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Protein

MICAL-like protein 1

Gene

MICALL1

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

Functioni

Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth.4 Publications

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • phosphatidic acid binding Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to nerve growth factor stimulus Source: Ensembl
  • endocytosis Source: UniProtKB
  • membrane tubulation Source: UniProtKB
  • neuron projection development Source: UniProtKB
  • protein localization to endosome Source: UniProtKB
  • protein targeting to membrane Source: UniProtKB
  • receptor-mediated endocytosis Source: UniProtKB
  • retrograde transport, endosome to plasma membrane Source: UniProtKB
  • slow endocytic recycling Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
MICAL-like protein 1
Alternative name(s):
Molecule interacting with Rab13
Short name:
MIRab13
Gene namesi
Name:MICALL1
Synonyms:KIAA1668, MIRAB13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:29804. MICALL1.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of membrane Source: UniProtKB
  • late endosome Source: UniProtKB
  • late endosome membrane Source: UniProtKB-SubCell
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi385 – 3873PLP → ALA: No effect on interaction with PACSIN2. Loss of interaction with PACSIN2; when associated with 480-A--A-483. 1 Publication
Mutagenesisi425 – 4273NPF → APA: Partial loss of interaction with EHD1. Complete loss of interaction with EHD1; when associated with 633-A--A-635. 1 Publication
Mutagenesisi428 – 4303EEE → AAA: Strongly reduces interaction with EHD1. 1 Publication
Mutagenesisi480 – 4834PRAP → ARAA: No effect on interaction with PACSIN2. Loss of interaction with PACSIN2; when associated with 385-A--A-387. 1 Publication
Mutagenesisi633 – 6353NPF → APA: No effect on interaction with EHD1. Complete loss of interaction with EHD1; when associated with 425-A--A-427. 1 Publication
Mutagenesisi721 – 7266MLVDWF → AAAAAA: Altered association with membranes. 1 Publication

Organism-specific databases

PharmGKBiPA162395891.

Polymorphism and mutation databases

BioMutaiMICALL1.
DMDMi30173085.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 863863MICAL-like protein 1PRO_0000075848Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei309 – 3091PhosphoserineCombined sources
Modified residuei318 – 3181PhosphothreonineCombined sources
Modified residuei391 – 3911PhosphoserineCombined sources
Modified residuei467 – 4671PhosphothreonineCombined sources
Modified residuei469 – 4691PhosphothreonineCombined sources
Modified residuei470 – 4701PhosphoserineCombined sources
Modified residuei471 – 4711PhosphoserineCombined sources
Modified residuei484 – 4841PhosphoserineCombined sources
Modified residuei486 – 4861PhosphoserineCombined sources
Modified residuei578 – 5781PhosphoserineCombined sources
Modified residuei621 – 6211PhosphoserineCombined sources
Modified residuei740 – 7401PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N3F8.
MaxQBiQ8N3F8.
PaxDbiQ8N3F8.
PeptideAtlasiQ8N3F8.
PRIDEiQ8N3F8.

PTM databases

iPTMnetiQ8N3F8.
PhosphoSiteiQ8N3F8.

Expressioni

Gene expression databases

BgeeiQ8N3F8.
CleanExiHS_MICALL1.
ExpressionAtlasiQ8N3F8. baseline and differential.
GenevisibleiQ8N3F8. HS.

Organism-specific databases

HPAiHPA043480.

Interactioni

Subunit structurei

Homooligomer (Probable). Interacts (via NPF1 motif) with EHD1 (via EH domain); the interaction is direct and probably recruits EHD1 to membranes. Interacts with EHD3 (via EH domain). Interacts with RAB35 (GTP-bound form); the interaction is direct and probably recruits MICALL1 to membranes. Interacts with ACAP2; the interaction is indirect through RAB35. Interacts with RAB8A (GTP-bound form); regulates RAB8A association with recycling endosomes. Interacts with RAB13 (GTP-bound form). Interacts with ARF6 (GTP-bound form). Interacts with PACSIN2 (via the SH3 domain). Interacts with DPYSL2.Curated6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DPYSL2O026752EBI-1056885,EBI-8783505From a different organism.
RAB35Q152862EBI-1056885,EBI-722275

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi124504. 19 interactions.
IntActiQ8N3F8. 15 interactions.
MINTiMINT-1631011.
STRINGi9606.ENSP00000215957.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KSPNMR-B419-433[»]
ProteinModelPortaliQ8N3F8.
SMRiQ8N3F8. Positions 8-111, 143-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N3F8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 105104CHPROSITE-ProRule annotationAdd
BLAST
Domaini162 – 22564LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni652 – 863212RAB-binding domain (RBD); mediates the interaction with RAB13 and RAB35 and intramolecular interaction with the CH domainAdd
BLAST
Regioni700 – 863164Necessary and sufficient to associate with tubular recycling endosome membranes, mediate phosphatidic acid-binding and membrane tubulationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili682 – 71130Sequence analysisAdd
BLAST
Coiled coili785 – 83046Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi425 – 4273NPF1
Motifi633 – 6353NPF2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi253 – 667415Pro-richAdd
BLAST

Domaini

Probably exists in a closed and an opened conformation due to interaction of the C-terminal RAB-binding domain (RBD) with the N-terminal CH (calponin-homology) domain. The conformational change is regulated by RAB13 and may modulate MICALL1 interactions with functional partners.1 Publication

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

eggNOGiENOG410IG9K. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOVERGENiHBG052475.
InParanoidiQ8N3F8.
KOiK19948.
OMAiEGYRGVD.
OrthoDBiEOG7X3QR0.
PhylomeDBiQ8N3F8.
TreeFamiTF328311.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR028563. MICAL-L1.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR11915:SF323. PTHR11915:SF323. 2 hits.
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]

Sequencei

Sequence statusi: Complete.

Q8N3F8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPRGALLA WCRRQCEGYR GVEIRDLSSS FRDGLAFCAI LHRHRPDLLD
60 70 80 90 100
FDSLSKDNVF ENNRLAFEVA EKELGIPALL DPNDMVSMSV PDCLSIMTYV
110 120 130 140 150
SQYYNHFCSP GQAGVSPPRK GLAPCSPPSV APTPVEPEDV AQGEELSSGS
160 170 180 190 200
LSEQGTGQTP SSTCAACQQH VHLVQRYLAD GRLYHRHCFR CRRCSSTLLP
210 220 230 240 250
GAYENGPEEG TFVCAEHCAR LGPGTRSGTR PGPFSQPKQQ HQQQLAEDAK
260 270 280 290 300
DVPGGGPSSS APAGAEADGP KASPEARPQI PTKPRVPGKL QELASPPAGR
310 320 330 340 350
PTPAPRKASE STTPAPPTPR PRSSLQQENL VEQAGSSSLV NGRLHELPVP
360 370 380 390 400
KPRGTPKPSE GTPAPRKDPP WITLVQAEPK KKPAPLPPSS SPGPPSQDSR
410 420 430 440 450
QVENGGTEEV AQPSPTASLE SKPYNPFEEE EEDKEEEAPA APSLATSPAL
460 470 480 490 500
GHPESTPKSL HPWYGITPTS SPKTKKRPAP RAPSASPLAL HASRLSHSEP
510 520 530 540 550
PSATPSPALS VESLSSESAS QTAGAELLEP PAVPKSSSEP AVHAPGTPGN
560 570 580 590 600
PVSLSTNSSL ASSGELVEPR VEQMPQASPG LAPRTRGSSG PQPAKPCSGA
610 620 630 640 650
TPTPLLLVGD RSPVPSPGSS SPQLQVKSSC KENPFNRKPS PAASPATKKA
660 670 680 690 700
TKGSKPVRPP APGHGFPLIK RKVQADQYIP EEDIHGEMDT IERRLDALEH
710 720 730 740 750
RGVLLEEKLR GGLNEGREDD MLVDWFKLIH EKHLLVRRES ELIYVFKQQN
760 770 780 790 800
LEQRQADVEY ELRCLLNKPE KDWTEEDRAR EKVLMQELVT LIEQRNAIIN
810 820 830 840 850
CLDEDRQREE EEDKMLEAMI KKKEFQREAE PEGKKKGKFK TMKMLKLLGN
860
KRDAKSKSPR DKS
Length:863
Mass (Da):93,441
Last modified:April 23, 2003 - v2
Checksum:i755E3B57C6037292
GO

Sequence cautioni

The sequence CAD39036.1 differs from that shown. Reason: Frameshift at positions 486 and 507. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371P → S in BAB33338 (PubMed:11258795).Curated
Sequence conflicti212 – 2121F → Y in CAD39036 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti519 – 5191A → S.1 Publication
Corresponds to variant rs9610875 [ dbSNP | Ensembl ].
VAR_018262
Natural varianti583 – 5831P → L.
Corresponds to variant rs2272829 [ dbSNP | Ensembl ].
VAR_020258
Natural varianti685 – 6851H → R.
Corresponds to variant rs34834842 [ dbSNP | Ensembl ].
VAR_050158
Natural varianti817 – 8171E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_036192

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ496196 mRNA. Translation: CAD42713.1.
CR456437 mRNA. Translation: CAG30323.1.
AL022311 Genomic DNA. Translation: CAI18864.1.
AL834373 mRNA. Translation: CAD39036.1. Frameshift.
AL833860 mRNA. Translation: CAD38718.1.
AB051455 mRNA. Translation: BAB33338.1.
BC001090 mRNA. Translation: AAH01090.2.
BK000466 mRNA. Translation: DAA01345.1.
CCDSiCCDS13961.1.
RefSeqiNP_203744.1. NM_033386.3.
UniGeneiHs.517610.

Genome annotation databases

EnsembliENST00000215957; ENSP00000215957; ENSG00000100139.
GeneIDi85377.
KEGGihsa:85377.
UCSCiuc003aui.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ496196 mRNA. Translation: CAD42713.1.
CR456437 mRNA. Translation: CAG30323.1.
AL022311 Genomic DNA. Translation: CAI18864.1.
AL834373 mRNA. Translation: CAD39036.1. Frameshift.
AL833860 mRNA. Translation: CAD38718.1.
AB051455 mRNA. Translation: BAB33338.1.
BC001090 mRNA. Translation: AAH01090.2.
BK000466 mRNA. Translation: DAA01345.1.
CCDSiCCDS13961.1.
RefSeqiNP_203744.1. NM_033386.3.
UniGeneiHs.517610.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KSPNMR-B419-433[»]
ProteinModelPortaliQ8N3F8.
SMRiQ8N3F8. Positions 8-111, 143-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124504. 19 interactions.
IntActiQ8N3F8. 15 interactions.
MINTiMINT-1631011.
STRINGi9606.ENSP00000215957.

PTM databases

iPTMnetiQ8N3F8.
PhosphoSiteiQ8N3F8.

Polymorphism and mutation databases

BioMutaiMICALL1.
DMDMi30173085.

Proteomic databases

EPDiQ8N3F8.
MaxQBiQ8N3F8.
PaxDbiQ8N3F8.
PeptideAtlasiQ8N3F8.
PRIDEiQ8N3F8.

Protocols and materials databases

DNASUi85377.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215957; ENSP00000215957; ENSG00000100139.
GeneIDi85377.
KEGGihsa:85377.
UCSCiuc003aui.4. human.

Organism-specific databases

CTDi85377.
GeneCardsiMICALL1.
HGNCiHGNC:29804. MICALL1.
HPAiHPA043480.
neXtProtiNX_Q8N3F8.
PharmGKBiPA162395891.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG9K. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOVERGENiHBG052475.
InParanoidiQ8N3F8.
KOiK19948.
OMAiEGYRGVD.
OrthoDBiEOG7X3QR0.
PhylomeDBiQ8N3F8.
TreeFamiTF328311.

Miscellaneous databases

ChiTaRSiMICALL1. human.
EvolutionaryTraceiQ8N3F8.
GeneWikiiMICALL1.
GenomeRNAii85377.
PROiQ8N3F8.

Gene expression databases

BgeeiQ8N3F8.
CleanExiHS_MICALL1.
ExpressionAtlasiQ8N3F8. baseline and differential.
GenevisibleiQ8N3F8. HS.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR028563. MICAL-L1.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR11915:SF323. PTHR11915:SF323. 2 hits.
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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN ENDOCYTOSIS, INTERACTION WITH RAB13, SUBCELLULAR LOCATION, DOMAIN.
    Tissue: Uterine adenocarcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-863, VARIANT SER-519.
    Tissue: Melanoma.
  5. "Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping."
    Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.
    DNA Res. 8:1-9(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-863.
    Tissue: Brain.
  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] OF 514-863.
    Tissue: Choriocarcinoma.
  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: GENE STRUCTURE.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-309; THR-318; THR-467; SER-471; SER-484 AND SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling."
    Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.
    Mol. Biol. Cell 20:5181-5194(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOCYTIC RECYCLING, INTERACTION WITH EHD1; EHD3 AND RAB8A, SUBCELLULAR LOCATION, MUTAGENESIS OF 425-ASN--PHE-427; 633-ASN--PHE-635 AND 721-MET--PHE-726.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Collapsin response mediator protein-2 (Crmp2) regulates trafficking by linking endocytic regulatory proteins to dynein motors."
    Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.
    J. Biol. Chem. 285:31918-31922(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOCYTOSIS, INTERACTION WITH DPYSL2.
  13. "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 THR-467; THR-469; SER-470; SER-471; SER-484; SER-486 AND SER-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a."
    Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.
    Traffic 13:82-93(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARF6 AND RAB35, SUBCELLULAR LOCATION.
  16. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-391; THR-467; SER-471; SER-484; SER-486; SER-578 AND SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  17. "Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis."
    Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.
    Mol. Biol. Cell 24:1776-1790(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEMBRANE TUBULATION, LIPID-BINDING, HOMOOLIGOMERIZATION, INTERACTION WITH EHD1 AND PACSIN2, MUTAGENESIS OF 385-PRO--PRO-387 AND 480-PRO--PRO-483.
  18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Mechanism for the selective interaction of C-terminal Eps15 homology domain proteins with specific Asn-Pro-Phe-containing partners."
    Kieken F., Sharma M., Jovic M., Giridharan S.S., Naslavsky N., Caplan S., Sorgen P.L.
    J. Biol. Chem. 285:8687-8694(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 419-433 IN COMPLEX WITH EHD1, MUTAGENESIS OF 428-GLU--GLU-430.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-817.

Entry informationi

Entry nameiMILK1_HUMAN
AccessioniPrimary (citable) accession number: Q8N3F8
Secondary accession number(s): Q5TI16
, Q7RTP5, Q8N3N8, Q9BVL9, Q9BY92, Q9UH43, Q9UH44, Q9UH45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: July 6, 2016
This is version 132 of the entry and version 2 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 22
    Human chromosome 22: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.