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Q9P270

- SLAI2_HUMAN

UniProt

Q9P270 - SLAI2_HUMAN

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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

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 - Biological processi

  1. cytoplasmic microtubule organization Source: UniProtKB
  2. microtubule nucleation Source: UniProtKB
  3. positive 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
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
Complete GO annotation...

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 – 431Phosphoserine2 Publications
Modified residuei48 – 481Phosphoserine2 Publications
Modified residuei63 – 631Phosphoserine1 Publication
Modified residuei147 – 1471Phosphoserine1 Publication
Modified residuei160 – 1601Phosphoserine1 Publication
Modified residuei179 – 1791Phosphoserine1 Publication
Modified residuei247 – 2471Phosphoserine1 Publication
Modified residuei250 – 2501Phosphoserine1 Publication
Modified residuei251 – 2511Phosphoserine1 Publication
Modified residuei254 – 2541Phosphoserine1 Publication
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei323 – 3231Phosphoserine1 Publication
Modified residuei377 – 3771Phosphoserine1 Publication
Modified residuei391 – 3911Phosphoserine1 Publication
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei433 – 4331Phosphoserine1 Publication
Modified residuei456 – 4561Phosphoserine1 Publication
Modified residuei462 – 4621Phosphoserine2 Publications
Modified residuei467 – 4671Phosphoserine2 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

BgeeiQ9P270.
CleanExiHS_SLAIN2.
ExpressionAtlasiQ9P270. baseline and differential.
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 – 5773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000017860.
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

        10         20         30         40         50
MEDVNSNVNA DQEVRKLQEL VKKLEKQNEQ LRSRSGAVQG AGSLGPGSPV
60 70 80 90 100
RAGASIPSSG AASPRGFPLG LSAKSGGGPG SGPRRTSSEE LRDATSLLAA
110 120 130 140 150
GEGGLLDEVE PLRPDELERL SGWEEEEESW LYSSPKKKLT PMQKSVSPLV
160 170 180 190 200
WCRQVLDYPS PDVECAKKSL IHKLDQTMSA LKRQNLYNNP FNSMSYTSPY
210 220 230 240 250
SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNLKSS DRNPPLSPQS
260 270 280 290 300
SIDSELSASE LDEDSIGSNY KLNDVTDVQI LARMQEESLR QEYAATTSRR
310 320 330 340 350
SSGSSCNSTR RGTFSDQELD AQSLDDEDDN MHHAVYPAVN RFSPSPRNSP
360 370 380 390 400
RPSPKQSPRN SPRSRSPARG IEYSRVSPQP MISRLQQPRL SLQGHPTDLQ
410 420 430 440 450
TSNVKNEEKL RRSLPNLSRT SNTQVDSVKS SRSDSNFQVP NGGIPRMQPQ
460 470 480 490 500
ASAIPSPGKF RSPAAPSPLA LRQPVKAFSN HGSGSPGSQE ITQLTQTTSS
510 520 530 540 550
PGPPMVQSTV SANPPSNINS ATLTRPAGTT AMRSGLPRPS APSAGGIPVP
560 570 580
RSKLAQPVRR SLPAPKTYGS MKDDSWKDGC Y
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. Curated
The sequence BAA95982.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00390000017860.
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

Bgeei Q9P270.
CleanExi HS_SLAIN2.
ExpressionAtlasi Q9P270. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 83 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