Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9P270

- SLAI2_HUMAN

UniProt

Q9P270 - SLAI2_HUMAN

Protein

SLAIN motif-containing protein 2

Gene

SLAIN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 CLIP1

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cytoplasmic microtubule organization Source: UniProtKB
    2. microtubule nucleation Source: UniProtKB
    3. positive regulation of microtubule polymerization Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SLAIN motif-containing protein 2
    Gene namesi
    Name:SLAIN2
    Synonyms:KIAA1458
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:29282. SLAIN2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: HPA
    3. microtubule cytoskeleton Source: UniProtKB
    4. nucleolus Source: HPA
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi581 – 5811Missing: Abolishes interaction with CLIP1. 1 Publication

    Organism-specific databases

    PharmGKBiPA162403457.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 581581SLAIN motif-containing protein 2PRO_0000316965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei43 – 431Phosphoserine3 Publications
    Modified residuei48 – 481Phosphoserine3 Publications
    Modified residuei63 – 631Phosphoserine2 Publications
    Modified residuei147 – 1471Phosphoserine2 Publications
    Modified residuei160 – 1601Phosphoserine2 Publications
    Modified residuei179 – 1791Phosphoserine2 Publications
    Modified residuei247 – 2471Phosphoserine2 Publications
    Modified residuei250 – 2501Phosphoserine2 Publications
    Modified residuei251 – 2511Phosphoserine2 Publications
    Modified residuei254 – 2541Phosphoserine2 Publications
    Modified residuei315 – 3151PhosphoserineBy similarity
    Modified residuei323 – 3231Phosphoserine2 Publications
    Modified residuei377 – 3771Phosphoserine2 Publications
    Modified residuei391 – 3911Phosphoserine2 Publications
    Modified residuei413 – 4131Phosphoserine2 Publications
    Modified residuei433 – 4331Phosphoserine2 Publications
    Modified residuei456 – 4561Phosphoserine2 Publications
    Modified residuei462 – 4621Phosphoserine3 Publications
    Modified residuei467 – 4671Phosphoserine3 Publications

    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 CKAP5.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9P270.
    PaxDbiQ9P270.
    PRIDEiQ9P270.

    PTM databases

    PhosphoSiteiQ9P270.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ9P270.
    BgeeiQ9P270.
    CleanExiHS_SLAIN2.
    GenevestigatoriQ9P270.

    Organism-specific databases

    HPAiHPA035824.

    Interactioni

    Subunit structurei

    Interacts with CLIP1, CLIP2, CKAP5, CLASP1, MAPRE1 and MAPRE3.1 Publication

    Protein-protein interaction databases

    BioGridi121654. 12 interactions.
    IntActiQ9P270. 6 interactions.
    MINTiMINT-3306688.
    STRINGi9606.ENSP00000264313.

    Structurei

    Secondary structure

    1
    581
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi575 – 5773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RDVX-ray1.75E/F/G/H574-581[»]
    ProteinModelPortaliQ9P270.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili4 – 39361 PublicationAdd
    BLAST

    Compositional bias

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

    Domaini

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

    Sequence similaritiesi

    Belongs to the SLAIN motif-containing family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG29486.
    HOGENOMiHOG000057277.
    HOVERGENiHBG072961.
    InParanoidiQ9P270.
    KOiK16580.
    OMAiKRQNLYN.
    OrthoDBiEOG72ZCDW.
    PhylomeDBiQ9P270.
    TreeFamiTF331616.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q9P270-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDVNSNVNA DQEVRKLQEL VKKLEKQNEQ LRSRSGAVQG AGSLGPGSPV    50
    RAGASIPSSG AASPRGFPLG LSAKSGGGPG SGPRRTSSEE LRDATSLLAA 100
    GEGGLLDEVE PLRPDELERL SGWEEEEESW LYSSPKKKLT PMQKSVSPLV 150
    WCRQVLDYPS PDVECAKKSL IHKLDQTMSA LKRQNLYNNP FNSMSYTSPY 200
    SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNLKSS DRNPPLSPQS 250
    SIDSELSASE LDEDSIGSNY KLNDVTDVQI LARMQEESLR QEYAATTSRR 300
    SSGSSCNSTR RGTFSDQELD AQSLDDEDDN MHHAVYPAVN RFSPSPRNSP 350
    RPSPKQSPRN SPRSRSPARG IEYSRVSPQP MISRLQQPRL SLQGHPTDLQ 400
    TSNVKNEEKL RRSLPNLSRT SNTQVDSVKS SRSDSNFQVP NGGIPRMQPQ 450
    ASAIPSPGKF RSPAAPSPLA LRQPVKAFSN HGSGSPGSQE ITQLTQTTSS 500
    PGPPMVQSTV SANPPSNINS ATLTRPAGTT AMRSGLPRPS APSAGGIPVP 550
    RSKLAQPVRR SLPAPKTYGS MKDDSWKDGC Y 581
    Length:581
    Mass (Da):62,543
    Last modified:February 5, 2008 - v2
    Checksum:i44B10B1BBD555B26
    GO

    Sequence cautioni

    The sequence AAH31691.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA95982.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti233 – 2331N → D in BAF83695. (PubMed:14702039)Curated
    Sequence conflicti558 – 5581V → A in BAF83695. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040891 mRNA. Translation: BAA95982.1. Different initiation.
    AK291006 mRNA. Translation: BAF83695.1.
    BC031691 mRNA. Translation: AAH31691.2. Different initiation.
    CCDSiCCDS47051.1.
    RefSeqiNP_065897.1. NM_020846.1.
    UniGeneiHs.479677.

    Genome annotation databases

    EnsembliENST00000264313; ENSP00000264313; ENSG00000109171.
    GeneIDi57606.
    KEGGihsa:57606.
    UCSCiuc003gya.4. human.

    Polymorphism databases

    DMDMi166977679.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040891 mRNA. Translation: BAA95982.1 . Different initiation.
    AK291006 mRNA. Translation: BAF83695.1 .
    BC031691 mRNA. Translation: AAH31691.2 . Different initiation.
    CCDSi CCDS47051.1.
    RefSeqi NP_065897.1. NM_020846.1.
    UniGenei Hs.479677.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RDV X-ray 1.75 E/F/G/H 574-581 [» ]
    ProteinModelPortali Q9P270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121654. 12 interactions.
    IntActi Q9P270. 6 interactions.
    MINTi MINT-3306688.
    STRINGi 9606.ENSP00000264313.

    PTM databases

    PhosphoSitei Q9P270.

    Polymorphism databases

    DMDMi 166977679.

    Proteomic databases

    MaxQBi Q9P270.
    PaxDbi Q9P270.
    PRIDEi Q9P270.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264313 ; ENSP00000264313 ; ENSG00000109171 .
    GeneIDi 57606.
    KEGGi hsa:57606.
    UCSCi uc003gya.4. human.

    Organism-specific databases

    CTDi 57606.
    GeneCardsi GC04P048343.
    H-InvDB HIX0012487.
    HGNCi HGNC:29282. SLAIN2.
    HPAi HPA035824.
    MIMi 610492. gene.
    neXtProti NX_Q9P270.
    PharmGKBi PA162403457.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG29486.
    HOGENOMi HOG000057277.
    HOVERGENi HBG072961.
    InParanoidi Q9P270.
    KOi K16580.
    OMAi KRQNLYN.
    OrthoDBi EOG72ZCDW.
    PhylomeDBi Q9P270.
    TreeFami TF331616.

    Miscellaneous databases

    ChiTaRSi SLAIN2. human.
    GenomeRNAii 57606.
    NextBioi 64235.
    PROi Q9P270.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P270.
    Bgeei Q9P270.
    CleanExi HS_SLAIN2.
    Genevestigatori Q9P270.

    Family and domain databases

    InterProi IPR026179. Slain.
    [Graphical view ]
    PANTHERi PTHR22406. PTHR22406. 1 hit.
    Pfami PF15301. SLAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiSLAI2_HUMAN
    AccessioniPrimary (citable) accession number: Q9P270
    Secondary accession number(s): A8K4P1, Q8N5R3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 82 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3