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Q9Y6U3

- ADSV_HUMAN

UniProt

Q9Y6U3 - ADSV_HUMAN

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Protein

Adseverin

Gene

SCIN

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

Functioni

Ca2+-dependent actin filament-severing protein that is presumed to have a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane. In vitro, also has barbed end capping and nucleating activities in the presence of Ca2+. Regulates chondrocyte proliferation and differentiation. MAP kinases p38 and ERK1/2 mediate the adseverin-induced accelerated differentiation of non-hypertrophic chondrocytes (By similarity).By similarity

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: UniProtKB
  2. actin binding Source: UniProtKB
  3. actin filament binding Source: UniProtKB
  4. calcium ion binding Source: UniProtKB
  5. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  6. phosphatidylserine binding Source: UniProtKB

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. actin filament severing Source: UniProtKB
  3. actin nucleation Source: UniProtKB
  4. calcium ion-dependent exocytosis Source: UniProtKB
  5. negative regulation of cell proliferation Source: UniProtKB
  6. positive regulation of apoptotic process Source: UniProtKB
  7. positive regulation of megakaryocyte differentiation Source: UniProtKB
  8. positive regulation of secretion Source: UniProtKB
  9. regulation of chondrocyte differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Adseverin
Alternative name(s):
Scinderin
Gene namesi
Name:SCIN
Synonyms:KIAA1905
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:21695. SCIN.

Subcellular locationi

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-KW
  4. extracellular vesicular exosome Source: UniProt
  5. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi455 – 4551F → D: Loss of actin-binding. 1 Publication

Organism-specific databases

PharmGKBiPA134981389.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715AdseverinPRO_0000218744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphotyrosineBy similarity
Modified residuei599 – 5991PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y6U3.
PaxDbiQ9Y6U3.
PeptideAtlasiQ9Y6U3.
PRIDEiQ9Y6U3.

PTM databases

PhosphoSiteiQ9Y6U3.

Expressioni

Gene expression databases

BgeeiQ9Y6U3.
CleanExiHS_SCIN.
ExpressionAtlasiQ9Y6U3. baseline and differential.
GenevestigatoriQ9Y6U3.

Organism-specific databases

HPAiHPA020518.
HPA022009.
HPA024264.

Interactioni

Protein-protein interaction databases

BioGridi124552. 5 interactions.
IntActiQ9Y6U3. 1 interaction.
MINTiMINT-1141238.
STRINGi9606.ENSP00000297029.

Structurei

Secondary structure

1
715
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi397 – 4037Combined sources
Beta strandi405 – 4106Combined sources
Helixi413 – 4153Combined sources
Beta strandi424 – 4307Combined sources
Beta strandi435 – 4417Combined sources
Helixi447 – 46317Combined sources
Beta strandi469 – 4746Combined sources
Helixi480 – 4834Combined sources
Beta strandi491 – 4933Combined sources
Beta strandi511 – 5166Combined sources
Beta strandi519 – 5213Combined sources
Beta strandi524 – 5285Combined sources
Helixi532 – 5343Combined sources
Beta strandi539 – 5446Combined sources
Beta strandi548 – 5547Combined sources
Helixi560 – 57213Combined sources
Beta strandi576 – 5816Combined sources
Helixi587 – 5926Combined sources
Turni603 – 6053Combined sources
Beta strandi615 – 6206Combined sources
Beta strandi627 – 6304Combined sources
Helixi637 – 6393Combined sources
Beta strandi644 – 6496Combined sources
Beta strandi654 – 6585Combined sources
Helixi664 – 67411Combined sources
Beta strandi691 – 6955Combined sources
Helixi701 – 7044Combined sources
Beta strandi707 – 7093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FG6X-ray3.00A/B/C/D/E/F/G/H345-715[»]
ProteinModelPortaliQ9Y6U3.
SMRiQ9Y6U3. Positions 7-715.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6U3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 7650Gelsolin-like 1Add
BLAST
Repeati148 – 18841Gelsolin-like 2Add
BLAST
Repeati265 – 30743Gelsolin-like 3Add
BLAST
Repeati398 – 45154Gelsolin-like 4Add
BLAST
Repeati523 – 56442Gelsolin-like 5Add
BLAST
Repeati626 – 66843Gelsolin-like 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 363363Actin-severingSequence AnalysisAdd
BLAST
Regioni112 – 1198Polyphosphoinositide bindingBy similarity
Regioni138 – 1469Polyphosphoinositide bindingBy similarity
Regioni364 – 715352Ca(2+)-dependent actin bindingAdd
BLAST

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 6 gelsolin-like repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG304849.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiQ9Y6U3.
KOiK05768.
OMAiQVDQNSY.
OrthoDBiEOG7288RJ.
PhylomeDBiQ9Y6U3.
TreeFamiTF313468.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y6U3-1) [UniParc]FASTAAdd to Basket

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
MARELYHEEF ARAGKQAGLQ VWRIEKLELV PVPQSAHGDF YVGDAYLVLH
60 70 80 90 100
TAKTSRGFTY HLHFWLGKEC SQDESTAAAI FTVQMDDYLG GKPVQNRELQ
110 120 130 140 150
GYESNDFVSY FKGGLKYKAG GVASGLNHVL TNDLTAKRLL HVKGRRVVRA
160 170 180 190 200
TEVPLSWDSF NKGDCFIIDL GTEIYQWCGS SCNKYERLKA NQVATGIRYN
210 220 230 240 250
ERKGRSELIV VEEGSEPSEL IKVLGEKPEL PDGGDDDDII ADISNRKMAK
260 270 280 290 300
LYMVSDASGS MRVTVVAEEN PFSMAMLLSE ECFILDHGAA KQIFVWKGKD
310 320 330 340 350
ANPQERKAAM KTAEEFLQQM NYSKNTQIQV LPEGGETPIF KQFFKDWRDK
360 370 380 390 400
DQSDGFGKVY VTEKVAQIKQ IPFDASKLHS SPQMAAQHNM VDDGSGKVEI
410 420 430 440 450
WRVENNGRIQ VDQNSYGEFY GGDCYIILYT YPRGQIIYTW QGANATRDEL
460 470 480 490 500
TTSAFLTVQL DRSLGGQAVQ IRVSQGKEPV HLLSLFKDKP LIIYKNGTSK
510 520 530 540 550
KGGQAPAPPT RLFQVRRNLA SITRIVEVDV DANSLNSNDV FVLKLPQNSG
560 570 580 590 600
YIWVGKGASQ EEEKGAEYVA SVLKCKTLRI QEGEEPEEFW NSLGGKKDYQ
610 620 630 640 650
TSPLLETQAE DHPPRLYGCS NKTGRFVIEE IPGEFTQDDL AEDDVMLLDA
660 670 680 690 700
WEQIFIWIGK DANEVEKKES LKSAKMYLET DPSGRDKRTP IVIIKQGHEP
710
PTFTGWFLGW DSSKW
Length:715
Mass (Da):80,489
Last modified:January 4, 2005 - v4
Checksum:i20420C82DB2E2D24
GO
Isoform 2 (identifier: Q9Y6U3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     528-580: VDVDANSLNS...SVLKCKTLRI → RSSGIPLEGK...RFQESSPRMI
     581-715: Missing.

Note: No experimental confirmation available.

Show »
Length:580
Mass (Da):65,357
Checksum:i4291B928419AB445
GO
Isoform 3 (identifier: Q9Y6U3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-247: Missing.

Show »
Length:468
Mass (Da):52,814
Checksum:iFB1BAE7D65C7E39F
GO

Sequence cautioni

The sequence BAB67798.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481V → M in BAC11416. (PubMed:14702039)Curated
Sequence conflicti476 – 4761G → D in AAK60494. 1 PublicationCurated
Sequence conflicti546 – 5461P → S in AAK60494. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611H → R.1 Publication
Corresponds to variant rs2240572 [ dbSNP | Ensembl ].
VAR_059956
Natural varianti443 – 4431A → P.
Corresponds to variant rs35083013 [ dbSNP | Ensembl ].
VAR_059957
Natural varianti455 – 4551F → L.
Corresponds to variant rs17166250 [ dbSNP | Ensembl ].
VAR_057470
Natural varianti500 – 5001K → R.
Corresponds to variant rs35705332 [ dbSNP | Ensembl ].
VAR_059958
Natural varianti578 – 5781L → F.
Corresponds to variant rs1138957 [ dbSNP | Ensembl ].
VAR_057471

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 247247Missing in isoform 3. 1 PublicationVSP_040548Add
BLAST
Alternative sequencei528 – 58053VDVDA…KTLRI → RSSGIPLEGKKTTRPHHYWK PRLKTIHLGFTAALTKLEDL LLKRFQESSPRMI in isoform 2. 1 PublicationVSP_012427Add
BLAST
Alternative sequencei581 – 715135Missing in isoform 2. 1 PublicationVSP_012428Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF276507 mRNA. Translation: AAK60494.1.
AK027778 mRNA. Translation: BAB55361.1.
AK075123 mRNA. Translation: BAC11416.1.
AK290363 mRNA. Translation: BAF83052.1.
AB067492 mRNA. Translation: BAB67798.1. Different initiation.
AC005281 Genomic DNA. Translation: AAD15423.1.
CH471073 Genomic DNA. Translation: EAW93647.1.
BC021090 mRNA. Translation: AAH21090.1.
BU193785 mRNA. No translation available.
CCDSiCCDS47545.1. [Q9Y6U3-1]
CCDS47546.1. [Q9Y6U3-3]
RefSeqiNP_001106177.1. NM_001112706.2. [Q9Y6U3-1]
NP_149119.1. NM_033128.3. [Q9Y6U3-3]
UniGeneiHs.633359.
Hs.655515.

Genome annotation databases

EnsembliENST00000297029; ENSP00000297029; ENSG00000006747. [Q9Y6U3-1]
ENST00000341757; ENSP00000341375; ENSG00000006747. [Q9Y6U3-2]
ENST00000519209; ENSP00000430997; ENSG00000006747. [Q9Y6U3-3]
GeneIDi85477.
KEGGihsa:85477.
UCSCiuc003ssn.4. human. [Q9Y6U3-1]

Polymorphism databases

DMDMi57015325.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF276507 mRNA. Translation: AAK60494.1 .
AK027778 mRNA. Translation: BAB55361.1 .
AK075123 mRNA. Translation: BAC11416.1 .
AK290363 mRNA. Translation: BAF83052.1 .
AB067492 mRNA. Translation: BAB67798.1 . Different initiation.
AC005281 Genomic DNA. Translation: AAD15423.1 .
CH471073 Genomic DNA. Translation: EAW93647.1 .
BC021090 mRNA. Translation: AAH21090.1 .
BU193785 mRNA. No translation available.
CCDSi CCDS47545.1. [Q9Y6U3-1 ]
CCDS47546.1. [Q9Y6U3-3 ]
RefSeqi NP_001106177.1. NM_001112706.2. [Q9Y6U3-1 ]
NP_149119.1. NM_033128.3. [Q9Y6U3-3 ]
UniGenei Hs.633359.
Hs.655515.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FG6 X-ray 3.00 A/B/C/D/E/F/G/H 345-715 [» ]
ProteinModelPortali Q9Y6U3.
SMRi Q9Y6U3. Positions 7-715.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124552. 5 interactions.
IntActi Q9Y6U3. 1 interaction.
MINTi MINT-1141238.
STRINGi 9606.ENSP00000297029.

PTM databases

PhosphoSitei Q9Y6U3.

Polymorphism databases

DMDMi 57015325.

Proteomic databases

MaxQBi Q9Y6U3.
PaxDbi Q9Y6U3.
PeptideAtlasi Q9Y6U3.
PRIDEi Q9Y6U3.

Protocols and materials databases

DNASUi 85477.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297029 ; ENSP00000297029 ; ENSG00000006747 . [Q9Y6U3-1 ]
ENST00000341757 ; ENSP00000341375 ; ENSG00000006747 . [Q9Y6U3-2 ]
ENST00000519209 ; ENSP00000430997 ; ENSG00000006747 . [Q9Y6U3-3 ]
GeneIDi 85477.
KEGGi hsa:85477.
UCSCi uc003ssn.4. human. [Q9Y6U3-1 ]

Organism-specific databases

CTDi 85477.
GeneCardsi GC07P012610.
HGNCi HGNC:21695. SCIN.
HPAi HPA020518.
HPA022009.
HPA024264.
MIMi 613416. gene.
neXtProti NX_Q9Y6U3.
PharmGKBi PA134981389.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304849.
GeneTreei ENSGT00760000119111.
HOGENOMi HOG000233630.
HOVERGENi HBG004183.
InParanoidi Q9Y6U3.
KOi K05768.
OMAi QVDQNSY.
OrthoDBi EOG7288RJ.
PhylomeDBi Q9Y6U3.
TreeFami TF313468.

Miscellaneous databases

ChiTaRSi SCIN. human.
EvolutionaryTracei Q9Y6U3.
GeneWikii SCIN.
GenomeRNAii 85477.
NextBioi 76136.
PROi Q9Y6U3.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6U3.
CleanExi HS_SCIN.
ExpressionAtlasi Q9Y6U3. baseline and differential.
Genevestigatori Q9Y6U3.

Family and domain databases

Gene3Di 3.40.20.10. 6 hits.
InterProi IPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view ]
PANTHERi PTHR11977. PTHR11977. 1 hit.
Pfami PF00626. Gelsolin. 6 hits.
[Graphical view ]
PRINTSi PR00597. GELSOLIN.
SMARTi SM00262. GEL. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of human scinderin."
    Ladislas M.L., Hill S.J., Davis C.W.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
    Tissue: Placenta and Tongue.
  3. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-407 (ISOFORM 3), VARIANT ARG-61.
    Tissue: Melanoma and Skin.
  7. "The crystal structure of the C-terminus of adseverin reveals the actin-binding interface."
    Chumnarnsilpa S., Lee W.L., Nag S., Kannan B., Larsson M., Burtnick L.D., Robinson R.C.
    Proc. Natl. Acad. Sci. U.S.A. 106:13719-13724(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 345-715, MUTAGENESIS OF PHE-455.

Entry informationi

Entry nameiADSV_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6U3
Secondary accession number(s): A8K2U8
, Q8NBZ6, Q8WU97, Q96JC7, Q96PY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: January 4, 2005
Last modified: November 26, 2014
This is version 130 of the entry and version 4 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 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3