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Protein

MICAL-like protein 2

Gene

MICALL2

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

Functioni

Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth (By similarity).By similarity

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • filamin binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
MICAL-like protein 2
Alternative name(s):
Junctional Rab13-binding protein
Molecule interacting with CasL-like 2
Short name:
MICAL-L2
Gene namesi
Name:MICALL2
Synonyms:JRAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:29672. MICALL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Endosome, Membrane, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162395928.

Polymorphism and mutation databases

BioMutaiMICALL2.
DMDMi46396456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 904904MICAL-like protein 2PRO_0000075850Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431PhosphoserineCombined sources
Modified residuei153 – 1531PhosphoserineCombined sources
Modified residuei494 – 4941PhosphoserineCombined sources
Modified residuei644 – 6441PhosphothreonineCombined sources
Modified residuei649 – 6491PhosphoserineCombined sources
Modified residuei658 – 6581PhosphoserineCombined sources
Modified residuei660 – 6601PhosphoserineCombined sources
Modified residuei726 – 7261PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8IY33.
MaxQBiQ8IY33.
PaxDbiQ8IY33.
PRIDEiQ8IY33.

PTM databases

iPTMnetiQ8IY33.
PhosphoSiteiQ8IY33.

Expressioni

Gene expression databases

BgeeiQ8IY33.
CleanExiHS_MICALL2.
GenevisibleiQ8IY33. HS.

Organism-specific databases

HPAiHPA025695.

Interactioni

Subunit structurei

Interacts with RAB13 (GTP-bound form); competes with RAB8A and is involved in tight junctions assembly. Interacts with RAB8A; competes with RAB13 and is involved in E-cadherin endocytic recycling (By similarity). Interacts with RAB8B (By similarity). Interacts (preferentially in opened conformation) with ACTN1 and ACTN4; stimulated by RAB13 activation (By similarity). Interacts (via CH domain) with the filamins FLNA, FLNB and FLNC (via actin-binding domain).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN1P128143EBI-2555563,EBI-351710
ACTN2P356093EBI-2555563,EBI-77797

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • filamin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122879. 11 interactions.
IntActiQ8IY33. 10 interactions.
STRINGi9606.ENSP00000297508.

Structurei

3D structure databases

ProteinModelPortaliQ8IY33.
SMRiQ8IY33. Positions 6-106, 184-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 104104CHPROSITE-ProRule annotationAdd
BLAST
Domaini186 – 24863LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 260260Forms an intramolecular interaction with the C-terminal coiled coil domain keeping the protein in a closed conformationBy similarityAdd
BLAST
Regioni261 – 697437Mediates targeting to the cell plasma membraneBy similarityAdd
BLAST
Regioni261 – 388128Necessary and sufficient for interaction with actininsBy similarityAdd
BLAST
Regioni698 – 807110Forms an intramolecular interaction with the N-terminal CH and LIM zinc-binding domains-containing region keeping the protein in a closed conformationBy similarityAdd
BLAST
Regioni807 – 90397Mediates interaction with RAB13 and is required for transition from the closed to the opened conformationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili735 – 77137Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi356 – 3594Poly-Ala
Compositional biasi392 – 3976Poly-Ser
Compositional biasi663 – 6664Poly-Arg

Domaini

Probably exists in a closed and an opened conformation due to interaction of the C-terminal coiled-coil domain with an N-terminal region including the CH (calponin-homology) and the LIM zinc-binding domain. The conformational change is regulated by RAB13 (By similarity).By similarity

Sequence similaritiesi

Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, LIM domain

Phylogenomic databases

eggNOGiENOG410IKSW. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000290690.
HOVERGENiHBG052476.
InParanoidiQ8IY33.
KOiK19948.
OMAiRDVNICN.
OrthoDBiEOG7JT6VM.
PhylomeDBiQ8IY33.
TreeFamiTF328311.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IY33-1) [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
MAAIRALQQW CRQQCEGYRD VNICNMTTSF RDGLAFCAIL HRHRPDLINF
60 70 80 90 100
SALKKENIYE NNKLAFRVAE EHLGIPALLD AEDMVALKVP DRLSILTYVS
110 120 130 140 150
QYYNYFHGRS PIGGMAGVKR ASEDSEEEPS GKKAPVQAAK LPSPAPARKP
160 170 180 190 200
PLSPAQTNPV VQRRNEGAGG PPPKTDQALA GSLVSSTCGV CGKHVHLVQR
210 220 230 240 250
HLADGRLYHR SCFRCKQCSC TLHSGAYKAT GEPGTFVCTS HLPAAASASP
260 270 280 290 300
KLTGLVPRQP GAMGVDSRTS CSPQKAQEAN KARPSAWEPA AGNSPARASV
310 320 330 340 350
PAAPNPAATS ATSVHVRSPA RPSESRLAPT PTEGKVRPRV TNSSPMGWSS
360 370 380 390 400
AAPCTAAAAS HPAVPPSAPD PRPATPQGGG APRVAAPQTT LSSSSTSAAT
410 420 430 440 450
VDPPAWTPSA SRTQQARNKF FQTSAVPPGT SLSGRGPTPS LVLSKDSSKE
460 470 480 490 500
QARNFLKQAL SALEEAGAPA PGRPSPATAA VPSSQPKTEA PQASPLAKPL
510 520 530 540 550
QSSSPRVLGL PSRMEPPAPL STSSTSQASA LPPAGRRNLA ESSGVGRVGA
560 570 580 590 600
GSRPKPEAPM AKGKSTTLTQ DMSTSLQEGQ EDGPAGWRAN LKPVDRRSPA
610 620 630 640 650
ERTLKPKEPR ALAEPRAGEA PRKVSGSFAG SVHITLTPVR PDRTPRPASP
660 670 680 690 700
GPSLPARSPS PPRRRRLAVP ASLDVCDNWL RPEPPGQEAR VQSWKEEEKK
710 720 730 740 750
PHLQGKPGRP LSPANVPALP GETVTSPVRL HPDYLSPEEI QRQLQDIERR
760 770 780 790 800
LDALELRGVE LEKRLRAAEG DDAEDSLMVD WFWLIHEKQL LLRQESELMY
810 820 830 840 850
KSKAQRLEEQ QLDIEGELRR LMAKPEALKS LQERRREQEL LEQYVSTVND
860 870 880 890 900
RSDIVDSLDE DRLREQEEDQ MLRDMIEKLG LQRKKSKFRL SKIWSPKSKS

SPSQ
Length:904
Mass (Da):97,502
Last modified:March 1, 2003 - v1
Checksum:iA2C360EDDEFFA2EF
GO
Isoform 2 (identifier: Q8IY33-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLI → MFLSSR
     656-904: ARSPSPPRRR...SPKSKSSPSQ → GPPPHPAAGD...PMSLLCLARR

Note: No experimental confirmation available.
Show »
Length:680
Mass (Da):70,848
Checksum:i3996713704E4671D
GO
Isoform 3 (identifier: Q8IY33-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-570: MAAIRALQQW...AKGKSTTLTQ → MALSSWAQGT...LTPRPLASHP

Note: No experimental confirmation available.
Show »
Length:493
Mass (Da):55,298
Checksum:i9C6DB62BD33BF923
GO
Isoform 4 (identifier: Q8IY33-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     571-904: DMSTSLQEGQ...SPKSKSSPSQ → GE

Note: No experimental confirmation available.
Show »
Length:572
Mass (Da):59,484
Checksum:iB4A270575A51A4A4
GO
Isoform 5 (identifier: Q8IY33-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     29-240: Missing.

Note: No experimental confirmation available.
Show »
Length:692
Mass (Da):74,527
Checksum:iC449383F5CD5A47F
GO

Sequence cautioni

The sequence BAB15667.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB84894.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2551L → M in CAD98087 (Ref. 1) Curated
Sequence conflicti285 – 2851S → L in BAB15667 (PubMed:14702039).Curated
Sequence conflicti706 – 7061K → R in BAB15667 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti480 – 4801A → P.
Corresponds to variant rs12540098 [ dbSNP | Ensembl ].
VAR_034071
Natural varianti519 – 5191P → L.
Corresponds to variant rs4075307 [ dbSNP | Ensembl ].
VAR_034072
Natural varianti623 – 6231K → R.
Corresponds to variant rs61287564 [ dbSNP | Ensembl ].
VAR_061356
Natural varianti711 – 7111L → V.
Corresponds to variant rs11980797 [ dbSNP | Ensembl ].
VAR_050159

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 570570MAAIR…TTLTQ → MALSSWAQGTSWAAKGFSRS FSLAEFSLLKPRAGSCRTQE PRKPADGQPWLRCSPCTGGQ RIWVHGAHPATSPPIRQKGK LRPRGRESFPQGHTAQESQL GAPPLTPCPVLLMPPGRLAV GVSEGGVAMGRWQGEAQPPL QTPHSQHSFLTPRPLASHP in isoform 3. 1 PublicationVSP_009856Add
BLAST
Alternative sequencei1 – 4848MAAIR…RPDLI → MFLSSR in isoform 2. 1 PublicationVSP_009854Add
BLAST
Alternative sequencei29 – 240212Missing in isoform 5. 1 PublicationVSP_009858Add
BLAST
Alternative sequencei571 – 904334DMSTS…SSPSQ → GE in isoform 4. 1 PublicationVSP_009857Add
BLAST
Alternative sequencei656 – 904249ARSPS…SSPSQ → GPPPHPAAGDWPSLPASTFV TTGFGRSPLARKPECRAGRR RRRNLTFRANQGDPCPRPMS LLCLARR in isoform 2. 1 PublicationVSP_009855Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL833704 mRNA. Translation: CAD98087.1.
AK027124 mRNA. Translation: BAB15667.1. Different initiation.
AK126808 mRNA. Translation: BAC86702.1.
AK074068 mRNA. Translation: BAB84894.1. Different initiation.
AC102953 Genomic DNA. No translation available.
CH471144 Genomic DNA. Translation: EAW87200.1.
BC037988 mRNA. Translation: AAH37988.1.
BK000467 mRNA. Translation: DAA01346.1.
CCDSiCCDS5324.1. [Q8IY33-1]
RefSeqiNP_891554.1. NM_182924.3. [Q8IY33-1]
UniGeneiHs.376617.
Hs.663699.

Genome annotation databases

EnsembliENST00000297508; ENSP00000297508; ENSG00000164877. [Q8IY33-1]
ENST00000413446; ENSP00000405415; ENSG00000164877. [Q8IY33-2]
GeneIDi79778.
KEGGihsa:79778.
UCSCiuc003skj.5. human. [Q8IY33-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL833704 mRNA. Translation: CAD98087.1.
AK027124 mRNA. Translation: BAB15667.1. Different initiation.
AK126808 mRNA. Translation: BAC86702.1.
AK074068 mRNA. Translation: BAB84894.1. Different initiation.
AC102953 Genomic DNA. No translation available.
CH471144 Genomic DNA. Translation: EAW87200.1.
BC037988 mRNA. Translation: AAH37988.1.
BK000467 mRNA. Translation: DAA01346.1.
CCDSiCCDS5324.1. [Q8IY33-1]
RefSeqiNP_891554.1. NM_182924.3. [Q8IY33-1]
UniGeneiHs.376617.
Hs.663699.

3D structure databases

ProteinModelPortaliQ8IY33.
SMRiQ8IY33. Positions 6-106, 184-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122879. 11 interactions.
IntActiQ8IY33. 10 interactions.
STRINGi9606.ENSP00000297508.

PTM databases

iPTMnetiQ8IY33.
PhosphoSiteiQ8IY33.

Polymorphism and mutation databases

BioMutaiMICALL2.
DMDMi46396456.

Proteomic databases

EPDiQ8IY33.
MaxQBiQ8IY33.
PaxDbiQ8IY33.
PRIDEiQ8IY33.

Protocols and materials databases

DNASUi79778.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297508; ENSP00000297508; ENSG00000164877. [Q8IY33-1]
ENST00000413446; ENSP00000405415; ENSG00000164877. [Q8IY33-2]
GeneIDi79778.
KEGGihsa:79778.
UCSCiuc003skj.5. human. [Q8IY33-1]

Organism-specific databases

CTDi79778.
GeneCardsiMICALL2.
HGNCiHGNC:29672. MICALL2.
HPAiHPA025695.
neXtProtiNX_Q8IY33.
PharmGKBiPA162395928.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKSW. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000290690.
HOVERGENiHBG052476.
InParanoidiQ8IY33.
KOiK19948.
OMAiRDVNICN.
OrthoDBiEOG7JT6VM.
PhylomeDBiQ8IY33.
TreeFamiTF328311.

Miscellaneous databases

ChiTaRSiMICALL2. human.
GenomeRNAii79778.
PROiQ8IY33.

Gene expression databases

BgeeiQ8IY33.
CleanExiHS_MICALL2.
GenevisibleiQ8IY33. HS.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Spleen.
  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 3 AND 5).
    Tissue: Brain cortex and Small intestine.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lymph node.
  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).
    Tissue: Uterus.
  7. "MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion."
    Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.
    Cell 109:887-900(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  8. "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin."
    Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.
    Mol. Biol. Cell 17:2465-2475(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB13.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-649; SER-658 AND SER-660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins."
    Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T., Imoto I., Matsushita N., Sasaki T.
    Genes Cells 18:810-822(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLNA.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-153 AND THR-644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMILK2_HUMAN
AccessioniPrimary (citable) accession number: Q8IY33
Secondary accession number(s): D3YTD2
, Q7RTP4, Q7Z655, Q8TEQ4, Q9H5F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 113 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 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. 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.