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Q9P270 (SLAI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SLAIN motif-containing protein 2
Gene names
Name:SLAIN2
Synonyms:KIAA1458
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Subunit structure

Interacts with CLIP1, CLIP2, CKAP5, CLASP1, MAPRE1 and MAPRE3. Ref.11

Subcellular location

Cytoplasmcytoskeleton. Note: Colocalizes with microtubules. Detected at the plus end of growing microtubules.

Tissue specificity

Widely expressed with highest levels in adult liver, testis and ovary, and lowest levels in adult pancreas and spleen and in fetal brain. Ref.1

Domain

The N-terminus forms a two-stranded coiled coil. Ref.11

Post-translational modification

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. Ref.11

Sequence similarities

Belongs to the SLAIN motif-containing family.

Sequence caution

The sequence AAH31691.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAA95982.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 581581SLAIN motif-containing protein 2
PRO_0000316965

Regions

Coiled coil4 – 3936 Ref.11
Compositional bias124 – 1285Poly-Glu

Sites

Site5811Important for interaction with CLIP1

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6 Ref.10
Modified residue431Phosphoserine Ref.4 Ref.5
Modified residue481Phosphoserine Ref.4 Ref.5
Modified residue631Phosphoserine Ref.5
Modified residue1471Phosphoserine Ref.5
Modified residue1601Phosphoserine Ref.4
Modified residue1791Phosphoserine Ref.5
Modified residue2471Phosphoserine Ref.5
Modified residue2501Phosphoserine Ref.5
Modified residue2511Phosphoserine Ref.5
Modified residue2541Phosphoserine Ref.5
Modified residue3151Phosphoserine By similarity
Modified residue3231Phosphoserine Ref.5
Modified residue3771Phosphoserine Ref.5
Modified residue3911Phosphoserine Ref.8
Modified residue4131Phosphoserine Ref.5
Modified residue4331Phosphoserine Ref.7
Modified residue4561Phosphoserine Ref.5
Modified residue4621Phosphoserine Ref.5 Ref.8
Modified residue4671Phosphoserine Ref.5 Ref.8

Experimental info

Mutagenesis5811Missing: Abolishes interaction with CLIP1. Ref.11
Sequence conflict2331N → D in BAF83695. Ref.2
Sequence conflict5581V → A in BAF83695. Ref.2

Secondary structure

... 581
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P270 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: 44B10B1BBD555B26

FASTA58162,543
        10         20         30         40         50         60 
MEDVNSNVNA DQEVRKLQEL VKKLEKQNEQ LRSRSGAVQG AGSLGPGSPV RAGASIPSSG 

        70         80         90        100        110        120 
AASPRGFPLG LSAKSGGGPG SGPRRTSSEE LRDATSLLAA GEGGLLDEVE PLRPDELERL 

       130        140        150        160        170        180 
SGWEEEEESW LYSSPKKKLT PMQKSVSPLV WCRQVLDYPS PDVECAKKSL IHKLDQTMSA 

       190        200        210        220        230        240 
LKRQNLYNNP FNSMSYTSPY SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNLKSS 

       250        260        270        280        290        300 
DRNPPLSPQS SIDSELSASE LDEDSIGSNY KLNDVTDVQI LARMQEESLR QEYAATTSRR 

       310        320        330        340        350        360 
SSGSSCNSTR RGTFSDQELD AQSLDDEDDN MHHAVYPAVN RFSPSPRNSP RPSPKQSPRN 

       370        380        390        400        410        420 
SPRSRSPARG IEYSRVSPQP MISRLQQPRL SLQGHPTDLQ TSNVKNEEKL RRSLPNLSRT 

       430        440        450        460        470        480 
SNTQVDSVKS SRSDSNFQVP NGGIPRMQPQ ASAIPSPGKF RSPAAPSPLA LRQPVKAFSN 

       490        500        510        520        530        540 
HGSGSPGSQE ITQLTQTTSS PGPPMVQSTV SANPPSNINS ATLTRPAGTT AMRSGLPRPS 

       550        560        570        580 
APSAGGIPVP RSKLAQPVRR SLPAPKTYGS MKDDSWKDGC Y 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
Tissue: Brain.
[2]"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].
[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 180-581.
Tissue: Skin.
[4]"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-43; SER-48 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"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-43; SER-48; SER-63; SER-147; SER-179; SER-247; SER-250; SER-251; SER-254; SER-323; SER-377; SER-413; SER-456; SER-462 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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-391; SER-462 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 574-581 IN COMPLEX WITH CLIP1, FUNCTION, CIRCULAR DICHROISM, COILED-COIL DOMAIN, INTERACTION WITH CLIP1; CLIP2; CLASP1; CKAP5; MAPRE1 AND MAPRE3, PHOSPHORYLATION, MUTAGENESIS OF TYR-581, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB040891 mRNA. Translation: BAA95982.1. Different initiation.
AK291006 mRNA. Translation: BAF83695.1.
BC031691 mRNA. Translation: AAH31691.2. Different initiation.
CCDSCCDS47051.1.
RefSeqNP_065897.1. NM_020846.1.
UniGeneHs.479677.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RDVX-ray1.75E/F/G/H574-581[»]
ProteinModelPortalQ9P270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121654. 11 interactions.
IntActQ9P270. 6 interactions.
MINTMINT-3306688.
STRING9606.ENSP00000264313.

PTM databases

PhosphoSiteQ9P270.

Polymorphism databases

DMDM166977679.

Proteomic databases

MaxQBQ9P270.
PaxDbQ9P270.
PRIDEQ9P270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264313; ENSP00000264313; ENSG00000109171.
GeneID57606.
KEGGhsa:57606.
UCSCuc003gya.4. human.

Organism-specific databases

CTD57606.
GeneCardsGC04P048343.
H-InvDBHIX0012487.
HGNCHGNC:29282. SLAIN2.
HPAHPA035824.
MIM610492. gene.
neXtProtNX_Q9P270.
PharmGKBPA162403457.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG29486.
HOGENOMHOG000057277.
HOVERGENHBG072961.
InParanoidQ9P270.
KOK16580.
OMAKRQNLYN.
OrthoDBEOG72ZCDW.
PhylomeDBQ9P270.
TreeFamTF331616.

Gene expression databases

ArrayExpressQ9P270.
BgeeQ9P270.
CleanExHS_SLAIN2.
GenevestigatorQ9P270.

Family and domain databases

InterProIPR026179. Slain.
[Graphical view]
PANTHERPTHR22406. PTHR22406. 1 hit.
PfamPF15301. SLAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLAIN2. human.
GenomeRNAi57606.
NextBio64235.
PROQ9P270.
SOURCESearch...

Entry information

Entry nameSLAI2_HUMAN
AccessionPrimary (citable) accession number: Q9P270
Secondary accession number(s): A8K4P1, Q8N5R3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 81 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM