Q9ULH1 (ASAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1

Alternative name(s):
130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein
ADP-ribosylation factor-directed GTPase-activating protein 1
Short name=ARF GTPase-activating protein 1
Development and differentiation-enhancing factor 1
Short name=DEF-1
Short name=Differentiation-enhancing factor 1
PIP2-dependent ARF1 GAP

Gene names

Name:	ASAP1
Synonyms:	DDEF1, KIAA1249

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1129 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types By similarity. Plays a role in ciliogenesis. Ref.10
Enzyme regulation	Activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) By similarity.
Subunit structure	Homodimer. Interacts with SRC and CRK. Interacts with RAB11FIP3. Interacts with PTK2B/PYK2 By similarity. Interacts with CTTN. Interacts (via SH3 domain) with APC. Ref.15
Subcellular location	Cytoplasm By similarity. Membrane By similarity. Note: Predominantly cytoplasmic By similarity. Partially membrane-associated By similarity.
Domain	The PH domain most probably contributes to the phosphoinositide-dependent regulation of ADP ribosylation factors By similarity.
Post-translational modification	Phosphorylated on tyrosine residues by SRC By similarity.
Sequence similarities	Contains 2 ANK repeats. Contains 1 Arf-GAP domain. Contains 1 PH domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	ANK repeat Repeat SH3 domain Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cilium morphogenesis Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC regulation of ARF GTPase activity Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ARF GTPase activator activity Inferred from electronic annotation. Source: InterPro phospholipid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	2	EBI-346622,EBI-886
FYN	P06241	2	EBI-346622,EBI-515315
GRB2	P62993	7	EBI-346622,EBI-401755
NCK1	P16333	5	EBI-346622,EBI-389883
PLCG1	P19174	3	EBI-346622,EBI-79387
SRC	P12931	2	EBI-346622,EBI-621482

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q9ULH1-1)

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.

Isoform 1 (identifier: Q9ULH1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     303-303: E → ESRR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1129

1129

Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1

PRO_0000074196

Regions

Domain

324 – 416

93

PH

Domain

439 – 560

122

Arf-GAP

Repeat

600 – 632

33

ANK 1

Repeat

636 – 665

30

ANK 2

Domain

1067 – 1129

63

SH3

Zinc finger

454 – 477

24

C4-type

Compositional bias

783 – 993

211

Pro-rich

Amino acid modifications

Modified residue

717

1

Phosphoserine By similarity

Modified residue

843

1

Phosphoserine Ref.8 Ref.9

Modified residue

1008

1

Phosphoserine Ref.8

Modified residue

1027

1

Phosphoserine Ref.7 Ref.9 Ref.11

Natural variations

Alternative sequence

303

1

E → ESRR in isoform 1.

VSP_008365

Natural variant

728

1

I → V.
Corresponds to variant rs966185 [ dbSNP | Ensembl ].

VAR_055528

Secondary structure

1

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1129

Helix Strand Turn

Details...

Beta strand

327 – 334

8

Beta strand

336 – 338

3

Beta strand

342 – 350

9

Beta strand

353 – 356

4

Beta strand

366 – 369

4

Turn

370 – 372

3

Beta strand

373 – 377

5

Beta strand

379 – 383

5

Beta strand

385 – 389

5

Beta strand

392 – 397

6

Helix

401 – 419

19

Beta strand

1070 – 1076

7

Beta strand

1081 – 1085

5

Beta strand

1093 – 1098

6

Beta strand

1101 – 1109

9

Beta strand

1116 – 1120

5

Helix

1121 – 1123

3

Beta strand

1124 – 1126

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified May 18, 2010. Version 4. Checksum: 7F54B22015638D55	FASTA	1,129	125,498
	10 20 30 40 50 60 MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL 70 80 90 100 110 120 EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK 130 140 150 160 170 180 FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYETKFTKI 190 200 210 220 230 240 EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL 250 260 270 280 290 300 IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD 310 320 330 340 350 360 QKEDSQSRQG GYSMHQLQGN KEYGSEKKGY LLKKSDGIRK VWQRRKCSVK NGILTISHAT 370 380 390 400 410 420 SNRQPAKLNL LTCQVKPNAE DKKSFDLISH NRTYHFQAED EQDYVAWISV LTNSKEEALT 430 440 450 460 470 480 MAFRGEQSAG ENSLEDLTKA IIEDVQRLPG NDICCDCGSS EPTWLSTNLG ILTCIECSGI 490 500 510 520 530 540 HREMGVHISR IQSLELDKLG TSELLLAKNV GNNSFNDIME ANLPSPSPKP TPSSDMTVRK 550 560 570 580 590 600 EYITAKYVDH RFSRKTCSTS SAKLNELLEA IKSRDLLALI QVYAEGVELM EPLLEPGQEL 610 620 630 640 650 660 GETALHLAVR TADQTSLHLV DFLVQNCGNL DKQTALGNTV LHYCSMYSKP ECLKLLLRSK 670 680 690 700 710 720 PTVDIVNQAG ETALDIAKRL KATQCEDLLS QAKSGKFNPH VHVEYEWNLR QEEIDESDDD 730 740 750 760 770 780 LDDKPSPIKK ERSPRPQSFC HSSSISPQDK LALPGFSTPR DKQRLSYGAF TNQIFVSTST 790 800 810 820 830 840 DSPTSPTTEA PPLPPRNAGK GPTGPPSTLP LSTQTSSGSS TLSKKRPPPP PPGHKRTLSD 850 860 870 880 890 900 PPSPLPHGPP NKGAVPWGND GGPSSSSKTT NKFEGLSQQS STSSAKTALG PRVLPKLPQK 910 920 930 940 950 960 VALRKTDHLS LDKATIPPEI FQKSSQLAEL PQKPPPGDLP PKPTELAPKP QIGDLPPKPG 970 980 990 1000 1010 1020 ELPPKPQLGD LPPKPQLSDL PPKPQMKDLP PKPQLGDLLA KSQTGDVSPK AQQPSEVTLK 1030 1040 1050 1060 1070 1080 SHPLDLSPNV QSRDAIQKQA SEDSNDLTPT LPETPVPLPR KINTGKNKVR RVKTIYDCQA 1090 1100 1110 1120 DNDDELTFIE GEVIIVTGEE DQEWWIGHIE GQPERKGVFP VSFVHILSD
	Isoform 1 [UniParc]. Checksum: A0440C36242D033C	FASTA	1,132	125,897
	10 20 30 40 50 60 MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL 70 80 90 100 110 120 EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK 130 140 150 160 170 180 FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYETKFTKI 190 200 210 220 230 240 EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL 250 260 270 280 290 300 IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD 310 320 330 340 350 360 QKESRRDSQS RQGGYSMHQL QGNKEYGSEK KGYLLKKSDG IRKVWQRRKC SVKNGILTIS 370 380 390 400 410 420 HATSNRQPAK LNLLTCQVKP NAEDKKSFDL ISHNRTYHFQ AEDEQDYVAW ISVLTNSKEE 430 440 450 460 470 480 ALTMAFRGEQ SAGENSLEDL TKAIIEDVQR LPGNDICCDC GSSEPTWLST NLGILTCIEC 490 500 510 520 530 540 SGIHREMGVH ISRIQSLELD KLGTSELLLA KNVGNNSFND IMEANLPSPS PKPTPSSDMT 550 560 570 580 590 600 VRKEYITAKY VDHRFSRKTC STSSAKLNEL LEAIKSRDLL ALIQVYAEGV ELMEPLLEPG 610 620 630 640 650 660 QELGETALHL AVRTADQTSL HLVDFLVQNC GNLDKQTALG NTVLHYCSMY SKPECLKLLL 670 680 690 700 710 720 RSKPTVDIVN QAGETALDIA KRLKATQCED LLSQAKSGKF NPHVHVEYEW NLRQEEIDES 730 740 750 760 770 780 DDDLDDKPSP IKKERSPRPQ SFCHSSSISP QDKLALPGFS TPRDKQRLSY GAFTNQIFVS 790 800 810 820 830 840 TSTDSPTSPT TEAPPLPPRN AGKGPTGPPS TLPLSTQTSS GSSTLSKKRP PPPPPGHKRT 850 860 870 880 890 900 LSDPPSPLPH GPPNKGAVPW GNDGGPSSSS KTTNKFEGLS QQSSTSSAKT ALGPRVLPKL 910 920 930 940 950 960 PQKVALRKTD HLSLDKATIP PEIFQKSSQL AELPQKPPPG DLPPKPTELA PKPQIGDLPP 970 980 990 1000 1010 1020 KPGELPPKPQ LGDLPPKPQL SDLPPKPQMK DLPPKPQLGD LLAKSQTGDV SPKAQQPSEV 1030 1040 1050 1060 1070 1080 TLKSHPLDLS PNVQSRDAIQ KQASEDSNDL TPTLPETPVP LPRKINTGKN KVRRVKTIYD 1090 1100 1110 1120 1130 CQADNDDELT FIEGEVIIVT GEEDQEWWIG HIEGQPERKG VFPVSFVHIL SD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]. Tissue: Brain.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-1129 (ISOFORM 2). Tissue: Bone marrow.
[5]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-1129 (ISOFORM 1). Tissue: Brain.
[6]	"ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src." Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A., Randazzo P.A. Mol. Cell. Biol. 18:7038-7051(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[7]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843 AND SER-1008, MASS SPECTROMETRY. Tissue: Platelet.
[9]	"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-843 AND SER-1027, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Functional genomic screen for modulators of ciliogenesis and cilium length." Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G. Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"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-1027, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis." Hashimoto S., Hirose M., Hashimoto A., Morishige M., Yamada A., Hosaka H., Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M., Kobayashi H., Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H. Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 823-837 IN COMPLEX WITH CTTN.
[13]	"Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 319-428.
[14]	"Solution structure of the SH3 domain of 130 kDA phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1067-1129.
[15]	"Structural basis of the recognition of the SAMP motif of adenomatous polyposis coli by the Src-homology 3 domain." Kaieda S., Matsui C., Mimori-Kiyosue Y., Ikegami T. Biochemistry 49:5143-5153(2010) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1069-1129 IN COMPLEX WITH APC, INTERACTION WITH APC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AC009682 Genomic DNA. No translation available.
AC103725 Genomic DNA. No translation available.
AC131568 Genomic DNA. No translation available.
AC139019 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW92130.1.
BC137135 mRNA. Translation: AAI37136.1.
BX537768 mRNA. Translation: CAD97831.1.
AB033075 mRNA. Translation: BAA86563.1.

IPI

IPI00376976.
IPI00873747.

RefSeq

NP_001234925.1. NM_001247996.1.
NP_060952.2. NM_018482.3.

UniGene

Hs.655552.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D1X	X-ray	1.90	P/Q	823-837	[»]
2DA0	NMR	-	A	323-423	[»]
2ED1	NMR	-	A	1067-1129	[»]
2RQT	NMR	-	A	1069-1129	[»]
2RQU	NMR	-	A	1069-1129	[»]

ProteinModelPortal

Q9ULH1.

SMR

Q9ULH1. Positions 31-429, 437-709, 1069-1129.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9ULH1. 11 interactions.

MINT

MINT-243352.

STRING

9606.ENSP00000350297.

PTM databases

PhosphoSite

Q9ULH1.

Polymorphism databases

DMDM

296439459.

Proteomic databases

PaxDb

Q9ULH1.

PRIDE

Q9ULH1.

Protocols and materials databases

DNASU

50807.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357668; ENSP00000350297; ENSG00000153317.
ENST00000518721; ENSP00000429900; ENSG00000153317.

GeneID

50807.

KEGG

hsa:50807.

UCSC

uc003ysz.2. human.
uc003yta.2. human.

Organism-specific databases

CTD

50807.

GeneCards

GC08M131064.

H-InvDB

HIX0007806.

HGNC

HGNC:2720. ASAP1.

HPA

CAB037292.

MIM

605953. gene.

neXtProt

NX_Q9ULH1.

PharmGKB

PA164716055.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5347.

HOGENOM

HOG000230570.

HOVERGEN

HBG051327.

KO

K12488.

OrthoDB

EOG4PC9RD.

PhylomeDB

Q9ULH1.

Enzyme and pathway databases

Pathway_Interaction_DB

arf_3pathway. Arf1 pathway.

Gene expression databases

ArrayExpress

Q9ULH1.

Bgee

Q9ULH1.

CleanEx

HS_ASAP1.

Genevestigator

Q9ULH1.

GermOnline

ENSG00000153317. Homo sapiens.

Family and domain databases

Gene3D

1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.

InterPro

IPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00405. REVINTRACTNG.

SMART

SM00248. ANK. 2 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ASAP1. human.

EvolutionaryTrace

Q9ULH1.

GenomeRNAi

50807.

NextBio

53242.

SOURCE

Search...

Entry information

Entry name

ASAP1_HUMAN

Accession

Primary (citable) accession number: Q9ULH1
Secondary accession number(s): B2RNV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 122 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.