HPA	CAB010107.
MIM	151442. gene.
neXtProt	NX_P16949.
PharmGKB	PA35491.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG054037.
InParanoid	P16949.
OMA	KEAVPEF.
OrthoDB	EOG46MBKT.
PhylomeDB	P16949.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling. p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.
Gene expression databases
ArrayExpress	P16949.
Bgee	P16949.
CleanEx	HS_STMN1.
Genevestigator	P16949.
GermOnline	ENSG00000117632. Homo sapiens.
Family and domain databases
InterPro	IPR000956. Stathmin. [Graphical view]
KO	K04381.
PANTHER	PTHR10104. Stathmin. 1 hit.
Pfam	PF00836. Stathmin. 1 hit. [Graphical view]
PIRSF	PIRSF002285. Stathmin. 1 hit.
PRINTS	PR00345. STATHMIN.
SUPFAM	SSF101494. Stathmin. 1 hit.
PROSITE	PS00563. STATHMIN_1. 1 hit. PS01041. STATHMIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	15415.
SOURCE	Search...

Entry information

Entry name

STMN1_HUMAN

Accession

Primary (citable) accession number: P16949
Secondary accession number(s): A2A2D1 , B2R4E7, B7Z8N4, D3DPJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.