Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O75366

- AVIL_HUMAN

UniProt

O75366 - AVIL_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Advillin

Gene

AVIL

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

Functioni

Ca2+-regulated actin-binding protein. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis.1 Publication

GO - Molecular functioni

  1. actin binding Source: UniProtKB

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. cilium morphogenesis Source: UniProtKB
  3. cytoskeleton organization Source: InterPro
  4. nervous system development Source: ProtInc
  5. positive regulation of neuron projection development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Advillin
Alternative name(s):
p92
Gene namesi
Name:AVIL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:14188. AVIL.

Subcellular locationi

Cytoplasmcytoskeleton. Cell projection By similarity. Cell projectionaxon By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: ProtInc
  2. cell projection Source: UniProtKB
  3. cytoplasm Source: UniProtKB-KW
  4. neuron projection Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621W → A: Reduces interaction with F-actin. 1 Publication

Organism-specific databases

PharmGKBiPA38380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 819819AdvillinPRO_0000218736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851PhosphotyrosineBy similarity
Modified residuei758 – 7581PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO75366.
PRIDEiO75366.

PTM databases

PhosphoSiteiO75366.

Expressioni

Tissue specificityi

Most highly expressed in the small intestine and colonic lining. Weaker expression also detected in the thymus, prostate, testes and uterus.1 Publication

Gene expression databases

BgeeiO75366.
CleanExiHS_AVIL.
ExpressionAtlasiO75366. baseline and differential.
GenevestigatoriO75366.

Organism-specific databases

HPAiHPA058864.

Interactioni

Subunit structurei

Associates (via C-terminus) with actin. Interacts with SCARF1 (By similarity). Interacts with F-actin.By similarity1 Publication

Protein-protein interaction databases

BioGridi115918. 3 interactions.
MINTiMINT-4990440.
STRINGi9606.ENSP00000257861.

Structurei

Secondary structure

1
819
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi787 – 7948Combined sources
Helixi798 – 8036Combined sources
Helixi806 – 81712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UNDNMR-A784-819[»]
ProteinModelPortaliO75366.
SMRiO75366. Positions 7-722, 759-819.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75366.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati24 – 7350Gelsolin-like 1Add
BLAST
Repeati145 – 18541Gelsolin-like 2Add
BLAST
Repeati262 – 30645Gelsolin-like 3Add
BLAST
Repeati403 – 45452Gelsolin-like 4Add
BLAST
Repeati525 – 56541Gelsolin-like 5Add
BLAST
Repeati628 – 66942Gelsolin-like 6Add
BLAST
Domaini753 – 81967HPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 731731CoreBy similarityAdd
BLAST
Regioni109 – 1168Polyphosphoinositide bindingBy similarity
Regioni135 – 1439Polyphosphoinositide bindingBy similarity
Regioni731 – 81989HeadpieceBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 6 gelsolin-like repeats.Curated
Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG304849.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiO75366.
KOiK08017.
OMAiCYVILST.
OrthoDBiEOG7288RJ.
PhylomeDBiO75366.
TreeFamiTF313468.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75366-1) [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
MPLTSAFRAV DNDPGIIVWR IEKMELALVP VSAHGNFYEG DCYVILSTRR
60 70 80 90 100
VASLLSQDIH FWIGKDSSQD EQSCAAIYTT QLDDYLGGSP VQHREVQYHE
110 120 130 140 150
SDTFRGYFKQ GIIYKQGGVA SGMKHVETNT YDVKRLLHVK GKRNIRATEV
160 170 180 190 200
EMSWDSFNRG DVFLLDLGKV IIQWNGPESN SGERLKAMLL AKDIRDRERG
210 220 230 240 250
GRAKIGVIEG DKEAASPELM KVLQDTLGRR SIIKPTVPDE IIDQKQKSTI
260 270 280 290 300
MLYHISDSAG QLAVTEVATR PLVQDLLNHD DCYILDQSGT KIYVWKGKGA
310 320 330 340 350
TKAEKQAAMS KALGFIKMKS YPSSTNVETV NDGAESAMFK QLFQKWSVKD
360 370 380 390 400
QTMGLGKTFS IGKIAKVFQD KFDVTLLHTK PEVAAQERMV DDGNGKVEVW
410 420 430 440 450
RIENLELVPV EYQWYGFFYG GDCYLVLYTY EVNGKPHHIL YIWQGRHASQ
460 470 480 490 500
DELAASAYQA VEVDRQFDGA AVQVRVRMGT EPRHFMAIFK GKLVIFEGGT
510 520 530 540 550
SRKGNAEPDP PVRLFQIHGN DKSNTKAVEV PAFASSLNSN DVFLLRTQAE
560 570 580 590 600
HYLWYGKGSS GDERAMAKEL ASLLCDGSEN TVAEGQEPAE FWDLLGGKTP
610 620 630 640 650
YANDKRLQQE ILDVQSRLFE CSNKTGQFVV TEITDFTQDD LNPTDVMLLD
660 670 680 690 700
TWDQVFLWIG AEANATEKES ALATAQQYLH THPSGRDPDT PILIIKQGFE
710 720 730 740 750
PPIFTGWFLA WDPNIWSAGK TYEQLKEELG DAAAIMRITA DMKNATLSLN
760 770 780 790 800
SNDSEPKYYP IAVLLKNQNQ ELPEDVNPAK KENYLSEQDF VSVFGITRGQ
810
FAALPGWKQL QMKKEKGLF
Length:819
Mass (Da):92,027
Last modified:November 30, 2010 - v3
Checksum:iF5EF3A94BA61E647
GO
Isoform 2 (identifier: O75366-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MPLTSAFRAVDNDPGIIVWRI → MSSTGHPGSYKIWG

Show »
Length:812
Mass (Da):91,163
Checksum:iCAACCD7994F2D989
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti445 – 4451G → D in AAC25051. (PubMed:9664034)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti204 – 2041K → E.4 Publications
Corresponds to variant rs2172521 [ dbSNP | Ensembl ].
VAR_054974

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MPLTS…IVWRI → MSSTGHPGSYKIWG in isoform 2. 1 PublicationVSP_036961Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041449 mRNA. Translation: AAC25051.1.
AK314362 mRNA. Translation: BAG36994.1.
AC025165 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97080.1.
BC111730 mRNA. Translation: AAI11731.1.
CCDSiCCDS8959.1. [O75366-1]
RefSeqiNP_006567.3. NM_006576.3. [O75366-1]
XP_006719261.1. XM_006719198.1. [O75366-1]
UniGeneiHs.584854.

Genome annotation databases

EnsembliENST00000257861; ENSP00000257861; ENSG00000135407. [O75366-1]
GeneIDi10677.
KEGGihsa:10677.
UCSCiuc001sqj.2. human. [O75366-1]
uc009zqe.2. human. [O75366-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041449 mRNA. Translation: AAC25051.1 .
AK314362 mRNA. Translation: BAG36994.1 .
AC025165 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97080.1 .
BC111730 mRNA. Translation: AAI11731.1 .
CCDSi CCDS8959.1. [O75366-1 ]
RefSeqi NP_006567.3. NM_006576.3. [O75366-1 ]
XP_006719261.1. XM_006719198.1. [O75366-1 ]
UniGenei Hs.584854.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UND NMR - A 784-819 [» ]
ProteinModelPortali O75366.
SMRi O75366. Positions 7-722, 759-819.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115918. 3 interactions.
MINTi MINT-4990440.
STRINGi 9606.ENSP00000257861.

PTM databases

PhosphoSitei O75366.

Proteomic databases

PaxDbi O75366.
PRIDEi O75366.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257861 ; ENSP00000257861 ; ENSG00000135407 . [O75366-1 ]
GeneIDi 10677.
KEGGi hsa:10677.
UCSCi uc001sqj.2. human. [O75366-1 ]
uc009zqe.2. human. [O75366-2 ]

Organism-specific databases

CTDi 10677.
GeneCardsi GC12M058191.
H-InvDB HIX0023233.
HGNCi HGNC:14188. AVIL.
HPAi HPA058864.
MIMi 613397. gene.
neXtProti NX_O75366.
PharmGKBi PA38380.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304849.
GeneTreei ENSGT00760000119111.
HOGENOMi HOG000233630.
HOVERGENi HBG004183.
InParanoidi O75366.
KOi K08017.
OMAi CYVILST.
OrthoDBi EOG7288RJ.
PhylomeDBi O75366.
TreeFami TF313468.

Miscellaneous databases

ChiTaRSi AVIL. human.
EvolutionaryTracei O75366.
GenomeRNAii 10677.
NextBioi 40597.
PROi O75366.
SOURCEi Search...

Gene expression databases

Bgeei O75366.
CleanExi HS_AVIL.
ExpressionAtlasi O75366. baseline and differential.
Genevestigatori O75366.

Family and domain databases

Gene3Di 1.10.950.10. 1 hit.
3.40.20.10. 6 hits.
InterProi IPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view ]
PANTHERi PTHR11977. PTHR11977. 1 hit.
Pfami PF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view ]
PRINTSi PR00597. GELSOLIN.
SMARTi SM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view ]
SUPFAMi SSF47050. SSF47050. 1 hit.
PROSITEi PS51089. HP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Advillin (p92): a new member of the gelsolin/villin family of actin regulatory proteins."
    Marks P.W., Arai M., Bandura J.L., Kwiatkowski D.J.
    J. Cell Sci. 111:2129-2136(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-204.
    Tissue: Uterus.
  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), VARIANT GLU-204.
    Tissue: Brain.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-204.
  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 2), VARIANT GLU-204.
  6. "Genomic structure, chromosome mapping and expression analysis of the human AVIL gene, and its exclusion as a candidate for locus for inflammatory bowel disease at 12q13-14 (IBD2)."
    Tumer Z., Croucher P.J., Jensen L.R., Hampe J., Hansen C., Kalscheuer V., Ropers H.H., Tommerup N., Schreiber S.
    Gene 288:179-185(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "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.
  8. "Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements."
    Vermeulen W., Vanhaesebrouck P., Van Troys M., Verschueren M., Fant F., Goethals M., Ampe C., Martins J.C., Borremans F.A.
    Protein Sci. 13:1276-1287(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 784-819, INTERACTION WITH F-ACTIN, MUTAGENESIS OF TRP-62.

Entry informationi

Entry nameiAVIL_HUMAN
AccessioniPrimary (citable) accession number: O75366
Secondary accession number(s): B2RAU7, Q2NKM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 123 of the entry and version 3 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 12
    Human chromosome 12: 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