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P16949

- STMN1_HUMAN

UniProt

P16949 - STMN1_HUMAN

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Protein
Stathmin
Gene
STMN1, C1orf215, LAP18, OP18
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. signal transducer activity Source: ProtInc
  2. tubulin binding Source: MGI

GO - Biological processi

  1. axonogenesis Source: Ensembl
  2. intracellular signal transduction Source: ProtInc
  3. microtubule depolymerization Source: MGI
  4. mitotic spindle organization Source: MGI
  5. negative regulation of microtubule polymerization Source: Ensembl
  6. positive regulation of cellular component movement Source: Ensembl
  7. response to virus Source: UniProtKB
  8. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

SignaLinkiP16949.

Names & Taxonomyi

Protein namesi
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 namesi
Name:STMN1
Synonyms:C1orf215, LAP18, OP18
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6510. STMN1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. intracellular Source: LIFEdb
  4. membrane Source: Ensembl
  5. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35491.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 149148Stathmin
PRO_0000182389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei9 – 91N6-acetyllysine1 Publication
Modified residuei16 – 161Phosphoserine9 Publications
Modified residuei25 – 251Phosphoserine; by CDK1, MAPK1 and MAPK312 Publications
Modified residuei31 – 311Phosphoserine1 Publication
Modified residuei38 – 381Phosphoserine; by CDK1, MAPK1 and MAPK311 Publications
Modified residuei63 – 631Phosphoserine; by PKA5 Publications
Modified residuei100 – 1001N6-acetyllysine1 Publication
Modified residuei119 – 1191N6-acetyllysine1 Publication

Post-translational modificationi

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.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP16949.
PaxDbiP16949.
PeptideAtlasiP16949.
PRIDEiP16949.

2D gel databases

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

PTM databases

PhosphoSiteiP16949.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

Down-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

Gene expression databases

ArrayExpressiP16949.
BgeeiP16949.
CleanExiHS_STMN1.
GenevestigatoriP16949.

Organism-specific databases

HPAiCAB010107.

Interactioni

Subunit structurei

Binds to two alpha/beta-tubulin heterodimers. Interacts with KIST.2 Publications

Protein-protein interaction databases

BioGridi110119. 28 interactions.
IntActiP16949. 11 interactions.
MINTiMINT-2860454.
STRINGi9606.ENSP00000410452.

Structurei

3D structure databases

DisProtiDP00174.
ProteinModelPortaliP16949.
SMRiP16949. Positions 6-141.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 145142SLD
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili41 – 140100 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the stathmin family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG75290.
HOGENOMiHOG000013197.
HOVERGENiHBG054037.
InParanoidiP16949.
KOiK04381.
OMAiKECARIA.
OrthoDBiEOG744TBN.
PhylomeDBiP16949.
TreeFamiTF326935.

Family and domain databases

InterProiIPR000956. Stathmin_fam.
[Graphical view]
PANTHERiPTHR10104. PTHR10104. 1 hit.
PfamiPF00836. Stathmin. 1 hit.
[Graphical view]
PIRSFiPIRSF002285. Stathmin. 1 hit.
PRINTSiPR00345. STATHMIN.
SUPFAMiSSF101494. SSF101494. 1 hit.
PROSITEiPS00563. STATHMIN_1. 1 hit.
PS01041. STATHMIN_2. 1 hit.
PS51663. STATHMIN_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P16949-1) [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

MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI    50
QKKLEAAEER RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK 100
LTHKMEANKE NREAQMAAKL ERLREKDKHI EEVRKNKESK DPADETEAD 149
Length:149
Mass (Da):17,303
Last modified:January 23, 2007 - v3
Checksum:i316426F60DABCD01
GO
Isoform 2 (identifier: P16949-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-149: DKHIEEVRKNKESKDPADETEAD → MYFWTHGPGAHPAQISAEQSCLHSVPALCPALGLQSALITWSDLSHHH

Note: No experimental confirmation available.

Show »
Length:174
Mass (Da):19,824
Checksum:i7F66FFAB6C32A5AB
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei127 – 14923DKHIE…ETEAD → MYFWTHGPGAHPAQISAEQS CLHSVPALCPALGLQSALIT WSDLSHHH in isoform 2.
VSP_041377Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS269.1. [P16949-1]
CCDS44090.1. [P16949-2]
PIRiA40936.
RefSeqiNP_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]
UniGeneiHs.209983.

Genome annotation databases

EnsembliENST00000357865; ENSP00000350531; ENSG00000117632. [P16949-1]
ENST00000374291; ENSP00000363409; ENSG00000117632. [P16949-1]
ENST00000399728; ENSP00000382633; ENSG00000117632. [P16949-1]
ENST00000426559; ENSP00000410452; ENSG00000117632. [P16949-2]
ENST00000455785; ENSP00000387858; ENSG00000117632. [P16949-1]
GeneIDi3925.
KEGGihsa:3925.
UCSCiuc001bkz.3. human. [P16949-1]
uc010oev.2. human. [P16949-2]

Polymorphism databases

DMDMi134973.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS269.1. [P16949-1 ]
CCDS44090.1. [P16949-2 ]
PIRi A40936.
RefSeqi NP_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 ]
UniGenei Hs.209983.

3D structure databases

DisProti DP00174.
ProteinModelPortali P16949.
SMRi P16949. Positions 6-141.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110119. 28 interactions.
IntActi P16949. 11 interactions.
MINTi MINT-2860454.
STRINGi 9606.ENSP00000410452.

PTM databases

PhosphoSitei P16949.

Polymorphism databases

DMDMi 134973.

2D gel databases

DOSAC-COBS-2DPAGE P16949.
REPRODUCTION-2DPAGE IPI00479997.
SWISS-2DPAGE P16949.
UCD-2DPAGE P16949.

Proteomic databases

MaxQBi P16949.
PaxDbi P16949.
PeptideAtlasi P16949.
PRIDEi P16949.

Protocols and materials databases

DNASUi 3925.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357865 ; ENSP00000350531 ; ENSG00000117632 . [P16949-1 ]
ENST00000374291 ; ENSP00000363409 ; ENSG00000117632 . [P16949-1 ]
ENST00000399728 ; ENSP00000382633 ; ENSG00000117632 . [P16949-1 ]
ENST00000426559 ; ENSP00000410452 ; ENSG00000117632 . [P16949-2 ]
ENST00000455785 ; ENSP00000387858 ; ENSG00000117632 . [P16949-1 ]
GeneIDi 3925.
KEGGi hsa:3925.
UCSCi uc001bkz.3. human. [P16949-1 ]
uc010oev.2. human. [P16949-2 ]

Organism-specific databases

CTDi 3925.
GeneCardsi GC01M026211.
HGNCi HGNC:6510. STMN1.
HPAi CAB010107.
MIMi 151442. gene.
neXtProti NX_P16949.
PharmGKBi PA35491.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG75290.
HOGENOMi HOG000013197.
HOVERGENi HBG054037.
InParanoidi P16949.
KOi K04381.
OMAi KECARIA.
OrthoDBi EOG744TBN.
PhylomeDBi P16949.
TreeFami TF326935.

Enzyme and pathway databases

SignaLinki P16949.

Miscellaneous databases

ChiTaRSi STMN1. human.
GeneWikii Stathmin.
GenomeRNAii 3925.
NextBioi 15415.
PROi P16949.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16949.
Bgeei P16949.
CleanExi HS_STMN1.
Genevestigatori P16949.

Family and domain databases

InterProi IPR000956. Stathmin_fam.
[Graphical view ]
PANTHERi PTHR10104. PTHR10104. 1 hit.
Pfami PF00836. Stathmin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002285. Stathmin. 1 hit.
PRINTSi PR00345. STATHMIN.
SUPFAMi SSF101494. SSF101494. 1 hit.
PROSITEi PS00563. STATHMIN_1. 1 hit.
PS01041. STATHMIN_2. 1 hit.
PS51663. STATHMIN_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTMN1_HUMAN
AccessioniPrimary (citable) accession number: P16949
Secondary accession number(s): A2A2D1
, B2R4E7, B7Z8N4, D3DPJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

External Data

Dasty 3

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