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Protein

CLIP-associating protein 2

Gene

CLASP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.8 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • dystroglycan binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • protein tyrosine kinase binding Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • establishment or maintenance of cell polarity Source: UniProtKB
  • exit from mitosis Source: UniProtKB
  • Golgi organization Source: UniProtKB
  • microtubule anchoring Source: UniProtKB
  • microtubule cytoskeleton organization Source: UniProtKB
  • microtubule nucleation Source: UniProtKB
  • microtubule organizing center organization Source: UniProtKB
  • mitotic spindle organization Source: UniProtKB
  • negative regulation of focal adhesion assembly Source: UniProtKB
  • negative regulation of microtubule depolymerization Source: UniProtKB
  • negative regulation of stress fiber assembly Source: UniProtKB
  • negative regulation of wound healing, spreading of epidermal cells Source: UniProtKB
  • platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  • positive regulation of basement membrane assembly involved in embryonic body morphogenesis Source: UniProtKB
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of exocytosis Source: UniProtKB
  • positive regulation of extracellular matrix disassembly Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of axon extension Source: UniProtKB
  • regulation of epithelial to mesenchymal transition Source: UniProtKB
  • regulation of gastrulation Source: UniProtKB
  • regulation of microtubule-based process Source: UniProtKB
  • regulation of microtubule polymerization Source: UniProtKB
  • regulation of microtubule polymerization or depolymerization Source: UniProtKB
  • sister chromatid cohesion Source: Reactome
  • vesicle targeting Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-428890. Role of Abl in Robo-Slit signaling.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
CLIP-associating protein 2
Alternative name(s):
Cytoplasmic linker-associated protein 2
Protein Orbit homolog 2
Short name:
hOrbit2
Gene namesi
Name:CLASP2
Synonyms:KIAA0627
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:17078. CLASP2.

Subcellular locationi

GO - Cellular componenti

  • axonal growth cone Source: UniProtKB
  • basal cortex Source: UniProtKB
  • cell cortex Source: MGI
  • cell leading edge Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cortical microtubule plus-end Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic microtubule Source: UniProtKB
  • cytosol Source: Reactome
  • Golgi apparatus Source: UniProtKB
  • kinetochore microtubule Source: UniProtKB
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB
  • microtubule organizing center Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • ruffle membrane Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Kinetochore, Membrane, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106W → E: Decreases affinity for microtubules; when associated with A-191; E-667; E-833; A-838 and A-839. 1 Publication1
Mutagenesisi191K → A: Decreases affinity for microtubules; when associated with E-106; E-667; E-833; A-838 and A-839. 1 Publication1
Mutagenesisi496 – 497IP → AA: No effect on MAPRE1 binding. Abolishes interaction with MAPRE1; when associated with 519-A-A-520. 1 Publication2
Mutagenesisi496 – 497IP → SS: Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 519-S-S-520. 1 Publication2
Mutagenesisi499S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-503; D-507; D-525; D-529; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi503S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-507; D-525; D-529; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi507S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-525; D-529; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi519 – 520IP → AA: No effect on MAPRE1 binding. Abolishes interaction with MAPRE1; when associated with 496-A-A-497. 1 Publication2
Mutagenesisi519 – 520IP → SS: Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 496-S-S-497. 1 Publication2
Mutagenesisi525S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-529; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi529S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-533; D-537 and D-541. 1 Publication1
Mutagenesisi533S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-537 and D-541. 1 Publication1
Mutagenesisi537S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-533 and D-541. 1 Publication1
Mutagenesisi541S → D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-533 and D-537. 1 Publication1
Mutagenesisi667W → E: Decreases affinity for microtubules; when associated with E-106; A-191; E-833; A-838 and A-839. 1 Publication1
Mutagenesisi833K → E: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; A-838 and A-839. 1 Publication1
Mutagenesisi838R → A: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; E-833 and A-839. 1 Publication1
Mutagenesisi839K → A: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; E-833 and A-838. 1 Publication1

Organism-specific databases

DisGeNETi23122.
PharmGKBiPA38435.

Polymorphism and mutation databases

BioMutaiCLASP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000898491 – 1294CLIP-associating protein 2Add BLAST1294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8PhosphoserineCombined sources1
Modified residuei14PhosphoserineBy similarity1
Modified residuei316PhosphoserineCombined sources1
Modified residuei327PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei360PhosphoserineCombined sources1
Modified residuei368PhosphoserineBy similarity1
Modified residuei370PhosphoserineCombined sources1
Modified residuei407PhosphoserineBy similarity1
Modified residuei455PhosphoserineCombined sources1
Modified residuei459PhosphoserineCombined sources1
Modified residuei463PhosphoserineCombined sources1
Modified residuei478PhosphoserineCombined sources1
Modified residuei489PhosphoserineCombined sources1
Modified residuei507PhosphoserineCombined sources1
Modified residuei525PhosphoserineCombined sources1
Modified residuei529PhosphoserineCombined sources1
Modified residuei585PhosphoserineCombined sources1
Modified residuei587PhosphoserineCombined sources1
Modified residuei596PhosphoserineCombined sources1
Modified residuei621PhosphoserineCombined sources1
Modified residuei627PhosphoserineBy similarity1
Modified residuei787PhosphothreonineCombined sources1
Modified residuei892PhosphoserineCombined sources1
Modified residuei952PhosphoserineCombined sources1
Modified residuei955PhosphoserineCombined sources1
Modified residuei1013PhosphoserineCombined sources1
Modified residuei1029PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by GSK3B. Phosphorylation reduces MAPRE1 binding (PubMed:26003921). Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella.1 Publication1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO75122.
MaxQBiO75122.
PaxDbiO75122.
PeptideAtlasiO75122.
PRIDEiO75122.

PTM databases

iPTMnetiO75122.
PhosphoSitePlusiO75122.

Expressioni

Tissue specificityi

Brain-specific.

Gene expression databases

BgeeiENSG00000163539.
CleanExiHS_CLASP2.
ExpressionAtlasiO75122. baseline and differential.
GenevisibleiO75122. HS.

Organism-specific databases

HPAiHPA059476.

Interactioni

Subunit structurei

Interacts with microtubules (PubMed:11290329, PubMed:15631994, PubMed:15955847, PubMed:26003921). Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends (PubMed:15631994, PubMed:19632184, PubMed:26003921). Interacts with CLIP2, ERC1, MAPRE3, PHLDB2 and RSN (PubMed:11290329, PubMed:15631994). The interaction with ERC1 may be mediated by PHLDB2 (PubMed:16824950). Interacts with GCC2; recruits CLASP2 to Golgi membranes (PubMed:17543864). Interacts with MACF1 (By similarity).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Clip2O551563EBI-913524,EBI-349416From a different organism.
MAPRE1Q156913EBI-913524,EBI-1004115

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • dystroglycan binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • protein tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116743. 42 interactors.
DIPiDIP-36804N.
IntActiO75122. 27 interactors.
MINTiMINT-4526878.
STRINGi9606.ENSP00000419974.

Structurei

Secondary structure

11294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi64 – 75Combined sources12
Helixi85 – 100Combined sources16
Helixi106 – 121Combined sources16
Helixi124 – 126Combined sources3
Helixi128 – 136Combined sources9
Helixi138 – 144Combined sources7
Helixi150 – 167Combined sources18
Helixi168 – 171Combined sources4
Helixi172 – 185Combined sources14
Helixi191 – 207Combined sources17
Helixi213 – 220Combined sources8
Helixi226 – 242Combined sources17
Helixi245 – 248Combined sources4
Helixi249 – 251Combined sources3
Helixi252 – 263Combined sources12
Helixi268 – 284Combined sources17
Helixi286 – 294Combined sources9
Helixi298 – 303Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WOYX-ray2.10A60-310[»]
ProteinModelPortaliO75122.
SMRiO75122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati173 – 208HEAT 1Sequence analysisAdd BLAST36
Repeati209 – 245HEAT 2Sequence analysisAdd BLAST37
Repeati250 – 287HEAT 3Sequence analysisAdd BLAST38
Repeati710 – 747HEAT 4Sequence analysisAdd BLAST38
Repeati772 – 809HEAT 5Sequence analysisAdd BLAST38
Repeati1054 – 1091HEAT 6Sequence analysisAdd BLAST38
Repeati1098 – 1135HEAT 7Sequence analysisAdd BLAST38
Repeati1216 – 1253HEAT 8Sequence analysisAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 311TOG 11 PublicationAdd BLAST252
Regioni444 – 580Interaction with microtubules, MAPRE1 and MAPRE31 PublicationAdd BLAST137
Regioni649 – 881TOG 21 PublicationAdd BLAST233
Regioni872 – 1294Interaction with RSN and localization to the Golgi and kinetochoresAdd BLAST423
Regioni1017 – 1294Required for cortical localizationAdd BLAST278

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi494 – 497SXIP motif 1; mediates interaction with MAPRE1 and targeting to microtubule plus ends2 Publications4
Motifi517 – 520SXIP motif 2; mediates interaction with MAPRE1 and targeting to microtubule plus ends2 Publications4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi310 – 587Ser-richAdd BLAST278
Compositional biasi1104 – 1108Poly-Leu5

Domaini

The two SXIP sequence motifs mediate interaction with MAPRE1; this is necessary for targeting to growing microtubule plus ends.1 Publication
Two TOG regions display structural characteristics similar to HEAT repeat domains and mediate interaction with microtubules.1 Publication

Sequence similaritiesi

Belongs to the CLASP family.Curated
Contains 8 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2956. Eukaryota.
ENOG410ZMY0. LUCA.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiO75122.
KOiK16578.
OrthoDBiEOG091G0GTV.
PhylomeDBiO75122.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view]
PfamiPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms exist.
Isoform 1 (identifier: O75122-1) [UniParc]FASTAAdd to basket
Also known as: CLASP2 gamma

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
MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTSGNPAN SARKPGSAGG
60 70 80 90 100
PKVGGASKEG GAGAVDEDDF IKAFTDVPSI QIYSSRELEE TLNKIREILS
110 120 130 140 150
DDKHDWDQRA NALKKIRSLL VAGAAQYDCF FQHLRLLDGA LKLSAKDLRS
160 170 180 190 200
QVVREACITV AHLSTVLGNK FDHGAEAIVP TLFNLVPNSA KVMATSGCAA
210 220 230 240 250
IRFIIRHTHV PRLIPLITSN CTSKSVPVRR RSFEFLDLLL QEWQTHSLER
260 270 280 290 300
HAAVLVETIK KGIHDADAEA RVEARKTYMG LRNHFPGEAE TLYNSLEPSY
310 320 330 340 350
QKSLQTYLKS SGSVASLPQS DRSSSSSQES LNRPFSSKWS TANPSTVAGR
360 370 380 390 400
VSAGSSKASS LPGSLQRSRS DIDVNAAAGA KAHHAAGQSV RRGRLGAGAL
410 420 430 440 450
NAGSYASLED TSDKLDGTAS EDGRVRAKLS APLAGMGNAK ADSRGRSRTK
460 470 480 490 500
MVSQSQPGSR SGSPGRVLTT TALSTVSSGV QRVLVNSASA QKRSKIPRSQ
510 520 530 540 550
GCSREASPSR LSVARSSRIP RPSVSQGCSR EASRESSRDT SPVRSFQPLA
560 570 580 590 600
SRHHSRSTGA LYAPEVYGAS GPGYGISQSS RLSSSVSAMR VLNTGSDVEE
610 620 630 640 650
AVADALKKPA RRRYESYGMH SDDDANSDAS SACSERSYSS RNGSIPTYMR
660 670 680 690 700
QTEDVAEVLN RCASSNWSER KEGLLGLQNL LKNQRTLSRV ELKRLCEIFT
710 720 730 740 750
RMFADPHGKR VFSMFLETLV DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL
760 770 780 790 800
GSVQAKVQKA LDVTRESFPN DLQFNILMRF TVDQTQTPSL KVKVAILKYI
810 820 830 840 850
ETLAKQMDPG DFINSSETRL AVSRVITWTT EPKSSDVRKA AQSVLISLFE
860 870 880 890 900
LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM GSPLTRPTPR
910 920 930 940 950
SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN
960 970 980 990 1000
FSFRSQEDMN EPLKRDSKKD DGDSMCGGPG MSDPRAGGDA TDSSQTALDN
1010 1020 1030 1040 1050
KASLLHSMPT HSSPRSRDYN PYNYSDSISP FNKSALKEAM FDDDADQFPD
1060 1070 1080 1090 1100
DLSLDHSDLV AELLKELSNH NERVEERKIA LYELMKLTQE ESFSVWDEHF
1110 1120 1130 1140 1150
KTILLLLLET LGDKEPTIRA LALKVLREIL RHQPARFKNY AELTVMKTLE
1160 1170 1180 1190 1200
AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA DYPINLAAIK
1210 1220 1230 1240 1250
MQTKVIERVS KETLNLLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV
1260 1270 1280 1290
IGDELKPHLS QLTGSKMKLL NLYIKRAQTG SGGADPTTDV SGQS
Length:1,294
Mass (Da):141,133
Last modified:October 11, 2005 - v2
Checksum:iE4FF7E06049E65E5
GO
Isoform 2 (identifier: O75122-2) [UniParc]FASTAAdd to basket
Also known as: CLASP2 beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MAMGDD → MRRLICKRICDY
     410-425: DTSDKLDGTASEDGRV → CEAFWRSGRTAKLYSV
     426-1294: Missing.

Show »
Length:431
Mass (Da):46,585
Checksum:i5C5C731ECD32FFEB
GO
Isoform 3 (identifier: O75122-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MAMGD → MEPRSMEYFC...SGGMILSVCK
     54-54: G → GA
     550-570: Missing.
     606-606: L → LLLGDIRTK

Note: No experimental confirmation available.
Show »
Length:1,515
Mass (Da):165,924
Checksum:iDEA3BC38A9E35DF5
GO

Sequence cautioni

The sequence BAA31602 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB14995 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti392R → S in BAA31602 (PubMed:9734811).Curated1
Sequence conflicti392R → S in AAH29035 (PubMed:15489334).Curated1
Sequence conflicti392R → S in AAI40779 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0158051 – 6MAMGDD → MRRLICKRICDY in isoform 2. 2 Publications6
Alternative sequenceiVSP_0572731 – 5MAMGD → MEPRSMEYFCAQVQQKDVGG RLQVGQELLLYLGAPGAISD LEEDLGRLGKTVDALTGWVG SSNYRVSLMGLEILSAFVDR LSTRFKSYVAMVIVALIDRM GDAKDKVRDEAQTLILKLMD QVAPPMYIWEQLASGFKHKN FRSREGVCLCLIETLNIFGA QPLVISKLIPHLCILFGDSN SQVRDAAILAIVEIYRHVGE KVRMDLYKRGIPPARLEMIF AKFDEVQSSGGMILSVCK in isoform 3. 1 Publication5
Alternative sequenceiVSP_05727454G → GA in isoform 3. 1 Publication1
Alternative sequenceiVSP_015806410 – 425DTSDK…EDGRV → CEAFWRSGRTAKLYSV in isoform 2. 2 PublicationsAdd BLAST16
Alternative sequenceiVSP_015807426 – 1294Missing in isoform 2. 2 PublicationsAdd BLAST869
Alternative sequenceiVSP_057275550 – 570Missing in isoform 3. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_057276606L → LLLGDIRTK in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014527 mRNA. Translation: BAA31602.2. Different initiation.
AC093114 Genomic DNA. No translation available.
AC113170 Genomic DNA. No translation available.
AC132515 Genomic DNA. No translation available.
BC029035 mRNA. Translation: AAH29035.1.
BC140778 mRNA. Translation: AAI40779.1.
AJ288058 mRNA. Translation: CAC35157.1.
AJ288059 mRNA. Translation: CAC35158.1.
AL137636 mRNA. Translation: CAB70852.1.
AK024770 mRNA. Translation: BAB14995.1. Different initiation.
PIRiT00386.
RefSeqiNP_001193973.1. NM_001207044.1.
NP_055912.2. NM_015097.2.
UniGeneiHs.108614.

Genome annotation databases

EnsembliENST00000313350; ENSP00000324364; ENSG00000163539.
ENST00000359576; ENSP00000352581; ENSG00000163539.
GeneIDi23122.
KEGGihsa:23122.
UCSCiuc003cfv.4. human. [O75122-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014527 mRNA. Translation: BAA31602.2. Different initiation.
AC093114 Genomic DNA. No translation available.
AC113170 Genomic DNA. No translation available.
AC132515 Genomic DNA. No translation available.
BC029035 mRNA. Translation: AAH29035.1.
BC140778 mRNA. Translation: AAI40779.1.
AJ288058 mRNA. Translation: CAC35157.1.
AJ288059 mRNA. Translation: CAC35158.1.
AL137636 mRNA. Translation: CAB70852.1.
AK024770 mRNA. Translation: BAB14995.1. Different initiation.
PIRiT00386.
RefSeqiNP_001193973.1. NM_001207044.1.
NP_055912.2. NM_015097.2.
UniGeneiHs.108614.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WOYX-ray2.10A60-310[»]
ProteinModelPortaliO75122.
SMRiO75122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116743. 42 interactors.
DIPiDIP-36804N.
IntActiO75122. 27 interactors.
MINTiMINT-4526878.
STRINGi9606.ENSP00000419974.

PTM databases

iPTMnetiO75122.
PhosphoSitePlusiO75122.

Polymorphism and mutation databases

BioMutaiCLASP2.

Proteomic databases

EPDiO75122.
MaxQBiO75122.
PaxDbiO75122.
PeptideAtlasiO75122.
PRIDEiO75122.

Protocols and materials databases

DNASUi23122.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313350; ENSP00000324364; ENSG00000163539.
ENST00000359576; ENSP00000352581; ENSG00000163539.
GeneIDi23122.
KEGGihsa:23122.
UCSCiuc003cfv.4. human. [O75122-1]

Organism-specific databases

CTDi23122.
DisGeNETi23122.
GeneCardsiCLASP2.
HGNCiHGNC:17078. CLASP2.
HPAiHPA059476.
MIMi605853. gene.
neXtProtiNX_O75122.
PharmGKBiPA38435.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2956. Eukaryota.
ENOG410ZMY0. LUCA.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiO75122.
KOiK16578.
OrthoDBiEOG091G0GTV.
PhylomeDBiO75122.

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-428890. Role of Abl in Robo-Slit signaling.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiCLASP2. human.
GeneWikiiCLASP2.
GenomeRNAii23122.
PROiO75122.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163539.
CleanExiHS_CLASP2.
ExpressionAtlasiO75122. baseline and differential.
GenevisibleiO75122. HS.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view]
PfamiPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
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Entry informationi

Entry nameiCLAP2_HUMAN
AccessioniPrimary (citable) accession number: O75122
Secondary accession number(s): B2RTR1
, F5H604, Q7L8F6, Q8N6R6, Q9BQT3, Q9BQT4, Q9H7A3, Q9NSZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: November 30, 2016
This is version 146 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 3
    Human chromosome 3: 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

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.