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Protein

SLAIN motif-containing protein 2

Gene

Slain2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Required for normal structure of the microtubule cytoskeleton during interphase.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei581 – 5811Important for interaction with CLIP1By similarity

GO - Biological processi

  • cytoplasmic microtubule organization Source: UniProtKB
  • microtubule nucleation Source: UniProtKB
  • positive regulation of microtubule polymerization Source: UniProtKB
  • regulation of microtubule polymerization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SLAIN motif-containing protein 2
Gene namesi
Name:Slain2
Synonyms:Kiaa1458
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1923241. Slain2.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity

  • Note: Colocalizes with microtubules. Detected at the plus end of growing microtubules (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 581581SLAIN motif-containing protein 2PRO_0000316967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei63 – 631PhosphoserineCombined sources
Modified residuei88 – 881PhosphoserineCombined sources
Modified residuei147 – 1471PhosphoserineCombined sources
Modified residuei160 – 1601PhosphoserineBy similarity
Modified residuei179 – 1791PhosphoserineBy similarity
Modified residuei248 – 2481PhosphoserineCombined sources
Modified residuei251 – 2511PhosphoserineBy similarity
Modified residuei252 – 2521PhosphoserineBy similarity
Modified residuei255 – 2551PhosphoserineBy similarity
Modified residuei316 – 3161PhosphoserineCombined sources
Modified residuei324 – 3241PhosphoserineCombined sources
Modified residuei378 – 3781PhosphoserineBy similarity
Modified residuei392 – 3921PhosphoserineBy similarity
Modified residuei414 – 4141PhosphoserineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei457 – 4571PhosphoserineBy similarity
Modified residuei463 – 4631PhosphoserineBy similarity
Modified residuei468 – 4681PhosphoserineBy similarity

Post-translational modificationi

Is highly phosphorylated during mitosis, but not during interphase. The highly phosphorylated form does not localize at microtubule plus ends and does not interact with MAPRE1 or CKAP5 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CI08.
MaxQBiQ8CI08.
PaxDbiQ8CI08.
PRIDEiQ8CI08.

PTM databases

iPTMnetiQ8CI08.
PhosphoSiteiQ8CI08.

Expressioni

Gene expression databases

BgeeiQ8CI08.
CleanExiMM_SLAIN2.
ExpressionAtlasiQ8CI08. baseline and differential.
GenevisibleiQ8CI08. MM.

Interactioni

Subunit structurei

Interacts with CLIP1, CLIP2, CKAP5, CLASP1, MAPRE1 and MAPRE3.By similarity

Protein-protein interaction databases

BioGridi217891. 6 interactions.
IntActiQ8CI08. 7 interactions.
STRINGi10090.ENSMUSP00000115871.

Structurei

3D structure databases

ProteinModelPortaliQ8CI08.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili4 – 3936Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi124 – 1285Poly-Glu

Domaini

The N-terminus forms a two-stranded coiled coil.By similarity

Sequence similaritiesi

Belongs to the SLAIN motif-containing family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IF0R. Eukaryota.
ENOG410XPVV. LUCA.
GeneTreeiENSGT00390000017860.
HOGENOMiHOG000057277.
HOVERGENiHBG072961.
InParanoidiQ8CI08.
KOiK16580.
OMAiKDESWKD.
OrthoDBiEOG72ZCDW.
PhylomeDBiQ8CI08.
TreeFamiTF331616.

Family and domain databases

InterProiIPR026179. Slain.
[Graphical view]
PANTHERiPTHR22406. PTHR22406. 1 hit.
PfamiPF15301. SLAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8CI08-1) [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
MEDVNSNVNA DQEVRKLQEL VKKLEKQNEQ LRSRSGAVQG AGLLGPGSPA
60 70 80 90 100
RVGVSTPSSG AASPRGFPLG LGAKASGGAG SGPRRTSSED LRDATSLLAA
110 120 130 140 150
GEGGLLDEVE PLRPDELERL SGWEEEEESW LYSSPKKKLT PMQKSVSPLV
160 170 180 190 200
WCRQVLDYPS PDVECAKKSL IHKLDQTMSA LKRQNLYNNP FNSVSYSNSY
210 220 230 240 250
SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNFKSS SDRNPPLSPQ
260 270 280 290 300
SSIDSELSAS ELDEDSIGSN YKLNDVTDVQ ILARMQEESL RQEYAASTSR
310 320 330 340 350
RSSGSSCNST RRGTFSDQEL DAQSLDDEDD SLQHAVHPAL NRFSPSPRNS
360 370 380 390 400
PRPSPKQSPR NSPRSRSPAR GIEYSRASPQ PMISRLQQPR LSLQGHPTDL
410 420 430 440 450
QTSNVKNEEK LRRSLPNLSR TSSTQVDSVK SSRSDSNFQV PNGGIPRMQP
460 470 480 490 500
QASAIPSPGK FRSPAAPSPL ALRQPVKAFS NHGSGSGSQE TTQFTQTTSS
510 520 530 540 550
PGPPVVQNSA PANPSSNINS ATLTRPAGTT AMRSGLPRPS APSAGGIPVP
560 570 580
RSKLVQPVRR SLPAPKSYGS MKDDSWKDGC Y
Length:581
Mass (Da):62,378
Last modified:February 5, 2008 - v2
Checksum:i1C412715B6E313DC
GO
Isoform 2 (identifier: Q8CI08-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-455: AI → ATSQRLKSLPRTSLKAKQLLPTSSTKRV

Show »
Length:607
Mass (Da):65,272
Checksum:iF7EBA67F8A740E48
GO

Sequence cautioni

The sequence AAH10836.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH10836.1 differs from that shown.Contaminating sequence. Potential vector sequence.Curated
The sequence AAH38019.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC98175.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE27166.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti462 – 4621R → H in BAE27166 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 4552AI → ATSQRLKSLPRTSLKAKQLL PTSSTKRV in isoform 2. 1 PublicationVSP_030834

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129365 mRNA. Translation: BAC98175.1. Different initiation.
AK146432 mRNA. Translation: BAE27166.1. Different initiation.
BC010836 mRNA. Translation: AAH10836.1. Sequence problems.
BC038019 mRNA. Translation: AAH38019.1. Sequence problems.
CCDSiCCDS19335.2. [Q8CI08-2]
CCDS51517.1. [Q8CI08-1]
RefSeqiNP_001106894.1. NM_001113423.2. [Q8CI08-1]
NP_705795.2. NM_153567.3. [Q8CI08-2]
UniGeneiMm.121285.

Genome annotation databases

EnsembliENSMUST00000143829; ENSMUSP00000115871; ENSMUSG00000036087. [Q8CI08-2]
ENSMUST00000144843; ENSMUSP00000116528; ENSMUSG00000036087. [Q8CI08-1]
GeneIDi75991.
KEGGimmu:75991.
UCSCiuc008xsh.3. mouse. [Q8CI08-1]
uc008xsi.1. mouse. [Q8CI08-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129365 mRNA. Translation: BAC98175.1. Different initiation.
AK146432 mRNA. Translation: BAE27166.1. Different initiation.
BC010836 mRNA. Translation: AAH10836.1. Sequence problems.
BC038019 mRNA. Translation: AAH38019.1. Sequence problems.
CCDSiCCDS19335.2. [Q8CI08-2]
CCDS51517.1. [Q8CI08-1]
RefSeqiNP_001106894.1. NM_001113423.2. [Q8CI08-1]
NP_705795.2. NM_153567.3. [Q8CI08-2]
UniGeneiMm.121285.

3D structure databases

ProteinModelPortaliQ8CI08.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217891. 6 interactions.
IntActiQ8CI08. 7 interactions.
STRINGi10090.ENSMUSP00000115871.

PTM databases

iPTMnetiQ8CI08.
PhosphoSiteiQ8CI08.

Proteomic databases

EPDiQ8CI08.
MaxQBiQ8CI08.
PaxDbiQ8CI08.
PRIDEiQ8CI08.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000143829; ENSMUSP00000115871; ENSMUSG00000036087. [Q8CI08-2]
ENSMUST00000144843; ENSMUSP00000116528; ENSMUSG00000036087. [Q8CI08-1]
GeneIDi75991.
KEGGimmu:75991.
UCSCiuc008xsh.3. mouse. [Q8CI08-1]
uc008xsi.1. mouse. [Q8CI08-2]

Organism-specific databases

CTDi57606.
MGIiMGI:1923241. Slain2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IF0R. Eukaryota.
ENOG410XPVV. LUCA.
GeneTreeiENSGT00390000017860.
HOGENOMiHOG000057277.
HOVERGENiHBG072961.
InParanoidiQ8CI08.
KOiK16580.
OMAiKDESWKD.
OrthoDBiEOG72ZCDW.
PhylomeDBiQ8CI08.
TreeFamiTF331616.

Miscellaneous databases

PROiQ8CI08.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CI08.
CleanExiMM_SLAIN2.
ExpressionAtlasiQ8CI08. baseline and differential.
GenevisibleiQ8CI08. MM.

Family and domain databases

InterProiIPR026179. Slain.
[Graphical view]
PANTHERiPTHR22406. PTHR22406. 1 hit.
PfamiPF15301. SLAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: DBA/2J.
  3. "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] OF 1-406 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-581 (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Kidney and Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-88; SER-147; SER-248; SER-316 AND SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  7. "SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase."
    van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M., Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O., Akhmanova A.
    J. Cell Biol. 193:1083-1099(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLIP1 AND MAPRE1, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSLAI2_MOUSE
AccessioniPrimary (citable) accession number: Q8CI08
Secondary accession number(s): Q05DK1, Q3UJI9, Q6ZPQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: June 8, 2016
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.