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Protein

Spermatogenesis-associated protein 13

Gene

SPATA13

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

Functioni

Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Regulates cell migration and adhesion assembly and disassembly through a RAC1, PI3K, RHOA and AKT1-dependent mechanism. Increases both RAC1 and CDC42 activity, but decreases the amount of active RHOA. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Involved in tumor angiogenesis and may play a role in intestinal adenoma formation and tumor progression.5 Publications

Enzyme regulationi

Both the ABR and the SH3 domains contribute to maintaining the protein in an inhibited conformation by associating with the C-terminal tail. Binding of these domains to the C-terminal tail inhibits the activity of the protein by blocking a region that is required for its GEF activity.1 Publication

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: UniProtKB
  • Rac guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

  • cell migration Source: UniProtKB
  • filopodium assembly Source: UniProtKB
  • lamellipodium assembly Source: UniProtKB
  • regulation of cell migration Source: UniProtKB
  • regulation of Rho protein signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Names & Taxonomyi

Protein namesi
Recommended name:
Spermatogenesis-associated protein 13
Alternative name(s):
APC-stimulated guanine nucleotide exchange factor 2
Short name:
Asef2
Gene namesi
Name:SPATA13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:23222. SPATA13.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • filopodium Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • nucleoplasm Source: HPA
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134912609.

Polymorphism and mutation databases

BioMutaiSPATA13.
DMDMi74752049.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 652652Spermatogenesis-associated protein 13PRO_0000278448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei114 – 1141PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96N96.
MaxQBiQ96N96.
PaxDbiQ96N96.
PeptideAtlasiQ96N96.
PRIDEiQ96N96.

PTM databases

iPTMnetiQ96N96.

Expressioni

Tissue specificityi

Expressed at high levels in the placenta, spleen and kidney, at moderate levels in lung, small intestine, liver, brain and heart, and at low levels in skeletal muscle. Expression is aberrantly enhanced in most colorectal tumors.3 Publications

Gene expression databases

BgeeiQ96N96.
CleanExiHS_SPATA13.
ExpressionAtlasiQ96N96. baseline and differential.
GenevisibleiQ96N96. HS.

Organism-specific databases

HPAiHPA040185.
HPA041208.

Interactioni

Subunit structurei

Interacts (via ABR and SH3 domain) with APC. The binding of APC enhances its GEF activity by relieving it from an autoinhibitory conformation, in which the ABR and SH3 domains are associated with the C-terminal tail. Interacts (via C-terminal tail) with PPP1R9B (via C-terminus). Interacts with RAC1.3 Publications

Protein-protein interaction databases

BioGridi128693. 8 interactions.
STRINGi9606.ENSP00000371542.

Structurei

3D structure databases

ProteinModelPortaliQ96N96.
SMRiQ96N96. Positions 127-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 20660SH3PROSITE-ProRule annotationAdd
BLAST
Domaini240 – 424185DHPROSITE-ProRule annotationAdd
BLAST
Domaini455 – 561107PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 15053ABR (APC-binding region) domainAdd
BLAST
Regioni561 – 65292C-terminal tailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 234Poly-Arg

Domaini

The C-terminal tail is required for its GEF activity.

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiENOG410ITS0. Eukaryota.
ENOG410XQDV. LUCA.
GeneTreeiENSGT00760000118925.
HOVERGENiHBG050568.
InParanoidiQ96N96.
OMAiNINVKNA.
PhylomeDBiQ96N96.
TreeFamiTF316832.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q96N96-1) [UniParc]FASTAAdd to basket

Also known as: ASEF-2b

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
MTSASPEDQN APVGCPKGAR RRRPISVIGG VSLYGTNQTE ELDNLLTQPA
60 70 80 90 100
SRPPMPAHQV PPYKAVSARF RPFTFSQSTP IGLDRVGRRR QMRASNVSSD
110 120 130 140 150
GGTEPSALVD DNGSEEDFSY EDLCQASPRY LQPGGEQLAI NELISDGNVV
160 170 180 190 200
CAEALWDHVT MDDQELGFKA GDVIQVLEAS NKDWWWGRSE DKEAWFPASF
210 220 230 240 250
VRLRVNQEEL SENSSSTPSE EQDEEASQSR HRHCENKQQM RTNVIREIMD
260 270 280 290 300
TERVYIKHLR DICEGYIRQC RKHTGMFTVA QLATIFGNIE DIYKFQRKFL
310 320 330 340 350
KDLEKQYNKE EPHLSEIGSC FLQNQEGFAI YSEYCNNHPG ACLELANLMK
360 370 380 390 400
QGKYRHFFEA CRLLQQMIDI AIDGFLLTPV QKICKYPLQL AELLKYTTQE
410 420 430 440 450
HGDYSNIKAA YEAMKNVACL INERKRKLES IDKIARWQVS IVGWEGLDIL
460 470 480 490 500
DRSSELIHSG ELTKITKQGK SQQRTFFLFD HQLVSCKKDL LRRDMLYYKG
510 520 530 540 550
RLDMDEMELV DLGDGRDKDC NLSVKNAFKL VSRTTDEVYL FCAKKQEDKA
560 570 580 590 600
RWLQACADER RRVQEDKEMG MEISENQKKL AMLNAQKAGH GKSKGYNRCP
610 620 630 640 650
VAPPHQGLHP IHQRHITMPT SVPQQQVFGL AEPKRKSSLF WHTFNRLTPF

RK
Length:652
Mass (Da):74,820
Last modified:December 1, 2001 - v1
Checksum:i7C922E8AF0A9C836
GO
Isoform 2 (identifier: Q96N96-2) [UniParc]FASTAAdd to basket

Also known as: ASEF-2a

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: MTSASPEDQN...GRRRQMRASN → MVARGEIARFWSLESLHL

Show »
Length:574
Mass (Da):66,403
Checksum:i34A1B7ECAF3C4C30
GO
Isoform 3 (identifier: Q96N96-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: MTSASPEDQN...GRRRQMRASN → MGFIIHIQQV...EKKCASLSFE

Show »
Length:596
Mass (Da):69,108
Checksum:iCBD88B1A30AF9B9A
GO
Isoform 4 (identifier: Q96N96-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     595-652: GYNRCPVAPP...TFNRLTPFRK → VRLQQVPRGP...SMELGVKRRN

Show »
Length:616
Mass (Da):70,446
Checksum:i15F635D80BA6B3C7
GO
Isoform 5 (identifier: Q96N96-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     203-264: Missing.

Show »
Length:536
Mass (Da):61,677
Checksum:iF449FEF56512EA27
GO
Isoform 6 (identifier: Q96N96-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTQAAVRPWA...RVDEDPQASM

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:1,277
Mass (Da):141,436
Checksum:i23BC07A9333FB2C7
GO

Sequence cautioni

The sequence BAC04977.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti304 – 3041E → G in BAG61802 (PubMed:14702039).Curated
Sequence conflicti520 – 5201C → R in BAG62740 (PubMed:14702039).Curated
Sequence conflicti537 – 5371E → G in BAG62740 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201R → W.
Corresponds to variant rs7330736 [ dbSNP | Ensembl ].
VAR_030776

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9696MTSAS…MRASN → MVARGEIARFWSLESLHL in isoform 2. 1 PublicationVSP_041030Add
BLAST
Alternative sequencei1 – 9696MTSAS…MRASN → MGFIIHIQQVKKQRKKLDQG LILKKEKYRKEKKCASLSFE in isoform 3. 1 PublicationVSP_041031Add
BLAST
Alternative sequencei1 – 5454Missing in isoform 4 and isoform 5. 1 PublicationVSP_041032Add
BLAST
Alternative sequencei1 – 11M → MTQAAVRPWAPCLENMTTAP NGLGPGPAAPCAGSDLKDAK MVTSLACGNGVCGCSPGGDT DTQEAKLSPAKLVRLFSTSR KRTGAHPERPHSMVLVGNSS TWNTLASFRKMGSFKKLKSS VLKGIQSREGSNACSKGEAS EHGLGKSIPNGAVPGAQASR GSPLAPGPACGALRPAEWGT LDGSDLEDTDDAFQRSTHRS RSLRRAYGLGRICLLDAPQN HATPTIATGQVPAVCEILVR DPENNSMGYRRSKSTDNLAF LKKSSFKRKSTSNLADLRTA HDARVPQRTLSSSSTDSQKL GSGRTKRWRSPIRAKDFDRV FKLVSNVTEAAWRRESPRSG APSPGEASLRLQAHSRLHDD YSRRVSRSTEQDSRRGGAVM HGTTATCTVAPGFGSATSKG PHLDADTAVFPLETKSSWAV ESDSSCTCSSLPSPIVQDVL SKDSCDPNAGSQLTFDPEQP PTPLRPTTPKPQSPQSPQSP GAGSASCHSNHSALSANSEE SEGRAEEPAQREPGPVSLQD PLEATHGDEGSKDLLVNIGV AAGPEEKEKEEVVPDGPWRR SSSQDEERTEAQRTPKRRWG SGRRPRPRPFSDYGQLASRS LSIPEDSVAADPQKEDRVDE DPQASM in isoform 6. CuratedVSP_054112
Alternative sequencei203 – 26462Missing in isoform 5. 1 PublicationVSP_041033Add
BLAST
Alternative sequencei595 – 65258GYNRC…TPFRK → VRLQQVPRGPTAPGPAPHPP APHHYAHKRPPAAGLWPGGT QEEVLALLAHLQQAHPLPEM KTGGCASMELGVKRRN in isoform 4. 1 PublicationVSP_041034Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BK006072 mRNA. Translation: DAA05848.1.
AK055770 mRNA. Translation: BAB71009.1.
AK097217 mRNA. Translation: BAC04977.1. Different initiation.
AK123031 mRNA. Translation: BAG53856.1.
AK298717 mRNA. Translation: BAG60873.1.
AK299981 mRNA. Translation: BAG61802.1.
AK301149 mRNA. Translation: BAG62740.1.
AL136963 Genomic DNA. No translation available.
AL139324 Genomic DNA. No translation available.
AL359736 Genomic DNA. Translation: CAH72289.1.
AL359736 Genomic DNA. Translation: CAH72290.2.
AL445985 Genomic DNA. No translation available.
CH471075 Genomic DNA. Translation: EAX08331.1.
BC109290 mRNA. Translation: AAI09291.1.
BC109291 mRNA. Translation: AAI09292.1.
AK074117 mRNA. Translation: BAB84943.1.
AK160371 mRNA. Translation: BAD18714.1.
CCDSiCCDS53857.1. [Q96N96-6]
CCDS66517.1. [Q96N96-2]
CCDS66518.1. [Q96N96-3]
CCDS9305.1. [Q96N96-1]
RefSeqiNP_001159743.1. NM_001166271.2. [Q96N96-6]
NP_001273721.1. NM_001286792.1.
NP_001273722.1. NM_001286793.1.
NP_001273723.1. NM_001286794.1. [Q96N96-3]
NP_001273724.1. NM_001286795.1. [Q96N96-2]
NP_694568.1. NM_153023.3. [Q96N96-1]
UniGeneiHs.434298.
Hs.595391.

Genome annotation databases

EnsembliENST00000343003; ENSP00000343631; ENSG00000182957. [Q96N96-3]
ENST00000382095; ENSP00000371527; ENSG00000182957. [Q96N96-1]
ENST00000382108; ENSP00000371542; ENSG00000182957. [Q96N96-6]
ENST00000399949; ENSP00000382830; ENSG00000182957. [Q96N96-2]
ENST00000424834; ENSP00000398560; ENSG00000182957. [Q96N96-6]
GeneIDi221178.
KEGGihsa:221178.
UCSCiuc001upg.4. human. [Q96N96-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BK006072 mRNA. Translation: DAA05848.1.
AK055770 mRNA. Translation: BAB71009.1.
AK097217 mRNA. Translation: BAC04977.1. Different initiation.
AK123031 mRNA. Translation: BAG53856.1.
AK298717 mRNA. Translation: BAG60873.1.
AK299981 mRNA. Translation: BAG61802.1.
AK301149 mRNA. Translation: BAG62740.1.
AL136963 Genomic DNA. No translation available.
AL139324 Genomic DNA. No translation available.
AL359736 Genomic DNA. Translation: CAH72289.1.
AL359736 Genomic DNA. Translation: CAH72290.2.
AL445985 Genomic DNA. No translation available.
CH471075 Genomic DNA. Translation: EAX08331.1.
BC109290 mRNA. Translation: AAI09291.1.
BC109291 mRNA. Translation: AAI09292.1.
AK074117 mRNA. Translation: BAB84943.1.
AK160371 mRNA. Translation: BAD18714.1.
CCDSiCCDS53857.1. [Q96N96-6]
CCDS66517.1. [Q96N96-2]
CCDS66518.1. [Q96N96-3]
CCDS9305.1. [Q96N96-1]
RefSeqiNP_001159743.1. NM_001166271.2. [Q96N96-6]
NP_001273721.1. NM_001286792.1.
NP_001273722.1. NM_001286793.1.
NP_001273723.1. NM_001286794.1. [Q96N96-3]
NP_001273724.1. NM_001286795.1. [Q96N96-2]
NP_694568.1. NM_153023.3. [Q96N96-1]
UniGeneiHs.434298.
Hs.595391.

3D structure databases

ProteinModelPortaliQ96N96.
SMRiQ96N96. Positions 127-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128693. 8 interactions.
STRINGi9606.ENSP00000371542.

PTM databases

iPTMnetiQ96N96.

Polymorphism and mutation databases

BioMutaiSPATA13.
DMDMi74752049.

Proteomic databases

EPDiQ96N96.
MaxQBiQ96N96.
PaxDbiQ96N96.
PeptideAtlasiQ96N96.
PRIDEiQ96N96.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343003; ENSP00000343631; ENSG00000182957. [Q96N96-3]
ENST00000382095; ENSP00000371527; ENSG00000182957. [Q96N96-1]
ENST00000382108; ENSP00000371542; ENSG00000182957. [Q96N96-6]
ENST00000399949; ENSP00000382830; ENSG00000182957. [Q96N96-2]
ENST00000424834; ENSP00000398560; ENSG00000182957. [Q96N96-6]
GeneIDi221178.
KEGGihsa:221178.
UCSCiuc001upg.4. human. [Q96N96-1]

Organism-specific databases

CTDi221178.
GeneCardsiSPATA13.
HGNCiHGNC:23222. SPATA13.
HPAiHPA040185.
HPA041208.
MIMi613324. gene.
neXtProtiNX_Q96N96.
PharmGKBiPA134912609.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITS0. Eukaryota.
ENOG410XQDV. LUCA.
GeneTreeiENSGT00760000118925.
HOVERGENiHBG050568.
InParanoidiQ96N96.
OMAiNINVKNA.
PhylomeDBiQ96N96.
TreeFamiTF316832.

Miscellaneous databases

ChiTaRSiSPATA13. human.
GenomeRNAii221178.
PROiQ96N96.
SOURCEiSearch...

Gene expression databases

BgeeiQ96N96.
CleanExiHS_SPATA13.
ExpressionAtlasiQ96N96. baseline and differential.
GenevisibleiQ96N96. HS.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR000219. DH-domain.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Asef2 functions as a Cdc42 exchange factor and is stimulated by the release of an autoinhibitory module from a concealed C-terminal activation element."
    Hamann M.J., Lubking C.M., Luchini D.N., Billadeau D.D.
    Mol. Cell. Biol. 27:1380-1393(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH APC AND RAC1, TISSUE SPECIFICITY, ENZYME REGULATION.
  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] (ISOFORMS 1; 2; 3; 4 AND 5).
    Tissue: Kidney, Lung and Spleen.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
  6. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
    Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-652.
    Tissue: Spleen.
  7. "Identification and characterization of Asef2, a guanine-nucleotide exchange factor specific for Rac1 and Cdc42."
    Kawasaki Y., Sagara M., Shibata Y., Shirouzu M., Yokoyama S., Akiyama T.
    Oncogene 26:7620-7627(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
  8. "The adenomatous polyposis coli-associated exchange factors Asef and Asef2 are required for adenoma formation in Apc(Min/+)mice."
    Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M., Ohwada S., Akiyama T.
    EMBO Rep. 10:1355-1362(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin dynamics and thereby regulate cell migration."
    Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L., Webb D.J.
    J. Cell Sci. 122:4535-4546(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal organization and are involved in HGF-induced cell migration."
    Sagara M., Kawasaki Y., Iemura S.I., Natsume T., Takai Y., Akiyama T.
    Oncogene 28:1357-1365(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1R9B.

Entry informationi

Entry nameiSPT13_HUMAN
AccessioniPrimary (citable) accession number: Q96N96
Secondary accession number(s): A2VEA9
, A6NF85, B4DQB1, B4DSZ0, B4DVM8, J3KPJ7, J3KQH2, Q5VX68, Q6ZML1, Q8N873, Q8TEK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 1, 2001
Last modified: July 6, 2016
This is version 130 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.